{"entity": "researcher", "timestamp": "2026-08-20T20:50:10.028Z", "family": "Cava", "given": "Felipe", "initials": "F", "orcid": "0000-0001-5995-718X", "affiliations": ["Department of Molecular Biology and Laboratory for Molecular Infection Medicine Sweden, Ume\u00e5 Centre for Microbial Research, SciLifeLab, Ume\u00e5 University, Ume\u00e5, Sweden. felipe.cava@umu.se."], "links": {"self": {"href": "https://publications-affiliated.scilifelab.se/researcher/bbcff12a06814d54afea533e125a1213.json"}, "display": {"href": "https://publications-affiliated.scilifelab.se/researcher/bbcff12a06814d54afea533e125a1213"}}, "publications": [{"entity": "publication", "iuid": "38cc5d17dc2b401ab546340eb022d747", "links": {"self": {"href": "https://publications-affiliated.scilifelab.se/publication/38cc5d17dc2b401ab546340eb022d747.json"}, "display": {"href": "https://publications-affiliated.scilifelab.se/publication/38cc5d17dc2b401ab546340eb022d747"}}, "title": "A novel mechanism for bacterial sporulation based on programmed peptidoglycan degradation", "authors": [{"family": "Ram\u00edrez Carb\u00f3", "given": "Carlos A", "initials": "CA"}, {"family": "Irazoki", "given": "Oihane", "initials": "O"}, {"family": "Venkatesan", "given": "Srutha", "initials": "S"}, {"family": "Chen", "given": "Lauren JS", "initials": "LJ"}, {"family": "Morales", "given": "Haylie A", "initials": "HA"}, {"family": "Garcia Avila", "given": "Assariel J", "initials": "AJ"}, {"family": "Cheung", "given": "Hoi Ling", "initials": "HL"}, {"family": "Cava", "given": "Felipe", "initials": "F", "orcid": "0000-0001-5995-718X", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/bbcff12a06814d54afea533e125a1213.json"}}, {"family": "Nan", "given": "Beiyan", "initials": "B", "orcid": "0000-0002-0326-9529", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/f3f841f4ad1c4558ae0c5ccdbf07c53c.json"}}], "type": "posted-content", "published": "2025-08-28", "journal": {"issn-l": null}, "abstract": null, "doi": "10.7554/elife.108250", "pmid": null, "labels": [], "xrefs": [], "notes": [], "created": "2026-08-20T13:51:31.390Z", "modified": "2026-08-20T13:51:31.460Z"}, {"entity": "publication", "iuid": "ecce52a348e94a939279418dcea6d0c5", "links": {"self": {"href": "https://publications-affiliated.scilifelab.se/publication/ecce52a348e94a939279418dcea6d0c5.json"}, "display": {"href": "https://publications-affiliated.scilifelab.se/publication/ecce52a348e94a939279418dcea6d0c5"}}, "title": "A novel mechanism for bacterial sporulation based on programmed peptidoglycan degradation", "authors": [{"family": "Ram\u00edrez Carb\u00f3", "given": "Carlos A", "initials": "CA"}, {"family": "Irazoki", "given": "Oihane", "initials": "O"}, {"family": "Venkatesan", "given": "Srutha", "initials": "S"}, {"family": "Chen", "given": "Lauren JS", "initials": "LJ"}, {"family": "Morales", "given": "Haylie A", "initials": "HA"}, {"family": "Garcia Avila", "given": "Assariel J", "initials": "AJ"}, {"family": "Cheung", "given": "Hoi Ling", "initials": "HL"}, {"family": "Cava", "given": "Felipe", "initials": "F", "orcid": "0000-0001-5995-718X", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/bbcff12a06814d54afea533e125a1213.json"}}, {"family": "Nan", "given": "Beiyan", "initials": "B", "orcid": "0000-0002-0326-9529", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/f3f841f4ad1c4558ae0c5ccdbf07c53c.json"}}], "type": "posted-content", "published": "2025-08-28", "journal": {"issn-l": null}, "abstract": null, "doi": "10.7554/elife.108250.1", "pmid": null, "labels": [], "xrefs": [], "notes": [], "created": "2026-08-20T13:51:41.835Z", "modified": "2026-08-20T13:51:41.855Z"}, {"entity": "publication", "iuid": "6ba415badb784b04adabe6ede02e693c", "links": {"self": {"href": "https://publications-affiliated.scilifelab.se/publication/6ba415badb784b04adabe6ede02e693c.json"}, "display": {"href": "https://publications-affiliated.scilifelab.se/publication/6ba415badb784b04adabe6ede02e693c"}}, "title": "A novel mechanism for bacterial sporulation based on programmed peptidoglycan degradation.", "authors": [{"family": "Ram\u00edrez Carb\u00f3", "given": "Carlos A", "initials": "CA"}, {"family": "Irazoki", "given": "Oihane", "initials": "O"}, {"family": "Venkatesan", "given": "Srutha", "initials": "S"}, {"family": "Chen", "given": "Lauren J S", "initials": "LJS"}, {"family": "Morales", "given": "Haylie A", "initials": "HA"}, {"family": "Garcia Avila", "given": "Assariel J", "initials": "AJ"}, {"family": "Cheung", "given": "Hoi-Ling", "initials": "HL"}, {"family": "Cava", "given": "Felipe", "initials": "F", "orcid": "0000-0001-5995-718X", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/bbcff12a06814d54afea533e125a1213.json"}}, {"family": "Nan", "given": "Beiyan", "initials": "B", "orcid": "0000-0002-0326-9529", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/f3f841f4ad1c4558ae0c5ccdbf07c53c.json"}}], "type": "journal article", "published": "2025-06-26", "journal": {"title": "bioRxiv", "issn": "2692-8205", "issn-l": null}, "abstract": "Many bacteria form spores to endure unfavorable conditions. While Firmicutes generate endospores through cell division, sporulation in non-Firmicutes remains less understood. The Gram-negative bacterium Myxococcus xanthus undergoes sporulation through two distinct mechanisms: rapid sporulation triggered by chemical induction and slow sporulation driven by starvation, both occurring independently of cell division. Instead, these processes depend on the complete degradation of the peptidoglycan (PG) cell wall by lytic transglycosylases (LTGs), with both LtgA and LtgB supporting rapid sporulation and LtgB alone driving slow sporulation. Remarkably, LtgB programs the pace of PG degradation by LtgA during rapid sporulation, ensuring a controlled process that prevents abrupt PG breakdown and the formation of non-resistant pseudospores. In addition to regulation between LTGs, PG degradation is also influenced by its synthesis; cells exhibiting increased muropeptide production often circumvent sporulation. These findings not only reveal novel mechanisms of bacterial sporulation but also shed light on the regulatory network governing PG dynamics.", "doi": "10.1101/2025.06.26.661752", "pmid": "40672182", "labels": [], "xrefs": [{"db": "pmc", "key": "PMC12265050"}, {"db": "pii", "key": "2025.06.26.661752"}], "notes": [], "created": "2026-08-20T11:06:18.981Z", "modified": "2026-08-20T11:06:19.072Z"}, {"entity": "publication", "iuid": "ebdcfc0ede674ee9b8f98c185eaf36aa", "links": {"self": {"href": "https://publications-affiliated.scilifelab.se/publication/ebdcfc0ede674ee9b8f98c185eaf36aa.json"}, "display": {"href": "https://publications-affiliated.scilifelab.se/publication/ebdcfc0ede674ee9b8f98c185eaf36aa"}}, "title": "Disruption of undecaprenyl phosphate recycling suppresses ampC beta-lactamase induction in Pseudomonas aeruginosa", "authors": [{"family": "Klycheva", "given": "Karina", "initials": "K"}, {"family": "Gyger", "given": "Jo\u00ebl", "initials": "J"}, {"family": "Frund", "given": "M\u00e9lissa", "initials": "M"}, {"family": "Torrens", "given": "Gabriel", "initials": "G"}, {"family": "Cava", "given": "Felipe", "initials": "F", "orcid": "0000-0001-5995-718X", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/bbcff12a06814d54afea533e125a1213.json"}}, {"family": "Fumeaux", "given": "Coralie", "initials": "C", "orcid": "0000-0002-6969-3111", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/34711f3602884fd690fdb859dae1cc8e.json"}}], "type": "posted-content", "published": "2025-06-05", "journal": {"issn-l": null}, "abstract": null, "doi": "10.1101/2025.06.03.657773", "pmid": null, "labels": [], "xrefs": [], "notes": [], "created": "2026-08-20T11:06:00.899Z", "modified": "2026-08-20T11:06:00.951Z"}, {"entity": "publication", "iuid": "ebd5d84b1ad249708b9e993a4c55fd26", "links": {"self": {"href": "https://publications-affiliated.scilifelab.se/publication/ebd5d84b1ad249708b9e993a4c55fd26.json"}, "display": {"href": "https://publications-affiliated.scilifelab.se/publication/ebd5d84b1ad249708b9e993a4c55fd26"}}, "title": "Evolutionary rescue of spherical mreB deletion mutants of the rod-shape bacterium Pseudomonas fluorescens SBW25", "authors": [{"family": "Yulo", "given": "Paul Richard J", "initials": "PRJ", "orcid": "0009-0008-2288-0711", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/e9a9ec12f9544be1b6d7d0619ce84a7e.json"}}, {"family": "Desprat", "given": "Nicolas", "initials": "N", "orcid": "0000-0002-5016-9360", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/391c6fe36720427184c3e3a67499a593.json"}}, {"family": "Gerth", "given": "Monica L", "initials": "ML"}, {"family": "Ritzl-Rinkenberger", "given": "Barbara", "initials": "B"}, {"family": "Farr", "given": "Andrew D", "initials": "AD"}, {"family": "Liu", "given": "Yunhao", "initials": "Y"}, {"family": "Zhang", "given": "Xue Xian", "initials": "XX"}, {"family": "Miller", "given": "Michael", "initials": "M"}, {"family": "Cava", "given": "Felipe", "initials": "F", "orcid": "0000-0001-5995-718X", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/bbcff12a06814d54afea533e125a1213.json"}}, {"family": "Rainey", "given": "Paul B", "initials": "PB", "orcid": "0000-0003-0879-5795", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/54e6f301a7a848f2aac5230a583e7de8.json"}}, {"family": "Hendrickson", "given": "Heather L", "initials": "HL", "orcid": "0000-0003-3471-4397", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/04d5b11678894b9992f668ad678c5b60.json"}}], "type": "journal-article", "published": "2025-03-31", "journal": {"issn": "2050-084X", "volume": "13", "title": "Elife", "issn-l": "2050-084X"}, "abstract": null, "doi": "10.7554/elife.98218.4", "pmid": null, "labels": [], "xrefs": [], "notes": [], "created": "2026-08-20T13:56:38.045Z", "modified": "2026-08-20T13:56:38.128Z"}, {"entity": "publication", "iuid": "effb37a1c03c41f281fc11b63232021f", "links": {"self": {"href": "https://publications-affiliated.scilifelab.se/publication/effb37a1c03c41f281fc11b63232021f.json"}, "display": {"href": "https://publications-affiliated.scilifelab.se/publication/effb37a1c03c41f281fc11b63232021f"}}, "title": "Evolutionary rescue of spherical mreB deletion mutants of the rod-shape bacterium Pseudomonas fluorescens SBW25.", "authors": [{"family": "Yulo", "given": "Paul Richard J", "initials": "PRJ", "orcid": "0009-0008-2288-0711", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/e9a9ec12f9544be1b6d7d0619ce84a7e.json"}}, {"family": "Desprat", "given": "Nicolas", "initials": "N", "orcid": "0000-0002-5016-9360", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/391c6fe36720427184c3e3a67499a593.json"}}, {"family": "Gerth", "given": "Monica L", "initials": "ML"}, {"family": "Ritzl-Rinkenberger", "given": "Barbara", "initials": "B"}, {"family": "Farr", "given": "Andrew D", "initials": "AD"}, {"family": "Liu", "given": "Yunhao", "initials": "Y"}, {"family": "Zhang", "given": "Xue-Xian", "initials": "XX"}, {"family": "Miller", "given": "Michael", "initials": "M"}, {"family": "Cava", "given": "Felipe", "initials": "F", "orcid": "0000-0001-5995-718X", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/bbcff12a06814d54afea533e125a1213.json"}}, {"family": "Rainey", "given": "Paul B", "initials": "PB", "orcid": "0000-0003-0879-5795", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/54e6f301a7a848f2aac5230a583e7de8.json"}}, {"family": "Hendrickson", "given": "Heather L", "initials": "HL", "orcid": "0000-0003-3471-4397", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/04d5b11678894b9992f668ad678c5b60.json"}}], "type": "journal article", "published": "2025-03-31", "journal": {"title": "Elife", "issn": "2050-084X", "volume": "13", "issn-l": "2050-084X"}, "abstract": "Maintenance of rod-shape in bacterial cells depends on the actin-like protein MreB. Deletion of mreB from Pseudomonas fluorescens SBW25 results in viable spherical cells of variable volume and reduced fitness. Using a combination of time-resolved microscopy and biochemical assay of peptidoglycan synthesis, we show that reduced fitness is a consequence of perturbed cell size homeostasis that arises primarily from differential growth of daughter cells. A 1000-generation selection experiment resulted in rapid restoration of fitness with derived cells retaining spherical shape. Mutations in the peptidoglycan synthesis protein Pbp1A were identified as the main route for evolutionary rescue with genetic reconstructions demonstrating causality. Compensatory pbp1A mutations that targeted transpeptidase activity enhanced homogeneity of cell wall synthesis on lateral surfaces and restored cell size homeostasis. Mechanistic explanations require enhanced understanding of why deletion of mreB causes heterogeneity in cell wall synthesis. We conclude by presenting two testable hypotheses, one of which posits that heterogeneity stems from non-functional cell wall synthesis machinery, while the second posits that the machinery is functional, albeit stalled. Overall, our data provide support for the second hypothesis and draw attention to the importance of balance between transpeptidase and glycosyltransferase functions of peptidoglycan building enzymes for cell shape determination.", "doi": "10.7554/eLife.98218", "pmid": "40163529", "labels": [], "xrefs": [{"db": "pmc", "key": "PMC11957537"}, {"db": "pii", "key": "98218"}], "notes": [], "created": "2026-08-20T13:56:30.018Z", "modified": "2026-08-20T13:56:30.245Z"}, {"entity": "publication", "iuid": "30b8eec8f8984554af52498bf2bd3aa3", "links": {"self": {"href": "https://publications-affiliated.scilifelab.se/publication/30b8eec8f8984554af52498bf2bd3aa3.json"}, "display": {"href": "https://publications-affiliated.scilifelab.se/publication/30b8eec8f8984554af52498bf2bd3aa3"}}, "title": "Evolutionary rescue of spherical mreB deletion mutants of the rod-shape bacterium Pseudomonas fluorescens SBW25", "authors": [{"family": "Yulo", "given": "P Richard J", "initials": "PRJ", "orcid": "0009-0008-2288-0711", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/e9a9ec12f9544be1b6d7d0619ce84a7e.json"}}, {"family": "Desprat", "given": "Nicolas", "initials": "N", "orcid": "0000-0002-5016-9360", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/391c6fe36720427184c3e3a67499a593.json"}}, {"family": "Gerth", "given": "Monica L", "initials": "ML", "orcid": "0000-0002-7959-7852", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/9c7e73febc234a15bfb1539af2321bdd.json"}}, {"family": "Ritzl- Rinkenberger", "given": "Barbara", "initials": "B"}, {"family": "Farr", "given": "Andrew D", "initials": "AD", "orcid": "0000-0002-3402-1665", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/8aeb2de20ef94a2799a14ff1eac049dd.json"}}, {"family": "Liu", "given": "Yunhao", "initials": "Y", "orcid": "0000-0002-0279-1307", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/19280708461440438e5f0b0497be5381.json"}}, {"family": "Zhang", "given": "Xue Xian", "initials": "XX", "orcid": "0000-0002-6536-3529", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/744837cd120040d980a9a389d513be3d.json"}}, {"family": "Miller", "given": "Michael", "initials": "M", "orcid": "0000-0002-1723-7958", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/76923e46e3384123bd3bc451a47a6eb7.json"}}, {"family": "Cava", "given": "Felipe", "initials": "F", "orcid": "0000-0001-5995-718X", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/bbcff12a06814d54afea533e125a1213.json"}}, {"family": "Rainey", "given": "Paul B", "initials": "PB", "orcid": "0000-0003-0879-5795", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/54e6f301a7a848f2aac5230a583e7de8.json"}}, {"family": "Hendrickson", "given": "Heather L", "initials": "HL", "orcid": "0000-0003-3471-4397", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/04d5b11678894b9992f668ad678c5b60.json"}}], "type": "posted-content", "published": "2025-02-18", "journal": {"issn-l": null}, "abstract": null, "doi": "10.7554/elife.98218.3", "pmid": null, "labels": [], "xrefs": [], "notes": [], "created": "2026-08-20T13:56:36.264Z", "modified": "2026-08-20T13:56:36.333Z"}, {"entity": "publication", "iuid": "53101f330a714f06af752ec675973649", "links": {"self": {"href": "https://publications-affiliated.scilifelab.se/publication/53101f330a714f06af752ec675973649.json"}, "display": {"href": "https://publications-affiliated.scilifelab.se/publication/53101f330a714f06af752ec675973649"}}, "title": "Maintenance of cell wall remodeling and vesicle production are connected in Mycobacterium tuberculosis.", "authors": [{"family": "Salgueiro-Toledo", "given": "Vivian C", "initials": "VC"}, {"family": "Bertol", "given": "Jorge", "initials": "J"}, {"family": "Gutierrez", "given": "Claude", "initials": "C", "orcid": "0000-0003-1777-0223", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/243d0f81388e4fb4bbf4655d54488f18.json"}}, {"family": "Serrano-Mestre", "given": "Jose L", "initials": "JL"}, {"family": "Ferrer-Luzon", "given": "Noelia", "initials": "N"}, {"family": "V\u00e1zquez-Iniesta", "given": "Lucia", "initials": "L"}, {"family": "Palacios", "given": "Ainhoa", "initials": "A"}, {"family": "Pasquina-Lemonche", "given": "Laia", "initials": "L"}, {"family": "Espaillat", "given": "Akbar", "initials": "A"}, {"family": "Lerma", "given": "Laura", "initials": "L"}, {"family": "Weinrick", "given": "Brian", "initials": "B", "orcid": "0000-0003-0880-4487", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/a16666554f444c0badeaa557985f2951.json"}}, {"family": "Lavin", "given": "Jose L", "initials": "JL"}, {"family": "Elortza", "given": "Felix", "initials": "F"}, {"family": "Azkargorta", "given": "Mikel", "initials": "M", "orcid": "0000-0001-9115-3202", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/873751c330dc4b9190c0508ac3706a0b.json"}}, {"family": "Prieto", "given": "Alicia", "initials": "A"}, {"family": "Buend\u00eda-Nacarino", "given": "Pilar", "initials": "P"}, {"family": "Luque-Garc\u00eda", "given": "Jose L", "initials": "JL", "orcid": "0000-0001-6273-0349", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/d5eaf77dcf004fd382998b6c1f34b81a.json"}}, {"family": "Neyrolles", "given": "Olivier", "initials": "O"}, {"family": "Cava", "given": "Felipe", "initials": "F", "orcid": "0000-0001-5995-718X", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/bbcff12a06814d54afea533e125a1213.json"}}, {"family": "Hobbs", "given": "Jamie K", "initials": "JK"}, {"family": "Sanz", "given": "Joaqu\u00edn", "initials": "J", "orcid": "0000-0002-2980-9685", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/0c67346934084624acaa036146732774.json"}}, {"family": "Prados-Rosales", "given": "Rafael", "initials": "R", "orcid": "0000-0001-5964-0166", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/d28b08c987cd4b40869b88ff498f6b97.json"}}], "type": "journal article", "published": "2025-02-17", "journal": {"title": "Elife", "issn": "2050-084X", "volume": "13", "issn-l": "2050-084X"}, "abstract": "Pathogenic and nonpathogenic mycobacteria secrete extracellular vesicles (EVs) under various conditions. EVs produced by Mycobacterium tuberculosis (Mtb) have raised significant interest for their potential in cell communication, nutrient acquisition, and immune evasion. However, the relevance of vesicle secretion during tuberculosis infection remains unknown due to the limited understanding of mycobacterial vesicle biogenesis. We have previously shown that a transposon mutant in the LCP-related gene virR (virR) manifested a strong attenuated phenotype during experimental macrophage and murine infections, concomitant to enhanced vesicle release. In this study, we aimed to understand the role of VirR in the vesicle production process in mutMtb. We employ genetic, transcriptional, proteomics, ultrastructural, and biochemical methods to investigate the underlying processes explaining the enhanced vesiculogenesis phenomenon observed in the virR. Our results establish that VirR is critical to sustain proper cell permeability via regulation of cell envelope remodeling possibly through the interaction with similar cell envelope proteins, which control the link between peptidoglycan and arabinogalactan. These findings advance our understanding of mycobacterial extracellular vesicle biogenesis and suggest that these set of proteins could be attractive targets for therapeutic intervention.mut", "doi": "10.7554/eLife.94982", "pmid": "39960848", "labels": [], "xrefs": [{"db": "pmc", "key": "PMC11832169"}, {"db": "pii", "key": "94982"}, {"db": "GEO", "key": "GSE143996"}, {"db": "GEO", "key": "GSE175812"}], "notes": [], "created": "2026-08-20T13:56:03.371Z", "modified": "2026-08-20T13:56:03.646Z"}, {"entity": "publication", "iuid": "af800a5ed9ef4beda0c151ef3c8846b7", "links": {"self": {"href": "https://publications-affiliated.scilifelab.se/publication/af800a5ed9ef4beda0c151ef3c8846b7.json"}, "display": {"href": "https://publications-affiliated.scilifelab.se/publication/af800a5ed9ef4beda0c151ef3c8846b7"}}, "title": "Maintenance of cell wall remodeling and vesicle production are connected in Mycobacterium tuberculosis", "authors": [{"family": "Salgueiro-Toledo", "given": "Vivian C", "initials": "VC"}, {"family": "Bertol", "given": "Jorge", "initials": "J"}, {"family": "Gutierrez", "given": "Claude", "initials": "C", "orcid": "0000-0003-1777-0223", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/243d0f81388e4fb4bbf4655d54488f18.json"}}, {"family": "Serrano-Mestre", "given": "Jose L", "initials": "JL"}, {"family": "Ferrer-Luzon", "given": "Noelia", "initials": "N"}, {"family": "V\u00e1zquez-Iniesta", "given": "Lucia", "initials": "L"}, {"family": "Palacios", "given": "Ainhoa", "initials": "A"}, {"family": "Pasquina-Lemonche", "given": "Laia", "initials": "L"}, {"family": "Espaillat", "given": "Akbar", "initials": "A"}, {"family": "Lerma", "given": "Laura", "initials": "L"}, {"family": "Weinrick", "given": "Brian", "initials": "B", "orcid": "0000-0003-0880-4487", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/a16666554f444c0badeaa557985f2951.json"}}, {"family": "Lavin", "given": "Jose L", "initials": "JL"}, {"family": "Elortza", "given": "Felix", "initials": "F"}, {"family": "Azkargorta", "given": "Mikel", "initials": "M", "orcid": "0000-0001-9115-3202", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/873751c330dc4b9190c0508ac3706a0b.json"}}, {"family": "Prieto", "given": "Alicia", "initials": "A"}, {"family": "Buend\u00eda-Nacarino", "given": "Pilar", "initials": "P"}, {"family": "Luque-Garc\u00eda", "given": "Jose L", "initials": "JL", "orcid": "0000-0001-6273-0349", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/d5eaf77dcf004fd382998b6c1f34b81a.json"}}, {"family": "Neyrolles", "given": "Olivier", "initials": "O"}, {"family": "Cava", "given": "Felipe", "initials": "F", "orcid": "0000-0001-5995-718X", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/bbcff12a06814d54afea533e125a1213.json"}}, {"family": "Hobbs", "given": "Jamie K", "initials": "JK"}, {"family": "Sanz", "given": "Joaqu\u00edn", "initials": "J", "orcid": "0000-0002-2980-9685", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/0c67346934084624acaa036146732774.json"}}, {"family": "Prados-Rosales", "given": "Rafael", "initials": "R", "orcid": "0000-0001-5964-0166", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/d28b08c987cd4b40869b88ff498f6b97.json"}}], "type": "journal-article", "published": "2025-02-17", "journal": {"issn": "2050-084X", "volume": "13", "title": "Elife", "issn-l": "2050-084X"}, "abstract": null, "doi": "10.7554/elife.94982.4", "pmid": null, "labels": [], "xrefs": [], "notes": [], "created": "2026-08-20T13:56:14.994Z", "modified": "2026-08-20T13:56:15.096Z"}, {"entity": "publication", "iuid": "86351291346f4af1a067544f06548a7b", "links": {"self": {"href": "https://publications-affiliated.scilifelab.se/publication/86351291346f4af1a067544f06548a7b.json"}, "display": {"href": "https://publications-affiliated.scilifelab.se/publication/86351291346f4af1a067544f06548a7b"}}, "title": "Bacteria use exogenous peptidoglycan as a danger signal to trigger biofilm formation.", "authors": [{"family": "Vaidya", "given": "Sanika", "initials": "S", "orcid": "0000-0001-6877-617X", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/a8f5afa582f24618ab9203cc6e914c5c.json"}}, {"family": "Saha", "given": "Dibya", "initials": "D", "orcid": "0000-0002-9891-2926", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/680f66681c8d418dafa52be54b3f7880.json"}}, {"family": "Rode", "given": "Daniel K H", "initials": "DKH", "orcid": "0000-0002-2950-9340", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/eefcabd0aaa04ef48655ffd4a2cad234.json"}}, {"family": "Torrens", "given": "Gabriel", "initials": "G", "orcid": "0000-0002-0450-1430", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/2a84794f089441ea8700f06f5a59fc2f.json"}}, {"family": "Hansen", "given": "Mads F", "initials": "MF", "orcid": "0000-0001-9283-304X", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/c4b30568f42d4c9aaa9adf4c40c4236b.json"}}, {"family": "Singh", "given": "Praveen K", "initials": "PK"}, {"family": "Jelli", "given": "Eric", "initials": "E"}, {"family": "Nosho", "given": "Kazuki", "initials": "K", "orcid": "0000-0002-4811-1397", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/98939cbb1f3846fabae4f6cc3dd50358.json"}}, {"family": "Jeckel", "given": "Hannah", "initials": "H", "orcid": "0000-0002-7080-4907", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/bae296847edf416eb5fb1c914c68d5eb.json"}}, {"family": "G\u00f6ttig", "given": "Stephan", "initials": "S", "orcid": "0000-0001-6896-5309", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/d0d88e8d89dd4773bb162eb97e1d9b47.json"}}, {"family": "Cava", "given": "Felipe", "initials": "F", "orcid": "0000-0001-5995-718X", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/bbcff12a06814d54afea533e125a1213.json"}}, {"family": "Drescher", "given": "Knut", "initials": "K", "orcid": "0000-0002-7340-2444", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/a9b570dc764c4e99a349e89f5493e3d0.json"}}], "type": "journal article", "published": "2025-01-00", "journal": {"title": "Nat. Microbiol", "issn": "2058-5276", "volume": "10", "issue": "1", "pages": "144-157", "issn-l": "2058-5276"}, "abstract": "For any organism, survival is enhanced by the ability to sense and respond to threats in advance. For bacteria, danger sensing among kin cells has been observed, but the presence or impacts of general danger signals are poorly understood. Here we show that different bacterial species use exogenous peptidoglycan fragments, which are released by nearby kin or non-kin cell lysis, as a general danger signal. Using microscopy and gene expression profiling of Vibrio cholerae, we find that even brief signal exposure results in a regulatory response that causes three-dimensional biofilm formation, which protects cells from a broad range of stresses, including bacteriophage predation. A diverse set of species (Pseudomonas aeruginosa, Acinetobacter baumannii, Staphylococcus aureus, Enterococcus faecalis) also respond to exogenous peptidoglycan by forming biofilms. As peptidoglycan from different Gram-negative and Gram-positive species triggered three-dimensional biofilm formation, we propose that this danger signal and danger response are conserved among bacteria.", "doi": "10.1038/s41564-024-01886-5", "pmid": "39753671", "labels": [], "xrefs": [{"db": "pmc", "key": "PMC11726461"}, {"db": "pii", "key": "10.1038/s41564-024-01886-5"}], "notes": [], "created": "2026-08-20T08:55:27.048Z", "modified": "2026-08-20T08:55:27.416Z"}, {"entity": "publication", "iuid": "cfe0e5a21b264459be8dac1dfbee6b1f", "links": {"self": {"href": "https://publications-affiliated.scilifelab.se/publication/cfe0e5a21b264459be8dac1dfbee6b1f.json"}, "display": {"href": "https://publications-affiliated.scilifelab.se/publication/cfe0e5a21b264459be8dac1dfbee6b1f"}}, "title": "Evolutionary rescue of spherical mreB deletion mutants of the rod-shape bacterium Pseudomonas fluorescens SBW25", "authors": [{"family": "Yulo", "given": "P Richard J", "initials": "PRJ", "orcid": "0009-0008-2288-0711", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/e9a9ec12f9544be1b6d7d0619ce84a7e.json"}}, {"family": "Desprat", "given": "Nicolas", "initials": "N", "orcid": "0000-0002-5016-9360", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/391c6fe36720427184c3e3a67499a593.json"}}, {"family": "Gerth", "given": "Monica L", "initials": "ML", "orcid": "0000-0002-7959-7852", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/9c7e73febc234a15bfb1539af2321bdd.json"}}, {"family": "Ritzl-Rinkenberger", "given": "Barbara", "initials": "B"}, {"family": "Farr", "given": "Andrew D", "initials": "AD", "orcid": "0000-0002-3402-1665", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/8aeb2de20ef94a2799a14ff1eac049dd.json"}}, {"family": "Liu", "given": "Yunhao", "initials": "Y", "orcid": "0000-0002-0279-1307", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/19280708461440438e5f0b0497be5381.json"}}, {"family": "Zhang", "given": "Xue Xian", "initials": "XX", "orcid": "0000-0002-6536-3529", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/744837cd120040d980a9a389d513be3d.json"}}, {"family": "Miller", "given": "Michael", "initials": "M", "orcid": "0000-0002-1723-7958", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/76923e46e3384123bd3bc451a47a6eb7.json"}}, {"family": "Cava", "given": "Felipe", "initials": "F", "orcid": "0000-0001-5995-718X", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/bbcff12a06814d54afea533e125a1213.json"}}, {"family": "Rainey", "given": "Paul B", "initials": "PB", "orcid": "0000-0003-0879-5795", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/54e6f301a7a848f2aac5230a583e7de8.json"}}, {"family": "Hendrickson", "given": "Heather L", "initials": "HL", "orcid": "0000-0003-3471-4397", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/04d5b11678894b9992f668ad678c5b60.json"}}], "type": "posted-content", "published": "2024-12-23", "journal": {"issn-l": null}, "abstract": null, "doi": "10.7554/elife.98218.2", "pmid": null, "labels": [], "xrefs": [], "notes": [], "created": "2026-08-20T13:56:34.223Z", "modified": "2026-08-20T13:56:34.337Z"}, {"entity": "publication", "iuid": "8e91f4b0748740f5a05727f4fc019b92", "links": {"self": {"href": "https://publications-affiliated.scilifelab.se/publication/8e91f4b0748740f5a05727f4fc019b92.json"}, "display": {"href": "https://publications-affiliated.scilifelab.se/publication/8e91f4b0748740f5a05727f4fc019b92"}}, "title": "Mechanisms conferring bacterial cell wall variability and adaptivity.", "authors": [{"family": "Torrens", "given": "Gabriel", "initials": "G", "orcid": "0000-0002-0450-1430", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/2a84794f089441ea8700f06f5a59fc2f.json"}}, {"family": "Cava", "given": "Felipe", "initials": "F", "orcid": "0000-0001-5995-718X", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/bbcff12a06814d54afea533e125a1213.json"}}], "type": "journal article", "published": "2024-10-30", "journal": {"title": "Biochem. Soc. Trans.", "issn": "1470-8752", "volume": "52", "issue": "5", "pages": "1981-1993", "issn-l": "0300-5127"}, "abstract": "The bacterial cell wall, a sophisticated and dynamic structure predominantly composed of peptidoglycan (PG), plays a pivotal role in bacterial survival and adaptation. Bacteria actively modify their cell walls by editing PG components in response to environmental challenges. Diverse variations in peptide composition, cross-linking patterns, and glycan strand structures empower bacteria to resist antibiotics, evade host immune detection, and adapt to dynamic environments. This review comprehensively summarizes the most common modifications reported to date and their associated adaptive role and further highlights how regulation of PG synthesis and turnover provides resilience to cell lysis.", "doi": "10.1042/BST20230027", "pmid": "39324635", "labels": [], "xrefs": [{"db": "pmc", "key": "PMC11555704"}, {"db": "pii", "key": "235010"}], "notes": [], "created": "2026-08-20T09:28:26.367Z", "modified": "2026-08-20T09:28:26.434Z"}, {"entity": "publication", "iuid": "a9cfff1aa2a24f22a98df7eee2f4eb5c", "links": {"self": {"href": "https://publications-affiliated.scilifelab.se/publication/a9cfff1aa2a24f22a98df7eee2f4eb5c.json"}, "display": {"href": "https://publications-affiliated.scilifelab.se/publication/a9cfff1aa2a24f22a98df7eee2f4eb5c"}}, "title": "Bacterial spore surface nanoenvironment requires a AAA+ ATPase to promote MurG function.", "authors": [{"family": "Delerue", "given": "Thomas", "initials": "T", "orcid": "0000-0002-8900-247X", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/e98591b1cc0349f5bfd3aeaa9abfe5a6.json"}}, {"family": "Updegrove", "given": "Taylor B", "initials": "TB", "orcid": "0000-0002-9763-3618", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/1f7584b3edb94db495422fd14557ee5f.json"}}, {"family": "Chareyre", "given": "Sylvia", "initials": "S"}, {"family": "Anantharaman", "given": "Vivek", "initials": "V", "orcid": "0000-0001-8395-0009", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/50872c7e2a114a5e9329134c0c0a203d.json"}}, {"family": "Gilmore", "given": "Michael C", "initials": "MC", "orcid": "0000-0002-6848-5134", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/afac90582c374ab9b15102bc27516d89.json"}}, {"family": "Jenkins", "given": "Lisa M", "initials": "LM", "orcid": "0000-0003-1245-1338", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/3dd3f6d782664134a47c5f2a67b774e3.json"}}, {"family": "Popham", "given": "David L", "initials": "DL", "orcid": "0000-0002-2614-143X", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/d7ccbe2816c54cfe9d729b794fcf6242.json"}}, {"family": "Cava", "given": "Felipe", "initials": "F", "orcid": "0000-0001-5995-718X", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/bbcff12a06814d54afea533e125a1213.json"}}, {"family": "Aravind", "given": "L", "initials": "L", "orcid": "0000-0003-0771-253X", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/2b3c1866cc2e407a9230dbff1e5609c8.json"}}, {"family": "Ramamurthi", "given": "Kumaran S", "initials": "KS"}], "type": "journal article", "published": "2024-10-22", "journal": {"title": "Proc. Natl. Acad. Sci. U.S.A.", "issn": "1091-6490", "volume": "121", "issue": "43", "pages": "e2414737121", "issn-l": "0027-8424"}, "abstract": "Bacillus subtilis spores are produced inside the cytosol of a mother cell. Spore surface assembly requires the SpoVK protein in the mother cell, but its function is unknown. Here, we report that SpoVK is a sporulation-specific, forespore-localized putative chaperone from a distinct higher-order clade of AAA+ ATPases that promotes the peptidoglycan glycosyltransferase activity of MurG during sporulation, even though MurG does not normally require activation during vegetative growth. MurG redeploys to the forespore surface during sporulation, where we show that the local pH is reduced and propose that this change in cytosolic nanoenvironment abrogates MurG function. Further, we show that SpoVK participates in a developmental checkpoint in which improper spore surface assembly mis-localizes SpoVK, which leads to sporulation arrest. The AAA+ ATPase clade containing SpoVK includes specialized chaperones involved in secretion, cell envelope biosynthesis, and carbohydrate metabolism, suggesting that such fine-tuning might be a widespread feature of different subcellular nanoenvironments.", "doi": "10.1073/pnas.2414737121", "pmid": "39405354", "labels": [], "xrefs": [{"db": "pmc", "key": "PMC11513918"}], "notes": [], "created": "2026-08-20T09:31:39.352Z", "modified": "2026-08-20T09:31:39.656Z"}, {"entity": "publication", "iuid": "dda09c0a9a3140d7b58c2557a6137522", "links": {"self": {"href": "https://publications-affiliated.scilifelab.se/publication/dda09c0a9a3140d7b58c2557a6137522.json"}, "display": {"href": "https://publications-affiliated.scilifelab.se/publication/dda09c0a9a3140d7b58c2557a6137522"}}, "title": "LD-transpeptidation is crucial for fitness and polar growth in Agrobacterium tumefaciens.", "authors": [{"family": "Aliashkevich", "given": "Alena", "initials": "A"}, {"family": "Guest", "given": "Thomas", "initials": "T", "orcid": "0000-0002-7868-0611", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/0210aa68ff384d83947c28a5a65917e1.json"}}, {"family": "Alvarez", "given": "Laura", "initials": "L", "orcid": "0000-0003-2429-7542", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/329d8b1460fe44789dbef53ea0493294.json"}}, {"family": "Gilmore", "given": "Michael C", "initials": "MC", "orcid": "0000-0002-6848-5134", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/afac90582c374ab9b15102bc27516d89.json"}}, {"family": "Rea", "given": "Daniel", "initials": "D", "orcid": "0009-0009-6904-1031", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/9f965bfb3ab44e82b84e6898fdf76ccf.json"}}, {"family": "Amstutz", "given": "Jennifer", "initials": "J"}, {"family": "Mateus", "given": "Andr\u00e9", "initials": "A", "orcid": "0000-0001-6870-0677", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/ebf0d242aa894a66b60828456bbc22aa.json"}}, {"family": "Schiffthaler", "given": "Bastian", "initials": "B", "orcid": "0000-0002-9771-467X", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/0d53293c611f44dda99e9249b1614132.json"}}, {"family": "Ruiz", "given": "I\u00f1igo", "initials": "I"}, {"family": "Typas", "given": "Athanasios", "initials": "A", "orcid": "0000-0002-0797-9018", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/d38ea7a531ad47cfa26df998f0e54dbe.json"}}, {"family": "Savitski", "given": "Mikhail M", "initials": "MM"}, {"family": "Brown", "given": "Pamela J B", "initials": "PJB", "orcid": "0000-0002-7558-7155", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/724518d7b8f24b438cd852bea2119e61.json"}}, {"family": "Cava", "given": "Felipe", "initials": "F", "orcid": "0000-0001-5995-718X", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/bbcff12a06814d54afea533e125a1213.json"}}], "type": "journal article", "published": "2024-10-00", "journal": {"title": "PLoS Genet", "issn": "1553-7404", "volume": "20", "issue": "10", "pages": "e1011449", "issn-l": "1553-7390"}, "abstract": "Peptidoglycan (PG), a mesh-like structure which is the primary component of the bacterial cell wall, is crucial to maintain cell integrity and shape. While most bacteria rely on penicillin binding proteins (PBPs) for crosslinking, some species also employ LD-transpeptidases (LDTs). Unlike PBPs, the essentiality and biological functions of LDTs remain largely unclear. The Hyphomicrobiales order of the Alphaproteobacteria, known for their polar growth, have PG which is unusually rich in LD-crosslinks, suggesting that LDTs may play a more significant role in PG synthesis in these bacteria. Here, we investigated LDTs in the plant pathogen Agrobacterium tumefaciens and found that LD-transpeptidation, resulting from at least one of 14 putative LDTs present in this bacterium, is essential for its survival. Notably, a mutant lacking a distinctive group of 7 LDTs which are broadly conserved among the Hyphomicrobiales exhibited reduced LD-crosslinking and tethering of PG to outer membrane \u03b2-barrel proteins. Consequently, this mutant suffered severe fitness loss and cell shape rounding, underscoring the critical role played by these Hyphomicrobiales-specific LDTs in maintaining cell wall integrity and promoting elongation. Tn-sequencing screens further revealed non-redundant functions for A. tumefaciens LDTs. Specifically, Hyphomicrobiales-specific LDTs exhibited synthetic genetic interactions with division and cell cycle proteins, and a single LDT from another group. Additionally, our findings demonstrate that strains lacking all LDTs except one displayed distinctive phenotypic profiles and genetic interactions. Collectively, our work emphasizes the critical role of LD-crosslinking in A. tumefaciens cell wall integrity and growth and provides insights into the functional specialization of these crosslinking activities.", "doi": "10.1371/journal.pgen.1011449", "pmid": "39432536", "labels": [], "xrefs": [{"db": "pmc", "key": "PMC11527210"}, {"db": "pii", "key": "PGENETICS-D-24-00706"}], "notes": [], "created": "2026-08-20T12:43:54.428Z", "modified": "2026-08-20T12:43:54.645Z"}, {"entity": "publication", "iuid": "7d1b9ef2c00c47b9b508ee060129596d", "links": {"self": {"href": "https://publications-affiliated.scilifelab.se/publication/7d1b9ef2c00c47b9b508ee060129596d.json"}, "display": {"href": "https://publications-affiliated.scilifelab.se/publication/7d1b9ef2c00c47b9b508ee060129596d"}}, "title": "A potential space-making role in cell wall biogenesis for SltB1and DacB revealed by a beta-lactamase induction phenotype in Pseudomonas aeruginosa.", "authors": [{"family": "Gyger", "given": "Jo\u00ebl", "initials": "J"}, {"family": "Torrens", "given": "Gabriel", "initials": "G"}, {"family": "Cava", "given": "Felipe", "initials": "F", "orcid": "0000-0001-5995-718X", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/bbcff12a06814d54afea533e125a1213.json"}}, {"family": "Bernhardt", "given": "Thomas G", "initials": "TG", "orcid": "0000-0003-3566-7756", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/ea73f668f266458f84121087f7b732cc.json"}}, {"family": "Fumeaux", "given": "Coralie", "initials": "C", "orcid": "0000-0002-6969-3111", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/34711f3602884fd690fdb859dae1cc8e.json"}}], "type": "journal article", "published": "2024-07-17", "journal": {"title": "MBio", "issn": "2150-7511", "volume": "15", "issue": "7", "pages": "e0141924", "issn-l": null}, "abstract": "Pseudomonas aeruginosa encodes the beta-lactamase AmpC, which promotes resistance to beta-lactam antibiotics. Expression of ampC is induced by anhydro-muropeptides (AMPs) released from the peptidoglycan (PG) cell wall upon beta-lactam treatment. AmpC can also be induced via genetic inactivation of PG biogenesis factors such as the endopeptidase DacB that cleaves PG crosslinks. Mutants in dacB occur in beta-lactam-resistant clinical isolates of P. aeruginosa, but it has remained unclear why DacB inactivation promotes ampC induction. Similarly, the inactivation of lytic transglycosylase (LT) enzymes such as SltB1 that cut PG glycans has also been associated with ampC induction and beta-lactam resistance. Given that LT enzymes are capable of producing AMP products that serve as ampC inducers, this latter observation has been especially difficult to explain. Here, we show that ampC induction in sltB1 or dacB mutants requires another LT enzyme called MltG. In Escherichia coli, MltG has been implicated in the degradation of nascent PG strands produced upon beta-lactam treatment. Accordingly, in P. aeruginosa sltB1 and dacB mutants, we detected the MltG-dependent production of pentapeptide-containing AMP products that are signatures of nascent PG degradation. Our results therefore support a model in which SltB1 and DacB use their PG-cleaving activity to open space in the PG matrix for the insertion of new material. Thus, their inactivation mimics low-level beta-lactam treatment by reducing the efficiency of new PG insertion into the wall, causing the degradation of some nascent PG material by MltG to produce the ampC-inducing signal.\n\nInducible beta-lactamases like the ampC system of Pseudomonas aeruginosa are a common determinant of beta-lactam resistance among gram-negative bacteria. The regulation of ampC is elegantly tuned to detect defects in cell wall synthesis caused by beta-lactam drugs. Studies of mutations causing ampC induction in the absence of drug therefore promise to reveal new insights into the process of cell wall biogenesis in addition to aiding our understanding of how resistance to beta-lactam antibiotics arises in the clinic. In this study, the ampC induction phenotype for mutants lacking a glycan-cleaving enzyme or an enzyme that cuts cell wall crosslinks was used to uncover a potential role for these enzymes in making space in the wall matrix for the insertion of new material during cell growth.", "doi": "10.1128/mbio.01419-24", "pmid": "38920394", "labels": [], "xrefs": [{"db": "pmc", "key": "PMC11253642"}], "notes": [], "created": "2026-08-20T12:00:28.713Z", "modified": "2026-08-20T12:00:28.846Z"}, {"entity": "publication", "iuid": "76c7e316ba154cd5b42e077d662a0fa5", "links": {"self": {"href": "https://publications-affiliated.scilifelab.se/publication/76c7e316ba154cd5b42e077d662a0fa5.json"}, "display": {"href": "https://publications-affiliated.scilifelab.se/publication/76c7e316ba154cd5b42e077d662a0fa5"}}, "title": "Evolutionary rescue of spherical mreB deletion mutants of the rod-shape bacterium Pseudomonas fluorescens SBW25", "authors": [{"family": "Yulo", "given": "P Richard J", "initials": "PRJ", "orcid": "0009-0008-2288-0711", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/e9a9ec12f9544be1b6d7d0619ce84a7e.json"}}, {"family": "Desprat", "given": "Nicolas", "initials": "N", "orcid": "0000-0002-5016-9360", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/391c6fe36720427184c3e3a67499a593.json"}}, {"family": "Gerth", "given": "Monica L", "initials": "ML", "orcid": "0000-0002-7959-7852", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/9c7e73febc234a15bfb1539af2321bdd.json"}}, {"family": "Ritzl-Rinkenberger", "given": "Barbara", "initials": "B"}, {"family": "Farr", "given": "Andrew D", "initials": "AD", "orcid": "0000-0002-3402-1665", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/8aeb2de20ef94a2799a14ff1eac049dd.json"}}, {"family": "Liu", "given": "Yunhao", "initials": "Y", "orcid": "0000-0002-0279-1307", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/19280708461440438e5f0b0497be5381.json"}}, {"family": "Zhang", "given": "Xue Xian", "initials": "XX", "orcid": "0000-0002-6536-3529", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/744837cd120040d980a9a389d513be3d.json"}}, {"family": "Miller", "given": "Michael", "initials": "M", "orcid": "0000-0002-1723-7958", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/76923e46e3384123bd3bc451a47a6eb7.json"}}, {"family": "Cava", "given": "Felipe", "initials": "F", "orcid": "0000-0001-5995-718X", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/bbcff12a06814d54afea533e125a1213.json"}}, {"family": "Rainey", "given": "Paul B", "initials": "PB", "orcid": "0000-0003-0879-5795", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/54e6f301a7a848f2aac5230a583e7de8.json"}}, {"family": "Hendrickson", "given": "Heather L", "initials": "HL", "orcid": "0000-0003-3471-4397", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/04d5b11678894b9992f668ad678c5b60.json"}}], "type": "posted-content", "published": "2024-07-10", "journal": {"issn-l": null}, "abstract": null, "doi": "10.7554/elife.98218.1", "pmid": null, "labels": [], "xrefs": [], "notes": [], "created": "2026-08-20T13:56:32.233Z", "modified": "2026-08-20T13:56:32.477Z"}, {"entity": "publication", "iuid": "769252f98d4d413f8169f10a9bc18d09", "links": {"self": {"href": "https://publications-affiliated.scilifelab.se/publication/769252f98d4d413f8169f10a9bc18d09.json"}, "display": {"href": "https://publications-affiliated.scilifelab.se/publication/769252f98d4d413f8169f10a9bc18d09"}}, "title": "Flotillin-mediated stabilization of unfolded proteins in bacterial membrane microdomains.", "authors": [{"family": "Ukleja", "given": "Marta", "initials": "M"}, {"family": "Kricks", "given": "Lara", "initials": "L"}, {"family": "Torrens", "given": "Gabriel", "initials": "G", "orcid": "0000-0002-0450-1430", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/2a84794f089441ea8700f06f5a59fc2f.json"}}, {"family": "Peschiera", "given": "Ilaria", "initials": "I"}, {"family": "Rodrigues-Lopes", "given": "Ines", "initials": "I", "orcid": "0000-0003-1527-543X", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/b55f926c177244acbc9e678dc34214cf.json"}}, {"family": "Krupka", "given": "Marcin", "initials": "M"}, {"family": "Garc\u00eda-Fern\u00e1ndez", "given": "Julia", "initials": "J", "orcid": "0000-0002-6937-6394", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/4edabdb1b90b40e5b135f493cfcc4c06.json"}}, {"family": "Melero", "given": "Roberto", "initials": "R"}, {"family": "Del Campo", "given": "Rosa", "initials": "R", "orcid": "0000-0003-1147-7923", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/04422045102340b882583dbd9646f02a.json"}}, {"family": "Eulalio", "given": "Ana", "initials": "A", "orcid": "0000-0002-7355-0674", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/835301642c0548a3984cbb9a07ed75ed.json"}}, {"family": "Mateus", "given": "Andr\u00e9", "initials": "A", "orcid": "0000-0001-6870-0677", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/ebf0d242aa894a66b60828456bbc22aa.json"}}, {"family": "L\u00f3pez-Bravo", "given": "Mar\u00eda", "initials": "M"}, {"family": "Rico", "given": "Ana I", "initials": "AI", "orcid": "0000-0001-6021-3970", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/808592d786cc42d3897b0f19eebeee70.json"}}, {"family": "Cava", "given": "Felipe", "initials": "F", "orcid": "0000-0001-5995-718X", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/bbcff12a06814d54afea533e125a1213.json"}}, {"family": "Lopez", "given": "Daniel", "initials": "D", "orcid": "0000-0002-8627-3813", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/6fb3e72f8f1e4cebb70e008a8a9acc08.json"}}], "type": "journal article", "published": "2024-07-03", "journal": {"title": "Nat Commun", "issn": "2041-1723", "volume": "15", "issue": "1", "pages": "5583", "issn-l": "2041-1723"}, "abstract": "The function of many bacterial processes depends on the formation of functional membrane microdomains (FMMs), which resemble the lipid rafts of eukaryotic cells. However, the mechanism and the biological function of these membrane microdomains remain unclear. Here, we show that FMMs in the pathogen methicillin-resistant Staphylococcus aureus (MRSA) are dedicated to confining and stabilizing proteins unfolded due to cellular stress. The FMM scaffold protein flotillin forms a clamp-shaped oligomer that holds unfolded proteins, stabilizing them and favoring their correct folding. This process does not impose a direct energy cost on the cell and is crucial to survival of ATP-depleted bacteria, and thus to pathogenesis. Consequently, FMM disassembling causes the accumulation of unfolded proteins, which compromise MRSA viability during infection and cause penicillin re-sensitization due to PBP2a unfolding. Thus, our results indicate that FMMs mediate ATP-independent stabilization of unfolded proteins, which is essential for bacterial viability during infection.", "doi": "10.1038/s41467-024-49951-1", "pmid": "38961085", "labels": [], "xrefs": [{"db": "pmc", "key": "PMC11222466"}, {"db": "pii", "key": "10.1038/s41467-024-49951-1"}], "notes": [], "created": "2026-08-20T08:53:28.683Z", "modified": "2026-08-20T08:53:29.010Z"}, {"entity": "publication", "iuid": "b48713e5b23044a7bd68d9fae8b70908", "links": {"self": {"href": "https://publications-affiliated.scilifelab.se/publication/b48713e5b23044a7bd68d9fae8b70908.json"}, "display": {"href": "https://publications-affiliated.scilifelab.se/publication/b48713e5b23044a7bd68d9fae8b70908"}}, "title": "Genetic interaction mapping reveals functional relationships between peptidoglycan endopeptidases and carboxypeptidases.", "authors": [{"family": "Alvarado Obando", "given": "Manuela", "initials": "M", "orcid": "0000-0003-0181-3284", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/d0c1a5e0b23241788d136cda3b810c2b.json"}}, {"family": "Rey-Varela", "given": "Diego", "initials": "D", "orcid": "0000-0003-1241-2881", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/671c327d978d4d8c8b6b3eae8dde209d.json"}}, {"family": "Cava", "given": "Felipe", "initials": "F", "orcid": "0000-0001-5995-718X", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/bbcff12a06814d54afea533e125a1213.json"}}, {"family": "D\u00f6rr", "given": "Tobias", "initials": "T", "orcid": "0000-0003-3283-9161", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/5ead1628262f4b459175cbd5ddf0ca31.json"}}], "type": "journal article", "published": "2024-04-00", "journal": {"title": "PLoS Genet", "issn": "1553-7404", "volume": "20", "issue": "4", "pages": "e1011234", "issn-l": "1553-7390"}, "abstract": "Peptidoglycan (PG) is the main component of the bacterial cell wall; it maintains cell shape while protecting the cell from internal osmotic pressure and external environmental challenges. PG synthesis is essential for bacterial growth and survival, and a series of PG modifications are required to allow expansion of the sacculus. Endopeptidases (EPs), for example, cleave the crosslinks between adjacent PG strands to allow the incorporation of newly synthesized PG. EPs are collectively essential for bacterial growth and must likely be carefully regulated to prevent sacculus degradation and cell death. However, EP regulation mechanisms are poorly understood. Here, we used TnSeq to uncover novel EP regulators in Vibrio cholerae. This screen revealed that the carboxypeptidase DacA1 (PBP5) alleviates EP toxicity. dacA1 is essential for viability on LB medium, and this essentiality was suppressed by EP overexpression, revealing that EP toxicity both mitigates, and is mitigated by, a defect in dacA1. A subsequent suppressor screen to restore viability of \u0394dacA1 in LB medium identified hypomorphic mutants in the PG synthesis pathway, as well as mutations that promote EP activation. Our data thus reveal a more complex role of DacA1 in maintaining PG homeostasis than previously assumed.", "doi": "10.1371/journal.pgen.1011234", "pmid": "38598601", "labels": [], "xrefs": [{"db": "pmc", "key": "PMC11034669"}, {"db": "pii", "key": "PGENETICS-D-23-01149"}, {"db": "BioProject", "key": "PRJNA1088767"}, {"db": "BioProject", "key": "PRJNA1088760"}], "notes": [], "created": "2026-08-20T12:43:52.596Z", "modified": "2026-08-20T12:43:52.766Z"}, {"entity": "publication", "iuid": "bfcbb43625f64058942fd2f5b18f87d4", "links": {"self": {"href": "https://publications-affiliated.scilifelab.se/publication/bfcbb43625f64058942fd2f5b18f87d4.json"}, "display": {"href": "https://publications-affiliated.scilifelab.se/publication/bfcbb43625f64058942fd2f5b18f87d4"}}, "title": "Breaking Barriers: pCF10 Type 4 Secretion System relies on a self-regulating muramidase to modulate the cell wall", "authors": [{"family": "Sun", "given": "Wei Sheng", "initials": "WS", "orcid": "0000-0001-9738-8862", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/d00b7dff289b4b988e3c21f921f8dc11.json"}}, {"family": "Torrens", "given": "Gabriel", "initials": "G", "orcid": "0000-0002-0450-1430", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/2a84794f089441ea8700f06f5a59fc2f.json"}}, {"family": "Beek", "given": "Josy ter", "initials": "Jt", "orcid": "0000-0003-4165-9277", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/b3d76493e80b4b57a951a0f94e6123ca.json"}}, {"family": "Cava", "given": "Felipe", "initials": "F", "orcid": "0000-0001-5995-718X", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/bbcff12a06814d54afea533e125a1213.json"}}, {"family": "Berntsson", "given": "Ronnie P A", "initials": "RPA", "orcid": "0000-0001-6848-322X", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/cb9399248b784100a8020261949fb910.json"}}], "type": "posted-content", "published": "2024-02-15", "journal": {"issn-l": null}, "abstract": null, "doi": "10.1101/2024.02.15.580431", "pmid": null, "labels": [], "xrefs": [], "notes": [], "created": "2026-08-20T10:52:16.449Z", "modified": "2026-08-20T10:52:16.557Z"}, {"entity": "publication", "iuid": "33463bd996d148f7abd7b70bcdca36c1", "links": {"self": {"href": "https://publications-affiliated.scilifelab.se/publication/33463bd996d148f7abd7b70bcdca36c1.json"}, "display": {"href": "https://publications-affiliated.scilifelab.se/publication/33463bd996d148f7abd7b70bcdca36c1"}}, "title": "A distinctive family of L,D-transpeptidases catalyzing L-Ala-mDAP crosslinks in Alpha- and Betaproteobacteria.", "authors": [{"family": "Espaillat", "given": "Akbar", "initials": "A"}, {"family": "Alvarez", "given": "Laura", "initials": "L", "orcid": "0000-0003-2429-7542", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/329d8b1460fe44789dbef53ea0493294.json"}}, {"family": "Torrens", "given": "Gabriel", "initials": "G", "orcid": "0000-0002-0450-1430", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/2a84794f089441ea8700f06f5a59fc2f.json"}}, {"family": "Ter Beek", "given": "Josy", "initials": "J", "orcid": "0000-0003-4165-9277", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/b3d76493e80b4b57a951a0f94e6123ca.json"}}, {"family": "Miguel-Ruano", "given": "Vega", "initials": "V", "orcid": "0000-0002-2492-7164", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/4ee0be393f7b44f3aeb6c926d39dfac9.json"}}, {"family": "Irazoki", "given": "Oihane", "initials": "O"}, {"family": "Gago", "given": "Federico", "initials": "F", "orcid": "0000-0002-3071-4878", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/2f4b917616c44f69acace2feeb97763d.json"}}, {"family": "Hermoso", "given": "Juan A", "initials": "JA"}, {"family": "Berntsson", "given": "Ronnie P-A", "initials": "RP", "orcid": "0000-0001-6848-322X", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/cb9399248b784100a8020261949fb910.json"}}, {"family": "Cava", "given": "Felipe", "initials": "F", "orcid": "0000-0001-5995-718X", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/bbcff12a06814d54afea533e125a1213.json"}}], "type": "journal article", "published": "2024-02-13", "journal": {"title": "Nat Commun", "issn": "2041-1723", "volume": "15", "issue": "1", "pages": "1343", "issn-l": "2041-1723"}, "abstract": "The bacterial cell-wall peptidoglycan is made of glycan strands crosslinked by short peptide stems. Crosslinks are catalyzed by DD-transpeptidases (4,3-crosslinks) and LD-transpeptidases (3,3-crosslinks). However, recent research on non-model species has revealed novel crosslink types, suggesting the existence of uncharacterized enzymes. Here, we identify an LD-transpeptidase, LDTGo, that generates 1,3-crosslinks in the acetic-acid bacterium Gluconobacter oxydans. LDTGo-like proteins are found in Alpha- and Betaproteobacteria lacking LD3,3-transpeptidases. In contrast with the strict specificity of typical LD- and DD-transpeptidases, LDTGo can use non-terminal amino acid moieties for crosslinking. A high-resolution crystal structure of LDTGo reveals unique features when compared to LD3,3-transpeptidases, including a proline-rich region that appears to limit substrate access, and a cavity accommodating both glycan chain and peptide stem from donor muropeptides. Finally, we show that DD-crosslink turnover is involved in supplying the necessary substrate for LD1,3-transpeptidation. This phenomenon underscores the interplay between distinct crosslinking mechanisms in maintaining cell wall integrity in G. oxydans.", "doi": "10.1038/s41467-024-45620-5", "pmid": "38351082", "labels": [], "xrefs": [{"db": "pmc", "key": "PMC10864386"}, {"db": "pii", "key": "10.1038/s41467-024-45620-5"}], "notes": [], "created": "2026-08-20T08:53:08.705Z", "modified": "2026-08-20T08:53:08.995Z"}, {"entity": "publication", "iuid": "4ac2dc06fb6a4cf89b011e164391d261", "links": {"self": {"href": "https://publications-affiliated.scilifelab.se/publication/4ac2dc06fb6a4cf89b011e164391d261.json"}, "display": {"href": "https://publications-affiliated.scilifelab.se/publication/4ac2dc06fb6a4cf89b011e164391d261"}}, "title": "Escherichia coli CadB is capable of promiscuously transporting muropeptides and contributing to peptidoglycan recycling.", "authors": [{"family": "Simpson", "given": "Brent W", "initials": "BW", "orcid": "0000-0002-1655-7407", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/305dbc02680144239c110e9fa9a8af70.json"}}, {"family": "Gilmore", "given": "Michael C", "initials": "MC"}, {"family": "McLean", "given": "Amanda Briann", "initials": "AB"}, {"family": "Cava", "given": "Felipe", "initials": "F", "orcid": "0000-0001-5995-718X", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/bbcff12a06814d54afea533e125a1213.json"}}, {"family": "Trent", "given": "M Stephen", "initials": "MS", "orcid": "0000-0001-6134-1800", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/c555a9ce60364c33a3fc70639bebb047.json"}}], "type": "journal article", "published": "2024-01-25", "journal": {"title": "J. Bacteriol.", "issn": "1098-5530", "volume": "206", "issue": "1", "pages": "e0036923", "issn-l": "0021-9193"}, "abstract": "The bacterial peptidoglycan (PG) cell wall is remodeled during growth and division, releasing fragments called muropeptides. Muropeptides can be internalized and reused in a process called PG recycling. Escherichia coli is highly devoted to recycling muropeptides and is known to have at least two transporters, AmpG and OppBCDF, that import them into the cytoplasm. While studying mutants lacking AmpG, we unintentionally isolated mutations that led to the altered expression of a third transporter, CadB. CadB is normally upregulated under acidic pH conditions and is an antiporter for lysine and cadaverine. Here, we explored if CadB was altering PG recycling to assist in the absence of AmpG. Surprisingly, CadB overexpression was able to restore PG recycling when both AmpG and OppBCDF were absent. CadB was found to import freed PG peptides, a subpopulation of muropeptides, through a promiscuous activity. Altogether, our data support that CadB is a third transporter capable of contributing to PG recycling. IMPORTANCE Bacteria produce a rigid mesh cell wall. During growth, the cell wall is remodeled, which releases cell wall fragments. If released into the extracellular environment, cell wall fragments can trigger inflammation by the immune system of a host. Gastrointestinal bacteria, like Escherichia coli, have dedicated pathways to recycle almost all cell wall fragments they produce. E. coli contains two known recycling transporters, AmpG and Opp, that we previously showed are optimized for growth in different environments. Here, we identify that a third transporter, CadB, can also contribute to cell wall recycling. This work expands our understanding of cell wall recycling and highlights the dedication of organisms like E. coli to ensure high recycling in multiple growth environments.", "doi": "10.1128/jb.00369-23", "pmid": "38169298", "labels": [], "xrefs": [{"db": "pmc", "key": "PMC10810205"}], "notes": [], "created": "2026-08-20T12:00:22.551Z", "modified": "2026-08-20T12:00:22.664Z"}, {"entity": "publication", "iuid": "3195ab9977a6442b8fbfb43653c315f6", "links": {"self": {"href": "https://publications-affiliated.scilifelab.se/publication/3195ab9977a6442b8fbfb43653c315f6.json"}, "display": {"href": "https://publications-affiliated.scilifelab.se/publication/3195ab9977a6442b8fbfb43653c315f6"}}, "title": "MacP bypass variants of Streptococcus pneumoniae PBP2a suggest a conserved mechanism for the activation of bifunctional cell wall synthases.", "authors": [{"family": "Midonet", "given": "Caroline", "initials": "C"}, {"family": "Bisset", "given": "Sean", "initials": "S"}, {"family": "Shlosman", "given": "Irina", "initials": "I"}, {"family": "Cava", "given": "Felipe", "initials": "F", "orcid": "0000-0001-5995-718X", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/bbcff12a06814d54afea533e125a1213.json"}}, {"family": "Rudner", "given": "David Z", "initials": "DZ", "orcid": "0000-0002-0236-7143", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/f12d8cd1d4644e5fa000b30b91cd7ee1.json"}}, {"family": "Bernhardt", "given": "Thomas G", "initials": "TG", "orcid": "0000-0003-3566-7756", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/ea73f668f266458f84121087f7b732cc.json"}}], "type": "journal article", "published": "2023-12-19", "journal": {"title": "MBio", "issn": "2150-7511", "volume": "14", "issue": "6", "pages": "e0239023", "issn-l": null}, "abstract": "Class A penicillin-binding proteins (aPBPs) play critical roles in bacterial cell wall biogenesis. As the targets of penicillin, they are among the most important drug targets in history. Although the biochemical activities of these enzymes have been well studied, little is known about how they are regulated in cells to control when and where peptidoglycan is made. In this report, we isolate variants of the Streptococcus pneumoniae enzyme PBP2a that function in cells without MacP, a partner normally required for its activity. The amino acid substitutions activate the cell wall synthase activity of PBP2a, and their location in a model structure suggests an activation mechanism for this enzyme that is shared with aPBPs from distantly related organisms with distinct activators.", "doi": "10.1128/mbio.02390-23", "pmid": "37847021", "labels": [], "xrefs": [{"db": "pmc", "key": "PMC10746261"}], "notes": [], "created": "2026-08-20T12:00:37.188Z", "modified": "2026-08-20T12:00:37.297Z"}, {"entity": "publication", "iuid": "427fd23a473f4521932a6b59e2d344af", "links": {"self": {"href": "https://publications-affiliated.scilifelab.se/publication/427fd23a473f4521932a6b59e2d344af.json"}, "display": {"href": "https://publications-affiliated.scilifelab.se/publication/427fd23a473f4521932a6b59e2d344af"}}, "title": "A distinctive family of L,D-transpeptidases catalyzing L-Ala-mDAP crosslinks in Alpha and Betaproteobacteria", "authors": [{"family": "Espaillat", "given": "Akbar", "initials": "A", "orcid": "0000-0003-0835-368X", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/70b05075063e4b0ebca0375644b5a4b6.json"}}, {"family": "Alvarez", "given": "Laura", "initials": "L", "orcid": "0000-0003-2429-7542", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/329d8b1460fe44789dbef53ea0493294.json"}}, {"family": "Torrens", "given": "Gabriel", "initials": "G", "orcid": "0000-0002-0450-1430", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/2a84794f089441ea8700f06f5a59fc2f.json"}}, {"family": "Beek", "given": "Josy ter", "initials": "Jt", "orcid": "0000-0003-4165-9277", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/b3d76493e80b4b57a951a0f94e6123ca.json"}}, {"family": "Miguel-Ruano", "given": "Vega", "initials": "V", "orcid": "0000-0002-2492-7164", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/4ee0be393f7b44f3aeb6c926d39dfac9.json"}}, {"family": "Irazoki", "given": "Oihane", "initials": "O", "orcid": "0000-0002-8896-7480", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/92d1aa46064a4ca1824bc91ffd7141c9.json"}}, {"family": "Gago", "given": "Federico", "initials": "F", "orcid": "0000-0002-3071-4878", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/2f4b917616c44f69acace2feeb97763d.json"}}, {"family": "Hermoso", "given": "Juan A", "initials": "JA", "orcid": "0000-0002-1862-8950", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/bb3d6a3d6ce34ce5a011f6036876cf69.json"}}, {"family": "Berntsson", "given": "Ronnie Per Arne", "initials": "RPA", "orcid": "0000-0001-6848-322X", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/cb9399248b784100a8020261949fb910.json"}}, {"family": "Cava", "given": "Felipe", "initials": "F", "orcid": "0000-0001-5995-718X", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/bbcff12a06814d54afea533e125a1213.json"}}], "type": "posted-content", "published": "2023-11-01", "journal": {"issn-l": null}, "abstract": null, "doi": "10.1101/2023.10.31.564931", "pmid": null, "labels": [], "xrefs": [], "notes": [], "created": "2026-08-20T10:48:43.639Z", "modified": "2026-08-20T10:49:16.855Z"}, {"entity": "publication", "iuid": "0a8add1340db46c8acdea6e91aa01ab1", "links": {"self": {"href": "https://publications-affiliated.scilifelab.se/publication/0a8add1340db46c8acdea6e91aa01ab1.json"}, "display": {"href": "https://publications-affiliated.scilifelab.se/publication/0a8add1340db46c8acdea6e91aa01ab1"}}, "title": "D-amino acids signal a stress-dependent run-away response in Vibrio cholerae.", "authors": [{"family": "Irazoki", "given": "Oihane", "initials": "O", "orcid": "0000-0002-8896-7480", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/92d1aa46064a4ca1824bc91ffd7141c9.json"}}, {"family": "Ter Beek", "given": "Josy", "initials": "J", "orcid": "0000-0003-4165-9277", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/b3d76493e80b4b57a951a0f94e6123ca.json"}}, {"family": "Alvarez", "given": "Laura", "initials": "L", "orcid": "0000-0003-2429-7542", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/329d8b1460fe44789dbef53ea0493294.json"}}, {"family": "Mateus", "given": "Andr\u00e9", "initials": "A", "orcid": "0000-0001-6870-0677", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/ebf0d242aa894a66b60828456bbc22aa.json"}}, {"family": "Colin", "given": "Remy", "initials": "R", "orcid": "0000-0001-9051-8003", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/48fcedae27254c06880cc48ad7276d9f.json"}}, {"family": "Typas", "given": "Athanasios", "initials": "A", "orcid": "0000-0002-0797-9018", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/d38ea7a531ad47cfa26df998f0e54dbe.json"}}, {"family": "Savitski", "given": "Mikhail M", "initials": "MM", "orcid": "0000-0003-2011-9247", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/374222bd4bce42f282690629b9679628.json"}}, {"family": "Sourjik", "given": "Victor", "initials": "V", "orcid": "0000-0003-1053-9192", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/d6aef6aa6af54827905ff16a446d27d0.json"}}, {"family": "Berntsson", "given": "Ronnie P-A", "initials": "RP", "orcid": "0000-0001-6848-322X", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/cb9399248b784100a8020261949fb910.json"}}, {"family": "Cava", "given": "Felipe", "initials": "F", "orcid": "0000-0001-5995-718X", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/bbcff12a06814d54afea533e125a1213.json"}}], "type": "journal article", "published": "2023-08-00", "journal": {"title": "Nat. Microbiol", "issn": "2058-5276", "volume": "8", "issue": "8", "pages": "1549-1560", "issn-l": "2058-5276"}, "abstract": "To explore favourable niches while avoiding threats, many bacteria use a chemotaxis navigation system. Despite decades of studies on chemotaxis, most signals and sensory proteins are still unknown. Many bacterial species release D-amino acids to the environment; however, their function remains largely unrecognized. Here we reveal that D-arginine and D-lysine are chemotactic repellent signals for the cholera pathogen Vibrio cholerae. These D-amino acids are sensed by a single chemoreceptor MCPDRK co-transcribed with the racemase enzyme that synthesizes them under the control of the stress-response sigma factor RpoS. Structural characterization of this chemoreceptor bound to either D-arginine or D-lysine allowed us to pinpoint the residues defining its specificity. Interestingly, the specificity for these D-amino acids appears to be restricted to those MCPDRK orthologues transcriptionally linked to the racemase. Our results suggest that D-amino acids can shape the biodiversity and structure of complex microbial communities under adverse conditions.", "doi": "10.1038/s41564-023-01419-6", "pmid": "37365341", "labels": [], "xrefs": [{"db": "pmc", "key": "PMC10390336"}, {"db": "pii", "key": "10.1038/s41564-023-01419-6"}], "notes": [], "created": "2026-08-20T08:55:21.117Z", "modified": "2026-08-20T08:55:21.397Z"}]}