{"entity": "researcher", "timestamp": "2026-08-20T21:02:02.631Z", "family": "Torrens", "given": "Gabriel", "initials": "G", "orcid": "0000-0002-0450-1430", "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."], "links": {"self": {"href": "https://publications-affiliated.scilifelab.se/researcher/2a84794f089441ea8700f06f5a59fc2f.json"}, "display": {"href": "https://publications-affiliated.scilifelab.se/researcher/2a84794f089441ea8700f06f5a59fc2f"}}, "publications": [{"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": "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": "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": "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": "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"}]}