{"entity": "journal", "iuid": "c0237251ccce480cb1607e78afe525f3", "timestamp": "2026-04-13T05:03:00.637Z", "links": {"self": {"href": "https://publications-affiliated.scilifelab.se/journal/Biochim%20Biophys%20Acta%20Biomembr.json"}, "display": {"href": "https://publications-affiliated.scilifelab.se/journal/Biochim%20Biophys%20Acta%20Biomembr"}}, "title": "Biochim Biophys Acta Biomembr", "issn": "1879-2642", "issn-l": "0005-2736", "publications_count": 3, "publications": [{"entity": "publication", "iuid": "16035be637ad4f55acfb77aacc09f124", "links": {"self": {"href": "https://publications-affiliated.scilifelab.se/publication/16035be637ad4f55acfb77aacc09f124.json"}, "display": {"href": "https://publications-affiliated.scilifelab.se/publication/16035be637ad4f55acfb77aacc09f124"}}, "title": "Probing effects of the SARS-CoV-2 E protein on membrane curvature and intracellular calcium.", "authors": [{"family": "Mehregan", "given": "Aujan", "initials": "A", "orcid": "0000-0001-6103-9572", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/0697bac9fd74496584d1850583794132.json"}}, {"family": "P\u00e9rez-Conesa", "given": "Sergio", "initials": "S", "orcid": "0000-0003-1951-2543", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/656db9d5b4eb4e9892dc39f0914b54a6.json"}}, {"family": "Zhuang", "given": "Yuxuan", "initials": "Y", "orcid": "0000-0003-4390-8556", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/61b8327a0f32416686748c52c38ecbf1.json"}}, {"family": "Elbahnsi", "given": "Ahmad", "initials": "A", "orcid": "0000-0002-5356-2440", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/41210b79b83845c79978e32dce118123.json"}}, {"family": "Pasini", "given": "Diletta", "initials": "D"}, {"family": "Lindahl", "given": "Erik", "initials": "E", "orcid": "0000-0002-2734-2794", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/9eb30fa60f9b4b95842ac9d9f3a0eaa9.json"}}, {"family": "Howard", "given": "Rebecca J", "initials": "RJ", "orcid": "0000-0003-2049-3378", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/5ce04593b5b24aaa8978fda1447dd0bf.json"}}, {"family": "Ulens", "given": "Chris", "initials": "C", "orcid": "0000-0002-8202-5281", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/d4d8b8899a354e0cae54b3ebeb9b7540.json"}}, {"family": "Delemotte", "given": "Lucie", "initials": "L", "orcid": "0000-0002-0828-3899", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/87eaf619d7bd487ebdbe68c46b827e66.json"}}], "type": "journal article", "published": "2022-10-01", "journal": {"title": "Biochim Biophys Acta Biomembr", "issn": "1879-2642", "issn-l": "0005-2736", "volume": "1864", "issue": "10", "pages": "183994"}, "abstract": "SARS-CoV-2 contains four structural proteins in its genome. These proteins aid in the assembly and budding of new virions at the ER-Golgi intermediate compartment (ERGIC). Current fundamental research efforts largely focus on one of these proteins - the spike (S) protein. Since successful antiviral therapies are likely to target multiple viral components, there is considerable interest in understanding the biophysical role of its other structural proteins, in particular structural membrane proteins. Here, we have focused our efforts on the characterization of the full-length envelope (E) protein from SARS-CoV-2, combining experimental and computational approaches. Recombinant expression of the full-length E protein from SARS-CoV-2 reveals that this membrane protein is capable of independent multimerization, possibly as a tetrameric or smaller species. Fluorescence microscopy shows that the protein localizes intracellularly, and coarse-grained MD simulations indicate it causes bending of the surrounding lipid bilayer, corroborating a potential role for the E protein in viral budding. Although we did not find robust electrophysiological evidence of ion-channel activity, cells transfected with the E protein exhibited reduced intracellular Ca2+, which may further promote viral replication. However, our atomistic MD simulations revealed that previous NMR structures are relatively unstable, and result in models incapable of ion conduction. Our study highlights the importance of using high-resolution structural data obtained from a full-length protein to gain detailed molecular insights, and eventually permitting virtual drug screening.", "doi": "10.1016/j.bbamem.2022.183994", "pmid": "35724739", "labels": {"Lucie Delemotte": null, "SciLifeLab Fellow": null}, "xrefs": [{"db": "pmc", "key": "PMC9212275"}, {"db": "pii", "key": "S0005-2736(22)00132-8"}], "notes": [], "created": "2021-12-08T08:12:46.454Z", "modified": "2023-05-15T08:04:06.223Z"}, {"entity": "publication", "iuid": "fbdc640286a848018fea262bfba4f1ce", "links": {"self": {"href": "https://publications-affiliated.scilifelab.se/publication/fbdc640286a848018fea262bfba4f1ce.json"}, "display": {"href": "https://publications-affiliated.scilifelab.se/publication/fbdc640286a848018fea262bfba4f1ce"}}, "title": "Giant plasma membrane vesicles to study plasma membrane structure and dynamics.", "authors": [{"family": "Sezgin", "given": "Erdinc", "initials": "E"}], "type": "journal article", "published": "2022-04-01", "journal": {"title": "Biochim Biophys Acta Biomembr", "issn": "1879-2642", "volume": "1864", "issue": "4", "pages": "183857", "issn-l": "0005-2736"}, "abstract": "The plasma membrane (PM) is a highly heterogenous structure intertwined with the cortical actin cytoskeleton and extracellular matrix. This complex architecture makes it difficult to study the processes taking place at the PM. Model membrane systems that are simple mimics of the PM overcome this bottleneck and allow us to study the biophysical principles underlying the processes at the PM. Among them, cell-derived giant plasma membrane vesicles (GPMVs) are considered the most physiologically relevant system, retaining the compositional complexity of the PM to a large extent. GPMVs have become a key tool in membrane research in the last few years. In this review, I will provide a brief overview of this system, summarize recent applications and discuss the limitations.", "doi": "10.1016/j.bbamem.2021.183857", "pmid": "34990591", "labels": {"SciLifeLab Fellow": null, "Erdinc Sezgin": null}, "xrefs": [{"db": "pii", "key": "S0005-2736(21)00306-0"}], "notes": [], "created": "2022-12-01T12:41:16.081Z", "modified": "2022-12-01T12:41:16.096Z"}, {"entity": "publication", "iuid": "e6dc8e7ef56d4350a71965c238d55dd8", "links": {"self": {"href": "https://publications-affiliated.scilifelab.se/publication/e6dc8e7ef56d4350a71965c238d55dd8.json"}, "display": {"href": "https://publications-affiliated.scilifelab.se/publication/e6dc8e7ef56d4350a71965c238d55dd8"}}, "title": "How to minimize dye-induced perturbations while studying biomembrane structure and dynamics: PEG linkers as a rational alternative.", "authors": [{"family": "Mobarak", "given": "Edouard", "initials": "E"}, {"family": "Javanainen", "given": "Matti", "initials": "M"}, {"family": "Kulig", "given": "Waldemar", "initials": "W"}, {"family": "Honigmann", "given": "Alf", "initials": "A"}, {"family": "Sezgin", "given": "Erdinc", "initials": "E"}, {"family": "Aho", "given": "Noora", "initials": "N"}, {"family": "Eggeling", "given": "Christian", "initials": "C"}, {"family": "Rog", "given": "Tomasz", "initials": "T"}, {"family": "Vattulainen", "given": "Ilpo", "initials": "I"}], "type": "journal article", "published": "2018-11-00", "journal": {"title": "Biochim Biophys Acta Biomembr", "issn": "1879-2642", "volume": "1860", "issue": "11", "pages": "2436-2445", "issn-l": "0005-2736"}, "abstract": "Organic dye-tagged lipid analogs are essential for many fluorescence-based investigations of complex membrane structures, especially when using advanced microscopy approaches. However, lipid analogs may interfere with membrane structure and dynamics, and it is not obvious that the properties of lipid analogs would match those of non-labeled host lipids. In this work, we bridged atomistic simulations with super-resolution imaging experiments and biomimetic membranes to assess the performance of commonly used sphingomyelin-based lipid analogs. The objective was to compare, on equal footing, the relative strengths and weaknesses of acyl chain labeling, headgroup labeling, and labeling based on poly-ethyl-glycol (PEG) linkers in determining biomembrane properties. We observed that the most appropriate strategy to minimize dye-induced membrane perturbations and to allow consideration of Brownian-like diffusion in liquid-ordered membrane environments is to decouple the dye from a membrane by a PEG linker attached to a lipid headgroup. Yet, while the use of PEG linkers may sound a rational and even an obvious approach to explore membrane dynamics, the results also suggest that the dyes exploiting PEG linkers interfere with molecular interactions and their dynamics. Overall, the results highlight the great care needed when using fluorescent lipid analogs, in particular accurate controls.", "doi": "10.1016/j.bbamem.2018.07.003", "pmid": "30028957", "labels": {"Erdinc Sezgin": null, "SciLifeLab Fellow": null}, "xrefs": [{"db": "pii", "key": "S0005-2736(18)30198-6"}], "notes": [], "created": "2020-09-28T08:55:06.709Z", "modified": "2022-11-07T11:31:19.105Z"}], "created": "2020-09-28T08:55:06.721Z", "modified": "2020-11-27T13:12:58.062Z"}