{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Petrlova J"],"funding":["Alfred Österlunds Stiftelse","Crafoordska Stiftelsen","Vetenskapsrådet","LEO Foundation","Torsten Söderbergs Stiftelse","Petrus och Augusta Hedlunds Stiftelse","Greta och Johan Kocks stiftelser"],"pagination":["2566-2575"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9538650"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["596(19)"],"pubmed_abstract":["SARS-CoV-2 spike (S) protein is crucial for virus invasion in COVID-19. Here, we showed that lipopolysaccharide (LPS) can trigger S protein aggregation at high doses of LPS and S protein. We demonstrated the formation of S protein aggregates by microscopy analyses, aggregation and gel shift assays. LPS at high levels boosts the formation of S protein aggregates as detected by amytracker and thioflavin T dyes that specifically bind to aggregating proteins. We validated the role of LPS by blocking the formation of aggregates by the endotoxin-scavenging thrombin-derived peptide TCP-25. Aggregation-prone sequences in S protein are predicted to be nearby LPS binding sites, while molecular simulations showed stable formation of S protein-LPS higher-order oligomers. Collectively, our results provide evidence of LPS-induced S protein aggregation."],"journal":["FEBS letters"],"pubmed_title":["SARS-CoV-2 spike protein aggregation is triggered by bacterial lipopolysaccharide."],"pmcid":["PMC9538650"],"funding_grant_id":["LF-OC-20-000435","2017‐02341","2020‐02016"],"pubmed_authors":["Bond PJ","Samsudin F","Petrlova J","Schmidtchen A"],"additional_accession":[]},"is_claimable":false,"name":"SARS-CoV-2 spike protein aggregation is triggered by bacterial lipopolysaccharide.","description":"SARS-CoV-2 spike (S) protein is crucial for virus invasion in COVID-19. Here, we showed that lipopolysaccharide (LPS) can trigger S protein aggregation at high doses of LPS and S protein. We demonstrated the formation of S protein aggregates by microscopy analyses, aggregation and gel shift assays. LPS at high levels boosts the formation of S protein aggregates as detected by amytracker and thioflavin T dyes that specifically bind to aggregating proteins. We validated the role of LPS by blocking the formation of aggregates by the endotoxin-scavenging thrombin-derived peptide TCP-25. Aggregation-prone sequences in S protein are predicted to be nearby LPS binding sites, while molecular simulations showed stable formation of S protein-LPS higher-order oligomers. Collectively, our results provide evidence of LPS-induced S protein aggregation.","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022 Oct","modification":"2025-04-04T22:32:45.222Z","creation":"2025-02-19T03:23:05.587Z"},"accession":"S-EPMC9538650","cross_references":{"pubmed":["36050806"],"doi":["10.1002/1873-3468.14490"]}}