{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Zhu S"],"funding":["NIDDK NIH HHS","Howard Hughes Medical Institute","NIAID NIH HHS","Wellcome Trust","NIGMS NIH HHS"],"pagination":["eabm9903"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC12091997"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["383(6686)"],"pubmed_abstract":["All living organisms deploy cell-autonomous defenses to combat infection. In plants and animals, large supramolecular complexes often activate immune proteins for protection. In this work, we resolved the native structure of a massive host-defense complex that polymerizes 30,000 guanylate-binding proteins (GBPs) over the surface of gram-negative bacteria inside human cells. Construction of this giant nanomachine took several minutes and remained stable for hours, required guanosine triphosphate hydrolysis, and recruited four GBPs plus caspase-4 and Gasdermin D as a cytokine and cell death immune signaling platform. Cryo-electron tomography suggests that GBP1 can adopt an extended conformation for bacterial membrane insertion to establish this platform, triggering lipopolysaccharide release"],"journal":["Science (New York, N.Y.)"],"pubmed_title":["Native architecture of a human GBP1 defense complex for cell-autonomous immunity to infection."],"pmcid":["PMC12091997"],"funding_grant_id":["R01 AI108834","R01 AI068041","203285/B/16/Z","P30 DK045735","R01 GM118486"],"pubmed_authors":["MacMicking JD","Bradfield CJ","Kim BH","Huang S","Maminska A","Park ES","Zhang Y","Bewersdorf J","Kumar P","Kim M","Zhu S"],"additional_accession":[]},"is_claimable":false,"name":"Native architecture of a human GBP1 defense complex for cell-autonomous immunity to infection.","description":"All living organisms deploy cell-autonomous defenses to combat infection. In plants and animals, large supramolecular complexes often activate immune proteins for protection. In this work, we resolved the native structure of a massive host-defense complex that polymerizes 30,000 guanylate-binding proteins (GBPs) over the surface of gram-negative bacteria inside human cells. Construction of this giant nanomachine took several minutes and remained stable for hours, required guanosine triphosphate hydrolysis, and recruited four GBPs plus caspase-4 and Gasdermin D as a cytokine and cell death immune signaling platform. Cryo-electron tomography suggests that GBP1 can adopt an extended conformation for bacterial membrane insertion to establish this platform, triggering lipopolysaccharide release","dates":{"release":"2024-01-01T00:00:00Z","publication":"2024 Mar","modification":"2026-06-01T06:19:47.311Z","creation":"2026-04-08T09:51:27.842Z"},"accession":"S-EPMC12091997","cross_references":{"pubmed":["38422126"],"doi":["10.1126/science.abm9903"]}}