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TitleNative architecture of a human GBP1 defense complex for cell-autonomous immunity to infection.
Journal, issue, pagesScience, Vol. 383, Issue 6686, Page eabm9903, Year 2024
Publish dateMar 1, 2024
AuthorsShiwei Zhu / Clinton J Bradfield / Agnieszka Maminska / Eui-Soon Park / Bae-Hoon Kim / Pradeep Kumar / Shuai Huang / Minjeong Kim / Yongdeng Zhang / Joerg Bewersdorf / John D MacMicking /
PubMed AbstractAll 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 ...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 that activated coassembled caspase-4. Our "open conformer" model provides a dynamic view into how the human GBP1 defense complex mobilizes innate immunity to infection.
External linksScience / PubMed:38422126
MethodsEM (subtomogram averaging)
Resolution9.7 - 17.0 Å
Structure data

EMDB-43091: hGBP1 conformer on the bacterial outer membrane
Method: EM (subtomogram averaging) / Resolution: 17.0 Å

EMDB-43153: hGBP1 conformer on the bacterial outer membrane
Method: EM (subtomogram averaging) / Resolution: 9.7 Å

Source
  • Salmonella enterica subsp. enterica serovar Typhimurium (bacteria)
  • Homo sapiens (human)

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