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TitleA broadly protective human antibody for GI genogroup noroviruses.
Journal, issue, pagesNat Microbiol, Vol. 10, Issue 5, Page 1227-1239, Year 2025
Publish dateApr 10, 2025
AuthorsInga Rimkute / Adam S Olia / Mehin Suleiman / Kamron D Woods / Tatsiana Bylund / Nicholas C Morano / Ena S Tully / Raffaello Verardi / Saran Bao / Margaret H Beddall / Natthawan Chaimongkol / Mitzi M Donaldson / Renguang Du / Caitlyn N M Dulan / Jason Gorman / Amy R Henry / Chaim A Schramm / Stanislav V Sosnovtsev / Tyler Stephens / John-Paul Todd / Yaroslav Tsybovsky / Daniel C Douek / Kim Y Green / Reda Rawi / Lawrence Shapiro / Tongqing Zhou / Peter D Kwong / Mario Roederer /
PubMed AbstractNoroviruses infect millions each year, and while effective countermeasures are eagerly sought, none have been reported for the GI genogroup, first described more than 50 years ago. Here, to provide ...Noroviruses infect millions each year, and while effective countermeasures are eagerly sought, none have been reported for the GI genogroup, first described more than 50 years ago. Here, to provide insight into GI norovirus neutralization, we isolated a broad GI antibody, 16E10, from a human blood donor and showed it neutralizes noroviruses in human enteroid cultures and abrogates or reduces infection in rhesus macaques. The cryogenic electron microscopy reconstruction of 16E10 with a norovirus protruding-domain dimer at 2.56-Å resolution reveals an exceptionally large binding surface, overlapping an antibody supersite, distal from host receptor-binding or cofactor-binding sites. Cryogenic electron microscopy reconstructions with virus-like particles (VLPs) showed that 16E10 disrupts protruding domains on the VLP surface and disassembles VLPs, altering viral organization required for avidity. While its epitope was generally conserved, 16E10 recognized multiple sequence-divergent residues, binding to which was enabled by corresponding cavities in the 16E10-norovirus interface. Broad recognition of noroviruses can thus incorporate sequence-divergent residues, through a cavity-based mechanism of diversity tolerance.
External linksNat Microbiol / PubMed:40211068
MethodsEM (single particle)
Resolution2.32 - 3.03 Å
Structure data

EMDB-44672: GI.1 DS1 virus-like particle
Method: EM (single particle) / Resolution: 3.03 Å

EMDB-44673: Norovirus GI.1 VLP bound to 16E10 Fab
Method: EM (single particle) / Resolution: 2.32 Å

44734

9bof

EMDB-44734, PDB-9bof:
16E10 Fab bound to norovirus GI.1 P domain
Method: EM (single particle) / Resolution: 2.61 Å

Source
  • norovirus
  • homo sapiens (human)
KeywordsVIRAL PROTEIN/IMMUNE SYSTEM / norovirus / VP1 / P-domain / antibody / VIRAL PROTEIN / VIRAL PROTEIN-IMMUNE SYSTEM complex

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