Structural Analyses of the GI.4 Norovirus by Cryo-electron Microscopy and X-ray Crystallography Revealing Binding Sites for Human Monoclonal Antibodies

Overview

Journal J Virol

Publisher American Society for Microbiology

Date 2024 Apr 9

PMID 38593321

Authors

Tomomi Kimura-Someya

Kazushige Katsura

Miyuki Kato-Murayama

Toshiaki Hosaka

Tomomi Uchikubo-Kamo

Kentaro Ihara

Kazuharu Hanada

Shin Sato

Kazutaka Murayama

Michiyo Kataoka

Mikako Shirouzu

Yuichi Someya

Affiliations

Soon will be listed here.

Abstract

Importance: We conducted the structural analyses of the VP1 protein from the GI.4 Chiba norovirus to identify the binding sites of the previously isolated human monoclonal antibodies CV-1A1 and CV-2F5. The cryo-electron microscopy of the Chiba virus-like particles (VLPs) complexed with the Fv-clasp forms of GI.4-specific CV-1A1 revealed that this antibody binds to the highly variable P2 subdomain, suggesting that this antibody may have neutralizing ability against the GI.4 strains. X-ray crystallography revealed that the CV-2F5 antibody bound to the P1 subdomain, which is rich in conserved amino acids. This result is consistent with the ability of the CV-2F5 antibody to react with a wide variety of GI norovirus strains. It is also found that the CV-2F5 antibody caused a disruption of VLPs. Our findings, together with previous reports on the structures of VP1 proteins and VLPs, are expected to open a path for the structure-based development of antivirals and vaccines against norovirus disease.

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