Atomic structure of the predominant GII.4 human norovirus capsid reveals novel stability and plasticity

Liya Hu; Wilhelm Salmen; Rong Chen; Yi Zhou; Frederick Neill; James E. Crowe; Robert L. Atmar; Mary K. Estes; B. V. Venkataram Prasad

doi:10.1038/s41467-022-28757-z

Nature Communications (Mar 2022)

Atomic structure of the predominant GII.4 human norovirus capsid reveals novel stability and plasticity

Liya Hu,
Wilhelm Salmen,
Rong Chen,
Yi Zhou,
Frederick Neill,
James E. Crowe,
Robert L. Atmar,
Mary K. Estes,
B. V. Venkataram Prasad

Affiliations

Liya Hu: Verna and Marrs McLean Department of Biochemistry and Molecular Biology, Baylor College of Medicine
Wilhelm Salmen: Department of Molecular Virology and Microbiology, Baylor College of Medicine
Rong Chen: Verna and Marrs McLean Department of Biochemistry and Molecular Biology, Baylor College of Medicine
Yi Zhou: Verna and Marrs McLean Department of Biochemistry and Molecular Biology, Baylor College of Medicine
Frederick Neill: Department of Molecular Virology and Microbiology, Baylor College of Medicine
James E. Crowe: The Vanderbilt Vaccine Center, Vanderbilt University Medical Center
Robert L. Atmar: Department of Molecular Virology and Microbiology, Baylor College of Medicine
Mary K. Estes: Department of Molecular Virology and Microbiology, Baylor College of Medicine
B. V. Venkataram Prasad: Verna and Marrs McLean Department of Biochemistry and Molecular Biology, Baylor College of Medicine

DOI: https://doi.org/10.1038/s41467-022-28757-z
Journal volume & issue: Vol. 13, no. 1
pp. 1 – 14

Abstract

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GII.4 variants of human noroviruses cause pandemic viral gastroenteritis. The atomic structure of GII.4 virus-like particles reveal novel insights into capsid stability, dynamics and antigenic presentation potentially useful for ongoing vaccine development.

Published in Nature Communications

ISSN: 2041-1723 (Online)
Publisher: Nature Portfolio
Country of publisher: United Kingdom
LCC subjects: Science
Website: https://www.nature.com/ncomms/

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