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Structure and Assembly

Norwalk Virus Minor Capsid Protein VP2 Associates within the VP1 Shell Domain

Sompong Vongpunsawad, B. V. Venkataram Prasad, Mary K. Estes
Sompong Vongpunsawad
aDepartment of Molecular Virology and Microbiology, Baylor College of Medicine, Houston, Texas, USA
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B. V. Venkataram Prasad
aDepartment of Molecular Virology and Microbiology, Baylor College of Medicine, Houston, Texas, USA
bVerna and Marrs McLean Department of Biochemistry and Molecular Biology, Baylor College of Medicine, Houston, Texas, USA
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Mary K. Estes
aDepartment of Molecular Virology and Microbiology, Baylor College of Medicine, Houston, Texas, USA
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DOI: 10.1128/JVI.03508-12
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ABSTRACT

The major capsid protein of norovirus VP1 assembles to form an icosahedral viral particle. Despite evidence that the Norwalk virus (NV) minor structural protein VP2 is present in infectious virions, the available crystallographic and electron cryomicroscopy structures of NV have not revealed the location of VP2. In this study, we determined that VP1 associates with VP2 at the interior surface of the capsid, specifically with the shell (S) domain of VP1. We mapped the interaction site to amino acid 52 of VP1, an isoleucine located within a sequence motif IDPWI in the S domain that is highly conserved across norovirus genogroups. Mutation of this isoleucine abrogated VP2 incorporation into virus-like particles without affecting the ability for VP1 to dimerize and form particles. The highly basic nature of VP2 and its location interior to the viral particle are consistent with its potential role in assisting capsid assembly and genome encapsidation.

  • Copyright © 2013, American Society for Microbiology. All Rights Reserved.
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Norwalk Virus Minor Capsid Protein VP2 Associates within the VP1 Shell Domain
Sompong Vongpunsawad, B. V. Venkataram Prasad, Mary K. Estes
Journal of Virology Apr 2013, 87 (9) 4818-4825; DOI: 10.1128/JVI.03508-12

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Norwalk Virus Minor Capsid Protein VP2 Associates within the VP1 Shell Domain
Sompong Vongpunsawad, B. V. Venkataram Prasad, Mary K. Estes
Journal of Virology Apr 2013, 87 (9) 4818-4825; DOI: 10.1128/JVI.03508-12
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