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Cited by 96Viral gastroenteritis research and epidemiologyEnzyme Structure and FunctionAdvanced Electron Microscopy Techniques and Applications

Structure of Antibody-Neutralized Murine Norovirus and Unexpected Differences from Viruslike Particles

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Katpally, Umesh, Wobus, Christiane E., Dryden, Kelly, Virgin, Herbert W., Smith, Thomas J.·2008·Journal of Virology
DOI 10.1128/jvi.02200-07PMC PMC2258928
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Abstract

Noroviruses (family Caliciviridae ) are the major cause of epidemic nonbacterial gastroenteritis in humans, but the mechanism of antibody neutralization is unknown and no structure of an infectious virion has been reported. Murine norovirus (MNV) is the only norovirus that can be grown in tissue culture, studied in an animal model, and reverse engineered via an infectious clone and to which neutralizing antibodies have been isolated. Presented here are the cryoelectron microscopy structures of an MNV virion and the virion in complex with neutralizing Fab fragments. The most striking differences between MNV and previous calicivirus structures are that the protruding domain is lifted off the shell domain by ∼16Å and rotated ∼40° in a clockwise fashion and forms new interactions at the P1 base that create a cagelike structure engulfing the shell domains. Neutralizing Fab fragments cover the outer surface of each copy of the capsid protein P2 domains without causing any apparent conformational changes. These unique features of MNV suggest that at least some caliciviruses undergo a capsid maturation process akin to that observed with other plant and bacterial viruses.

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  • The P domains of vesivirus 2117, sapovirus and FCV appear to be raised off the S domain, as previously observed for RHDV and MuNV-1, in contrast to the P domains of NoV, which form a more collapsed conformation.

    “The P domains of vesivirus 2117, sapovirus and FCV appear to be raised off the S domain, as previously observed for RHDV and MuNV-1, in contrast to the P domains of NoV, which form a more collapsed conformation in relation to the S domain [33, 34].”

    From Vesivirus 2117 capsids more closely resemble sapovirus and lagovirus particles than other known vesivirus structures (2017) · cites this paper as [33]

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Authors
Katpally, U., Wobus, C. E., Dryden, K., Virgin, H. W., & Smith, T. J.
Affiliations
  • Donald Danforth Plant Science Center (US)
  • Washington University in St. Louis (US)
  • Scripps Research Institute (US)
Corresponding author
Smith, Thomas J.
ORCID
Venue
Journal of Virology
Publisher
American Society for Microbiology
Published
2008-03
Volume
82
Issue
5
Pages
2079-2088
ISSN
  • 0022-538X (ISSN-L)
  • 1098-5514
DOI
10.1128/jvi.02200-07
PMC
PMC2258928
OpenAlex
W2157947651
Cited by
96
References
0
Citations by year
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FWCI
4.40
Type
journal article
Language
en
Open access
Licence
journals.asm.org/non-commercial-tdm-license (tdm)
Locations
  • Journal of Virology (publishedVersion)
  • PubMed Central (publishedVersion)
  • PubMed (publishedVersion)
Funders
  • National Institutes of Health
  • National Cancer Institute (T32 CA09547, T32CA009547)
  • National Institute of General Medical Sciences (R01GM066087, GM 066087)
  • National Institute of Allergy and Infectious Diseases (R01AI054483, U54AI057160)
  • National Center for Research Resources (P41 RR17573, P41RR017573)
Topics
  • Health Sciences › Medicine › Infectious Diseases › Viral gastroenteritis research and epidemiology
  • Physical Sciences › Materials Science › Materials Chemistry › Enzyme Structure and Function
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Advanced Electron Microscopy Techniques and Applications
Keywords
murine norovirus, antibody neutralization, protruding domain, capsid maturation, virus-like particles, calicivirus, cryo-electron microscopy
MeSH terms
Amino Acid Sequence, Animals, Antibodies, Viral, Cell Line, Immunoglobulin Fab Fragments, Molecular Sequence Data, Neutralization Tests, Virion, Sequence Homology, Amino Acid, Cryoelectron Microscopy, Norovirus, Mice

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