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The Dynamic Capsid Structures of the Noroviruses

Department of Biochemistry and Molecular Biology, University of Texas Medical Branch at Galveston, 301 University Boulevard, Galveston, TX 77555-0645, USA
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Viruses 2019, 11(3), 235; https://doi.org/10.3390/v11030235
Received: 30 January 2019 / Revised: 1 March 2019 / Accepted: 3 March 2019 / Published: 8 March 2019
(This article belongs to the Special Issue Noroviruses)
Noroviruses are responsible for almost a fifth of all cases of gastroenteritis worldwide. New strains evolve every 2–4 years by escaping herd immunity and cause worldwide epidemics. In the US alone, noroviruses are responsible for ~20 million cases and more than 70,000 hospitalizations of infected children, annually. Efforts towards a vaccine have been hindered by a lack of detailed structural information about antibody binding and the mechanisms of antibody escape. Caliciviruses have 180 copies of the major capsid protein (VP1; ~58 kDa), that is divided into the N-terminus (N), the shell (S) and C-terminal protruding (P) domains. The S domain forms a shell around the viral RNA genome, while the P domains dimerize to form protrusions on the capsid surface. The P domain is subdivided into P1 and P2 subdomains, with the latter containing the binding sites for cellular receptors and neutralizing antibodies. There is increasing evidence that these viruses are extremely dynamic and this flexibility is critical for viral replication. There are at least two modes of flexibility; the entire P domain relative to the shell and within the P domain itself. Here, the details and possible roles for this remarkable flexibility will be reviewed. View Full-Text
Keywords: caliciviruses; antibody neutralization; dynamics; viral receptors caliciviruses; antibody neutralization; dynamics; viral receptors
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Smith, H.Q.; Smith, T.J. The Dynamic Capsid Structures of the Noroviruses. Viruses 2019, 11, 235.

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