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      The Astrovirus Capsid: A Review

      review-article
      1 , 2 , *
      Viruses
      MDPI
      astrovirus, capsid, antigen, structure, virus entry, virus exit

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          Abstract

          Astroviruses are enterically transmitted viruses that cause infections in mammalian and avian species. Astroviruses are nonenveloped, icosahedral viruses comprised of a capsid protein shell and a positive-sense, single-stranded RNA genome. The capsid protein undergoes dramatic proteolytic processing both inside and outside of the host cell, resulting in a coordinated maturation process that affects cellular localization, virus structure, and infectivity. After maturation, the capsid protein controls the initial phases of virus infection, including virus attachment, endocytosis, and genome release into the host cell. The astrovirus capsid is the target of host antibodies including virus-neutralizing antibodies. The capsid protein also mediates the binding of host complement proteins and inhibits complement activation. Here, we will review our knowledge on the astrovirus capsid protein (CP), with particular attention to the recent structural, biochemical, and virological studies that have advanced our understanding of the astrovirus life cycle.

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          Most cited references61

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          The PSIPRED protein structure prediction server.

          The PSIPRED protein structure prediction server allows users to submit a protein sequence, perform a prediction of their choice and receive the results of the prediction both textually via e-mail and graphically via the web. The user may select one of three prediction methods to apply to their sequence: PSIPRED, a highly accurate secondary structure prediction method; MEMSAT 2, a new version of a widely used transmembrane topology prediction method; or GenTHREADER, a sequence profile based fold recognition method. Freely available to non-commercial users at http://globin.bio.warwick.ac.uk/psipred/
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            Multistep entry of rotavirus into cells: a Versaillesque dance.

            Rotavirus entry into a cell is a complex multistep process in which different domains of the rotavirus surface proteins interact with different cell surface molecules, which act as attachment and entry receptors. These recently described molecules include several integrins and a heat shock protein, which have been found to be associated with cell membrane lipid microdomains. The requirement during viral entry for several cell molecules, which might be required to be present and organized in a precise fashion, could explain the selective cell and tissue tropism of these viruses. This review focuses on recent data describing the virus-receptor interactions, the role of lipid microdomains in rotavirus infection and the mechanism of rotavirus cell entry.
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              Structure of hepatitis E virion-sized particle reveals an RNA-dependent viral assembly pathway.

              Hepatitis E virus (HEV) induces acute hepatitis in humans with a high fatality rate in pregnant women. There is a need for anti-HEV research to understand the assembly process of HEV native capsid. Here, we produced a large virion-sized and a small T=1 capsid by expressing the HEV capsid protein in insect cells with and without the N-terminal 111 residues, respectively, for comparative structural analysis. The virion-sized capsid demonstrates a T=3 icosahedral lattice and contains RNA fragment in contrast to the RNA-free T=1 capsid. However, both capsids shared common decameric organization. The in vitro assembly further demonstrated that HEV capsid protein had the intrinsic ability to form decameric intermediate. Our data suggest that RNA binding is the extrinsic factor essential for the assembly of HEV native capsids.
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                Author and article information

                Contributors
                Role: Academic Editor
                Journal
                Viruses
                Viruses
                viruses
                Viruses
                MDPI
                1999-4915
                19 January 2017
                January 2017
                : 9
                : 1
                : 15
                Affiliations
                [1 ]Departamento de Genética del Desarrollo y Fisiología Molecular, Instituto de Biotecnología, Universidad Nacional Autónoma de México, Cuernavaca, Morelos 62210, Mexico; arias@ 123456ibt.unam.mx
                [2 ]Department of Biomolecular Engineering, University of California, Santa Cruz, CA 95064, USA
                Author notes
                [* ]Correspondence: rmdubois@ 123456ucsc.edu ; Tel.: +1-831-459-4833
                Article
                viruses-09-00015
                10.3390/v9010015
                5294984
                28106836
                d0308648-7b7f-4adb-90b6-239654cfc7cd
                © 2017 by the authors; licensee MDPI, Basel, Switzerland.

                This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC-BY) license ( http://creativecommons.org/licenses/by/4.0/).

                History
                : 02 December 2016
                : 12 January 2017
                Categories
                Review

                Microbiology & Virology
                astrovirus,capsid,antigen,structure,virus entry,virus exit
                Microbiology & Virology
                astrovirus, capsid, antigen, structure, virus entry, virus exit

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