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      The structural biology of PRRSV

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          Research highlights

          ▶ Crystal structures of PRRSV proteases reveal domains that may be involved in modulation of host functions. ▶ The PRRSV N protein dimerization domain has a fold only seen in nidovirus nucleocapsid proteins. ▶ The PRRSV virion is a rounded or oval enveloped particle with a smooth outer surface and a hollow, double-layered core. ▶ The PRRSV nucleocapsid has an asymmetric, linear organization, similar to the coronaviruses.

          Abstract

          Porcine reproductive and respiratory syndrome virus (PRRSV) is an enveloped, positive-sense single-stranded RNA virus belonging to the Arteriviridae family. Arteriviruses and coronaviruses are grouped together in the order Nidovirales, based on similarities in genome organization and expression strategy. Over the past decade, crystal structures of several viral proteins, electron microscopic studies of the virion, as well as biochemical and in vivo studies on protein–protein interactions have led to a greatly increased understanding of PRRSV structural biology. At this point, crystal structures are available for the viral proteases NSP1α, NSP1β and NSP4 and the nucleocapsid protein, N. The NSP1α and NSP1β structures have revealed additional non-protease domains that may be involved in modulation of host functions. The N protein forms a dimer with a novel fold so far only seen in PRRSV and other nidoviruses. Cryo-electron tomographic studies have shown the three-dimensional organization of the PRRSV virion and suggest that the viral nucleocapsid has an asymmetric, linear arrangement, rather than the isometric core previously described. Together, these studies have revealed a closer structural relationship between arteri- and coronaviruses than previously anticipated.

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          Most cited references117

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          Nidovirales: a new order comprising Coronaviridae and Arteriviridae.

          D Cavanagh (1997)
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            The molecular biology of arteriviruses.

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              Severe acute respiratory syndrome coronavirus papain-like protease: structure of a viral deubiquitinating enzyme.

              Replication of severe acute respiratory syndrome (SARS) coronavirus (SARS-CoV) requires proteolytic processing of the replicase polyprotein by two viral cysteine proteases, a chymotrypsin-like protease (3CLpro) and a papain-like protease (PLpro). These proteases are important targets for development of antiviral drugs that would inhibit viral replication and reduce mortality associated with outbreaks of SARS-CoV. In this work, we describe the 1.85-A crystal structure of the catalytic core of SARS-CoV PLpro and show that the overall architecture adopts a fold closely resembling that of known deubiquitinating enzymes. Key features, however, distinguish PLpro from characterized deubiquitinating enzymes, including an intact zinc-binding motif, an unobstructed catalytically competent active site, and the presence of an intriguing, ubiquitin-like N-terminal domain. To gain insight into the active-site recognition of the C-terminal tail of ubiquitin and the related LXGG motif, we propose a model of PLpro in complex with ubiquitin-aldehyde that reveals well defined sites within the catalytic cleft that help to account for strict substrate-recognition motifs.
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                Author and article information

                Contributors
                Journal
                Virus Res
                Virus Res
                Virus Research
                Elsevier B.V.
                0168-1702
                1872-7492
                6 August 2010
                December 2010
                6 August 2010
                : 154
                : 1
                : 86-97
                Affiliations
                Department of Microbiology, University of Alabama at Birmingham, Birmingham, AL, United States
                Author notes
                [* ]845 19th St South, BBRB 311, Birmingham, AL 35242, United States. Tel.: +1 205 996 4502; fax: +1 205 996 2667. dokland@ 123456uab.edu
                Article
                S0168-1702(10)00275-3
                10.1016/j.virusres.2010.07.029
                7114433
                20692304
                f60c871b-f243-4f83-8c8d-8f814fb3fdc8
                Copyright © 2010 Elsevier B.V. All rights reserved.

                Since January 2020 Elsevier has created a COVID-19 resource centre with free information in English and Mandarin on the novel coronavirus COVID-19. The COVID-19 resource centre is hosted on Elsevier Connect, the company's public news and information website. Elsevier hereby grants permission to make all its COVID-19-related research that is available on the COVID-19 resource centre - including this research content - immediately available in PubMed Central and other publicly funded repositories, such as the WHO COVID database with rights for unrestricted research re-use and analyses in any form or by any means with acknowledgement of the original source. These permissions are granted for free by Elsevier for as long as the COVID-19 resource centre remains active.

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                Categories
                Article

                Microbiology & Virology
                eav, equine arteritis virus,em, electron microscopy,fmdv, food-and-mouth disease virus,gp, glycoprotein,ldv, lactate dehydrogenase-elevating virus,lv, lelystad virus,mhv, murine hepatitis virus,nsp, non-structural protein,orf, open reading frame,prrsv, porcine reproductive and respiratory syndrome virus,sars-cov, severe acute respiratory syndrome coronavirus,shfv, simian hemorrhagic fever virus,tm, transmembrane,vlp, virus-like particle,cryo-electron microscopy,envelope protein,nidovirus,nucleocapsid,virion,structure

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