Sialic acids as receptor determinants for coronaviruses
Identifieur interne : 000729 ( Istex/Corpus ); précédent : 000728; suivant : 000730Sialic acids as receptor determinants for coronaviruses
Auteurs : Christel Schwegmann-We Els ; Georg HerrlerSource :
- Glycoconjugate Journal [ 0282-0080 ] ; 2006-02-01.
English descriptors
Abstract
Abstract: Among coronaviruses, several members are able to interact with sialic acids. For bovine coronavirus (BCoV) and related viruses, binding to cell surface components containing N-acetyl-9- O-acetylneuraminic acid is essential for initiation of an infection. These viruses resemble influenza C viruses because they share not only the receptor determinant, but also the presence of an acetylesterase that releases the 9- O-acetyl group from sialic acid and thus abolishes the ability of the respective sialoglycoconjugate to function as a receptor for BCoV. As in the case of influenza viruses, the receptor-destroying enzyme of BCoV is believed to facilitate the spread of virus infection by removing receptor determinants from the surface of infected cells and by preventing the formation of virus aggregates. Another coronavirus, porcine transmissible gastroenteritis virus (TGEV) preferentially recognizes N-glycolylneuraminic acid. TGEV does not contain a receptor-destroying enzyme and does not depend on the sialic acid binding activity for infection of cultured cells. However, binding to sialic acids is required for the enteropathogenicity of TGEV. Interaction with sialoglycoconjugates may help the virus to pass through the sialic acid-rich mucus layer that covers the viral target cells in the epithelium of the small intestine. We discuss that the BCoV group of viruses may have evolved from a TGEV-like ancestor by acquiring an acetylesterase gene through heterologous recombination.
Url:
DOI: 10.1007/s10719-006-5437-9
Links to Exploration step
ISTEX:42568732A10B1148F141B13AEA1634BEFD14EC0ALe document en format XML
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For bovine coronavirus (BCoV) and related viruses, binding to cell surface components containing N-acetyl-9- O-acetylneuraminic acid is essential for initiation of an infection. These viruses resemble influenza C viruses because they share not only the receptor determinant, but also the presence of an acetylesterase that releases the 9- O-acetyl group from sialic acid and thus abolishes the ability of the respective sialoglycoconjugate to function as a receptor for BCoV. As in the case of influenza viruses, the receptor-destroying enzyme of BCoV is believed to facilitate the spread of virus infection by removing receptor determinants from the surface of infected cells and by preventing the formation of virus aggregates. Another coronavirus, porcine transmissible gastroenteritis virus (TGEV) preferentially recognizes N-glycolylneuraminic acid. TGEV does not contain a receptor-destroying enzyme and does not depend on the sialic acid binding activity for infection of cultured cells. However, binding to sialic acids is required for the enteropathogenicity of TGEV. Interaction with sialoglycoconjugates may help the virus to pass through the sialic acid-rich mucus layer that covers the viral target cells in the epithelium of the small intestine. We discuss that the BCoV group of viruses may have evolved from a TGEV-like ancestor by acquiring an acetylesterase gene through heterologous recombination.</div></front></TEI><istex><corpusName>springer-journals</corpusName><author><json:item><name>Christel Schwegmann-Weßels</name><affiliations><json:string>Institut für Virologie, Stiftung Tierärztliche Hochschule Hannover, Bünteweg 17, 30559, Hannover, Germany</json:string></affiliations></json:item><json:item><name>Georg Herrler</name><affiliations><json:string>Institut für Virologie, Stiftung Tierärztliche Hochschule Hannover, Bünteweg 17, 30559, Hannover, Germany</json:string><json:string>E-mail: Georg.Herrler@tiho-hannover.de</json:string></affiliations></json:item></author><subject><json:item><lang><json:string>eng</json:string></lang><value>Coronavirus</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>Receptor</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>Sialic acid</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>N-glycolyl-neuraminic acid</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>N-acetyl-neuraminic acid</value></json:item></subject><articleId><json:string>5437</json:string><json:string>NO00005437</json:string></articleId><arkIstex>ark:/67375/VQC-G9Z00D2X-C</arkIstex><language><json:string>eng</json:string></language><originalGenre><json:string>ReviewPaper</json:string></originalGenre><abstract>Abstract: Among coronaviruses, several members are able to interact with sialic acids. For bovine coronavirus (BCoV) and related viruses, binding to cell surface components containing N-acetyl-9- O-acetylneuraminic acid is essential for initiation of an infection. These viruses resemble influenza C viruses because they share not only the receptor determinant, but also the presence of an acetylesterase that releases the 9- O-acetyl group from sialic acid and thus abolishes the ability of the respective sialoglycoconjugate to function as a receptor for BCoV. As in the case of influenza viruses, the receptor-destroying enzyme of BCoV is believed to facilitate the spread of virus infection by removing receptor determinants from the surface of infected cells and by preventing the formation of virus aggregates. Another coronavirus, porcine transmissible gastroenteritis virus (TGEV) preferentially recognizes N-glycolylneuraminic acid. TGEV does not contain a receptor-destroying enzyme and does not depend on the sialic acid binding activity for infection of cultured cells. However, binding to sialic acids is required for the enteropathogenicity of TGEV. Interaction with sialoglycoconjugates may help the virus to pass through the sialic acid-rich mucus layer that covers the viral target cells in the epithelium of the small intestine. 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However, binding to sialic acids is required for the enteropathogenicity of TGEV. Interaction with sialoglycoconjugates may help the virus to pass through the sialic acid-rich mucus layer that covers the viral target cells in the epithelium of the small intestine. 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Review</ArticleCategory><ArticleFirstPage>51</ArticleFirstPage><ArticleLastPage>58</ArticleLastPage><ArticleHistory><RegistrationDate><Year>2006</Year><Month>1</Month><Day>1</Day></RegistrationDate></ArticleHistory><ArticleCopyright><CopyrightHolderName>Springer Science + Business Media, LLC</CopyrightHolderName><CopyrightYear>2006</CopyrightYear></ArticleCopyright><ArticleGrants Type="Regular"><MetadataGrant Grant="OpenAccess"></MetadataGrant><AbstractGrant Grant="OpenAccess"></AbstractGrant><BodyPDFGrant Grant="Restricted"></BodyPDFGrant><BodyHTMLGrant Grant="Restricted"></BodyHTMLGrant><BibliographyGrant Grant="Restricted"></BibliographyGrant><ESMGrant Grant="Restricted"></ESMGrant></ArticleGrants></ArticleInfo><ArticleHeader><AuthorGroup><Author AffiliationIDS="Aff1" CorrespondingAffiliationID="Aff1"><AuthorName DisplayOrder="Western"><GivenName>Christel</GivenName><FamilyName>Schwegmann-Weßels</FamilyName></AuthorName></Author><Author AffiliationIDS="Aff1"><AuthorName DisplayOrder="Western"><GivenName>Georg</GivenName><FamilyName>Herrler</FamilyName></AuthorName><Contact><Phone>+49-511-953-8857</Phone><Fax>+49-511-953-8898</Fax><Email>Georg.Herrler@tiho-hannover.de</Email></Contact></Author><Affiliation ID="Aff1"><OrgDivision>Institut für Virologie</OrgDivision><OrgName>Stiftung Tierärztliche Hochschule Hannover</OrgName><OrgAddress><Street>Bünteweg 17</Street><Postcode>30559</Postcode><City>Hannover</City><Country Code="DE">Germany</Country></OrgAddress></Affiliation></AuthorGroup><Abstract ID="Abs1" Language="En"><Heading>Abstract</Heading><Para>Among coronaviruses, several members are able to interact with sialic acids. For bovine coronavirus (BCoV) and related viruses, binding to cell surface components containing
<Emphasis Type="Italic">N</Emphasis>-acetyl-9-
<Emphasis Type="Italic">O</Emphasis>-acetylneuraminic acid is essential for initiation of an infection. These viruses resemble influenza C viruses because they share not only the receptor determinant, but also the presence of an acetylesterase that releases the 9-
<Emphasis Type="Italic">O</Emphasis>-acetyl group from sialic acid and thus abolishes the ability of the respective sialoglycoconjugate to function as a receptor for BCoV. As in the case of influenza viruses, the receptor-destroying enzyme of BCoV is believed to facilitate the spread of virus infection by removing receptor determinants from the surface of infected cells and by preventing the formation of virus aggregates. Another coronavirus, porcine transmissible gastroenteritis virus (TGEV) preferentially recognizes
<Emphasis Type="Italic">N</Emphasis>-glycolylneuraminic acid. TGEV does not contain a receptor-destroying enzyme and does not depend on the sialic acid binding activity for infection of cultured cells. However, binding to sialic acids is required for the enteropathogenicity of TGEV. Interaction with sialoglycoconjugates may help the virus to pass through the sialic acid-rich mucus layer that covers the viral target cells in the epithelium of the small intestine. We discuss that the BCoV group of viruses may have evolved from a TGEV-like ancestor by acquiring an acetylesterase gene through heterologous recombination.</Para></Abstract><KeywordGroup Language="En"><Heading>Keywords</Heading><Keyword>Coronavirus</Keyword><Keyword>Receptor</Keyword><Keyword>Sialic acid</Keyword><Keyword>N-glycolyl-neuraminic acid</Keyword><Keyword>N-acetyl-neuraminic acid</Keyword></KeywordGroup></ArticleHeader><NoBody></NoBody></Article></Issue></Volume></Journal></Publisher></istex:document></istex:metadataXml><mods version="3.6"><titleInfo lang="en"><title>Sialic acids as receptor determinants for coronaviruses</title></titleInfo><titleInfo type="alternative" contentType="CDATA"><title>Sialic acids as receptor determinants for coronaviruses</title></titleInfo><name type="personal" displayLabel="corresp"><namePart type="given">Christel</namePart><namePart type="family">Schwegmann-Weßels</namePart><affiliation>Institut für Virologie, Stiftung Tierärztliche Hochschule Hannover, Bünteweg 17, 30559, Hannover, Germany</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Georg</namePart><namePart type="family">Herrler</namePart><affiliation>Institut für Virologie, Stiftung Tierärztliche Hochschule Hannover, Bünteweg 17, 30559, Hannover, Germany</affiliation><affiliation>E-mail: Georg.Herrler@tiho-hannover.de</affiliation><role><roleTerm type="text">author</roleTerm></role></name><typeOfResource>text</typeOfResource><genre type="review-article" displayLabel="ReviewPaper" authority="ISTEX" authorityURI="https://content-type.data.istex.fr" valueURI="https://content-type.data.istex.fr/ark:/67375/XTP-L5L7X3NF-P">review-article</genre><originInfo><publisher>Kluwer Academic Publishers</publisher><place><placeTerm type="text">Boston</placeTerm></place><dateIssued encoding="w3cdtf">2006-02-01</dateIssued><copyrightDate encoding="w3cdtf">2006</copyrightDate></originInfo><language><languageTerm type="code" authority="rfc3066">en</languageTerm><languageTerm type="code" authority="iso639-2b">eng</languageTerm></language><abstract lang="en">Abstract: Among coronaviruses, several members are able to interact with sialic acids. For bovine coronavirus (BCoV) and related viruses, binding to cell surface components containing N-acetyl-9- O-acetylneuraminic acid is essential for initiation of an infection. These viruses resemble influenza C viruses because they share not only the receptor determinant, but also the presence of an acetylesterase that releases the 9- O-acetyl group from sialic acid and thus abolishes the ability of the respective sialoglycoconjugate to function as a receptor for BCoV. As in the case of influenza viruses, the receptor-destroying enzyme of BCoV is believed to facilitate the spread of virus infection by removing receptor determinants from the surface of infected cells and by preventing the formation of virus aggregates. Another coronavirus, porcine transmissible gastroenteritis virus (TGEV) preferentially recognizes N-glycolylneuraminic acid. TGEV does not contain a receptor-destroying enzyme and does not depend on the sialic acid binding activity for infection of cultured cells. However, binding to sialic acids is required for the enteropathogenicity of TGEV. Interaction with sialoglycoconjugates may help the virus to pass through the sialic acid-rich mucus layer that covers the viral target cells in the epithelium of the small intestine. We discuss that the BCoV group of viruses may have evolved from a TGEV-like ancestor by acquiring an acetylesterase gene through heterologous recombination.</abstract><note>Mini Review</note><subject lang="en"><genre>Keywords</genre><topic>Coronavirus</topic><topic>Receptor</topic><topic>Sialic acid</topic><topic>N-glycolyl-neuraminic acid</topic><topic>N-acetyl-neuraminic acid</topic></subject><relatedItem type="host"><titleInfo><title>Glycoconjugate Journal</title><subTitle>Official Journal of the International Glycoconjugate Organization</subTitle></titleInfo><titleInfo type="abbreviated"><title>Glycoconj J</title></titleInfo><name type="personal"><namePart type="given">Roland</namePart><namePart type="family">Schauer</namePart><role><roleTerm type="text">editor</roleTerm></role></name><name type="personal"><namePart type="given">Reinhard</namePart><namePart type="family">Vlasak</namePart><role><roleTerm type="text">editor</roleTerm></role></name><genre type="journal" authority="ISTEX" authorityURI="https://publication-type.data.istex.fr" valueURI="https://publication-type.data.istex.fr/ark:/67375/JMC-0GLKJH51-B">journal</genre><originInfo><publisher>Springer</publisher><dateIssued encoding="w3cdtf">2006-02-01</dateIssued><copyrightDate encoding="w3cdtf">2006</copyrightDate></originInfo><subject><genre>Life Sciences</genre><topic>Pathology</topic><topic>Biochemistry, general</topic></subject><identifier type="ISSN">0282-0080</identifier><identifier type="eISSN">1573-4986</identifier><identifier type="JournalID">10719</identifier><identifier type="JournalSPIN">GLYC</identifier><identifier type="IssueArticleCount">16</identifier><identifier type="VolumeIssueCount">9</identifier><part><date>2006</date><detail type="issue"><title>Special Issue: Viruses and Sialic Acids</title></detail><detail type="volume"><number>23</number><caption>vol.</caption></detail><detail type="issue"><number>1-2</number><caption>no.</caption></detail><extent unit="pages"><start>51</start><end>58</end></extent></part><recordInfo><recordOrigin>Springer Science + Business Media, LLC, 2006</recordOrigin></recordInfo></relatedItem><identifier type="istex">42568732A10B1148F141B13AEA1634BEFD14EC0A</identifier><identifier type="ark">ark:/67375/VQC-G9Z00D2X-C</identifier><identifier type="DOI">10.1007/s10719-006-5437-9</identifier><identifier type="ArticleID">5437</identifier><identifier type="ArticleID">NO00005437</identifier><accessCondition type="use and reproduction" contentType="copyright">Springer Science + Business Media, LLC, 2006</accessCondition><recordInfo><recordContentSource authority="ISTEX" authorityURI="https://loaded-corpus.data.istex.fr" valueURI="https://loaded-corpus.data.istex.fr/ark:/67375/XBH-3XSW68JL-F">springer</recordContentSource><recordOrigin>Springer Science + Business Media, LLC, 2006</recordOrigin></recordInfo></mods><json:item><extension>json</extension><original>false</original><mimetype>application/json</mimetype><uri>https://api.istex.fr/ark:/67375/VQC-G9Z00D2X-C/record.json</uri></json:item></metadata><serie></serie></istex></record>Pour manipuler ce document sous Unix (Dilib)
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