Sialic acids as receptor determinants for coronaviruses
Identifieur interne : 000381 ( Pmc/Corpus ); précédent : 000380; suivant : 000382Sialic acids as receptor determinants for coronaviruses
Auteurs : Christel Schwegmann-We Els ; Georg HerrlerSource :
- Glycoconjugate Journal [ 0282-0080 ] ; 2006.
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
Url:
DOI: 10.1007/s10719-006-5437-9
PubMed: 16575522
PubMed Central: 7088368
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PMC:7088368Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Sialic acids as receptor determinants for coronaviruses</title><author><name sortKey="Schwegmann We Els, Christel" sort="Schwegmann We Els, Christel" uniqKey="Schwegmann We Els C" first="Christel" last="Schwegmann-We Els">Christel Schwegmann-We Els</name><affiliation><nlm:aff id="Aff1"></nlm:aff></affiliation></author><author><name sortKey="Herrler, Georg" sort="Herrler, Georg" uniqKey="Herrler G" first="Georg" last="Herrler">Georg Herrler</name><affiliation><nlm:aff id="Aff1"></nlm:aff></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PMC</idno><idno type="pmid">16575522</idno><idno type="pmc">7088368</idno><idno type="url">http://www.ncbi.nlm.nih.gov/pmc/articles/PMC7088368</idno><idno type="RBID">PMC:7088368</idno><idno type="doi">10.1007/s10719-006-5437-9</idno><date when="2006">2006</date><idno type="wicri:Area/Pmc/Corpus">000381</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Corpus" wicri:corpus="PMC">000381</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en" level="a" type="main">Sialic acids as receptor determinants for coronaviruses</title><author><name sortKey="Schwegmann We Els, Christel" sort="Schwegmann We Els, Christel" uniqKey="Schwegmann We Els C" first="Christel" last="Schwegmann-We Els">Christel Schwegmann-We Els</name><affiliation><nlm:aff id="Aff1"></nlm:aff></affiliation></author><author><name sortKey="Herrler, Georg" sort="Herrler, Georg" uniqKey="Herrler G" first="Georg" last="Herrler">Georg Herrler</name><affiliation><nlm:aff id="Aff1"></nlm:aff></affiliation></author></analytic><series><title level="j">Glycoconjugate Journal</title><idno type="ISSN">0282-0080</idno><idno type="eISSN">1573-4986</idno><imprint><date when="2006">2006</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><p>Among coronaviruses, several members are able to interact with sialic acids. For bovine coronavirus (BCoV) and related viruses, binding to cell surface components containing
<italic>N</italic>-acetyl-9-
<italic>O</italic>-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-
<italic>O</italic>-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
<italic>N</italic>-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.</p></div></front><back><div1 type="bibliography"><listBibl><biblStruct><analytic><author><name sortKey="Delmas, B" uniqKey="Delmas B">B. Delmas</name></author><author><name sortKey="Gelfi, J" uniqKey="Gelfi J">J. Gelfi</name></author><author><name sortKey="L Haridon, R" uniqKey="L Haridon R">R. L'Haridon</name></author><author><name sortKey="Vogel, L K" uniqKey="Vogel L">L.K. 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<front><journal-meta><journal-id journal-id-type="nlm-ta">Glycoconj J</journal-id><journal-id journal-id-type="iso-abbrev">Glycoconj. J</journal-id><journal-title-group><journal-title>Glycoconjugate Journal</journal-title></journal-title-group><issn pub-type="ppub">0282-0080</issn><issn pub-type="epub">1573-4986</issn><publisher><publisher-name>Kluwer Academic Publishers</publisher-name><publisher-loc>Boston</publisher-loc></publisher></journal-meta><article-meta><article-id pub-id-type="pmid">16575522</article-id><article-id pub-id-type="pmc">7088368</article-id><article-id pub-id-type="publisher-id">5437</article-id><article-id pub-id-type="doi">10.1007/s10719-006-5437-9</article-id><article-categories><subj-group subj-group-type="heading"><subject>Mini Review</subject></subj-group></article-categories><title-group><article-title>Sialic acids as receptor determinants for coronaviruses</article-title></title-group><contrib-group><contrib contrib-type="author" corresp="yes"><name><surname>Schwegmann-Weßels</surname><given-names>Christel</given-names></name><xref ref-type="aff" rid="Aff1"></xref></contrib><contrib contrib-type="author"><name><surname>Herrler</surname><given-names>Georg</given-names></name><address><phone>+49-511-953-8857</phone><fax>+49-511-953-8898</fax><email>Georg.Herrler@tiho-hannover.de</email></address><xref ref-type="aff" rid="Aff1"></xref></contrib><aff id="Aff1"><institution-wrap><institution-id institution-id-type="GRID">grid.412970.9</institution-id><institution-id institution-id-type="ISNI">0000000101266191</institution-id><institution>Institut für Virologie,</institution><institution>Stiftung Tierärztliche Hochschule Hannover,</institution></institution-wrap>Bünteweg 17, 30559 Hannover, Germany</aff></contrib-group><pub-date pub-type="ppub"><year>2006</year></pub-date><volume>23</volume><issue>1</issue><fpage>51</fpage><lpage>58</lpage><permissions><copyright-statement>© Springer Science + Business Media, LLC 2006</copyright-statement><license><license-p>This article is made available via the PMC Open Access Subset for unrestricted research re-use and secondary analysis in any form or by any means with acknowledgement of the original source. These permissions are granted for the duration of the World Health Organization (WHO) declaration of COVID-19 as a global pandemic.</license-p></license></permissions><abstract id="Abs1"><p>Among coronaviruses, several members are able to interact with sialic acids. For bovine coronavirus (BCoV) and related viruses, binding to cell surface components containing
<italic>N</italic>-acetyl-9-
<italic>O</italic>-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-
<italic>O</italic>-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
<italic>N</italic>-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.</p></abstract><kwd-group xml:lang="en"><title>Keywords</title><kwd>Coronavirus</kwd><kwd>Receptor</kwd><kwd>Sialic acid</kwd><kwd>N-glycolyl-neuraminic acid</kwd><kwd>N-acetyl-neuraminic acid</kwd></kwd-group><custom-meta-group><custom-meta><meta-name>issue-copyright-statement</meta-name><meta-value>© Springer Science + Business Media, LLC 2006</meta-value></custom-meta></custom-meta-group></article-meta></front><back><ref-list id="Bib1"><title>References</title><ref id="CR1"><label>1.</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Delmas</surname><given-names>B.</given-names></name><name><surname>Gelfi</surname><given-names>J.</given-names></name><name><surname>L'Haridon</surname><given-names>R.</given-names></name><name><surname>Vogel</surname><given-names>L.K.</given-names></name><name><surname>Sjostrom</surname><given-names>H.</given-names></name><name><surname>Noren</surname><given-names>O.</given-names></name><name><surname>Laude</surname><given-names>H.</given-names></name></person-group><article-title>Aminopeptidase N is a major receptor for the entero-pathogenic coronavirus TGEV</article-title><source>Nature</source><year>1992</year><volume>357</volume><fpage>417</fpage><lpage>20</lpage><pub-id pub-id-type="doi">10.1038/357417a0</pub-id><pub-id pub-id-type="pmid">1350661</pub-id></element-citation></ref><ref id="CR2"><label>2.</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Yeager</surname><given-names>C.L.</given-names></name><name><surname>Ashmun</surname><given-names>R.A.</given-names></name><name><surname>Williams</surname><given-names>R.K.</given-names></name><name><surname>Cardellichio</surname><given-names>C.B.</given-names></name><name><surname>Shapiro</surname><given-names>L.H.</given-names></name><name><surname>Look</surname><given-names>A.T.</given-names></name><name><surname>Holmes</surname><given-names>K.V.</given-names></name></person-group><article-title>Human aminopeptidase N is a receptor for human coronavirus 229E</article-title><source>Nature</source><year>1992</year><volume>357</volume><fpage>420</fpage><lpage>22</lpage><pub-id pub-id-type="doi">10.1038/357420a0</pub-id><pub-id pub-id-type="pmid">1350662</pub-id></element-citation></ref><ref id="CR3"><label>3.</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Tresnan</surname><given-names>D.B.</given-names></name><name><surname>Levis</surname><given-names>R.</given-names></name><name><surname>Holmes</surname><given-names>K.V.</given-names></name></person-group><article-title>Feline aminopeptidase N serves as a receptor for feline, canine porcine, and human coronaviruses in serogroup I</article-title><source>J. 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