Structure, function and evolution of the hemagglutinin-esterase proteins of corona- and toroviruses
Identifieur interne : 000962 ( Pmc/Checkpoint ); précédent : 000961; suivant : 000963Structure, function and evolution of the hemagglutinin-esterase proteins of corona- and toroviruses
Auteurs : Raoul J. De GrootSource :
- Glycoconjugate Journal [ 0282-0080 ] ; 2006.
Abstract
Virus attachment to host cells is mediated by dedicated virion proteins, which specifically recognize one or, at most, a limited number of cell surface molecules. Receptor binding often involves protein-protein interactions, but carbohydrates may serve as receptor determinants as well. In fact, many different viruses use members of the sialic acid family either as their main receptor or as an initial attachment factor. Sialic acids (Sias) are 9-carbon negatively-charged monosaccharides commonly occurring as terminal residues of glycoconjugates. They come in a large variety and are differentially expressed in cells and tissues. By targeting specific Sia subtypes, viruses achieve host cell selectivity, but only to a certain extent. The Sia of choice might still be abundantly present on non-cell associated molecules, on non-target cells (including cells already infected) and even on virus particles themselves. This poses a hazard, as high-affinity virion binding to any of such “false'' receptors would result in loss of infectivity. Some enveloped RNA viruses deal with this problem by encoding virion-associated receptor-destroying enzymes (RDEs). These enzymes make the attachment to Sia reversible, thus providing the virus with an escape ticket. RDEs occur in two types: neuraminidases and sialate-
Url:
DOI: 10.1007/s10719-006-5438-8
PubMed: 16575523
PubMed Central: 7088178
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<sourceDesc><biblStruct><analytic><title xml:lang="en" level="a" type="main">Structure, function and evolution of the hemagglutinin-esterase proteins of corona- and toroviruses</title>
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<imprint><date when="2006">2006</date>
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<front><div type="abstract" xml:lang="en"><p>Virus attachment to host cells is mediated by dedicated virion proteins, which specifically recognize one or, at most, a limited number of cell surface molecules. Receptor binding often involves protein-protein interactions, but carbohydrates may serve as receptor determinants as well. In fact, many different viruses use members of the sialic acid family either as their main receptor or as an initial attachment factor. Sialic acids (Sias) are 9-carbon negatively-charged monosaccharides commonly occurring as terminal residues of glycoconjugates. They come in a large variety and are differentially expressed in cells and tissues. By targeting specific Sia subtypes, viruses achieve host cell selectivity, but only to a certain extent. The Sia of choice might still be abundantly present on non-cell associated molecules, on non-target cells (including cells already infected) and even on virus particles themselves. This poses a hazard, as high-affinity virion binding to any of such “false'' receptors would result in loss of infectivity. Some enveloped RNA viruses deal with this problem by encoding virion-associated receptor-destroying enzymes (RDEs). These enzymes make the attachment to Sia reversible, thus providing the virus with an escape ticket. RDEs occur in two types: neuraminidases and sialate-<italic>O</italic>
-acetylesterases. The latter, originally discovered in influenza C virus, are also found in certain nidoviruses, namely in group 2 coronaviruses and in toroviruses, as well as in infectious salmon anemia virus, an orthomyxovirus of teleosts. Here, the structure, function and evolution of viral sialate-<italic>O</italic>
-acetylesterases is reviewed with main focus on the hemagglutinin-esterases of nidoviruses.</p>
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<author><name sortKey="Weiss, S R" uniqKey="Weiss S">S.R. Weiss</name>
</author>
</analytic>
</biblStruct>
<biblStruct><analytic><author><name sortKey="Schultze, B" uniqKey="Schultze B">B. Schultze</name>
</author>
<author><name sortKey="Zimmer, G" uniqKey="Zimmer G">G. Zimmer</name>
</author>
<author><name sortKey="Herrler, G" uniqKey="Herrler G">G. Herrler</name>
</author>
</analytic>
</biblStruct>
<biblStruct><analytic><author><name sortKey="Popova, R" uniqKey="Popova R">R. Popova</name>
</author>
<author><name sortKey="Zhang, X" uniqKey="Zhang X">X. Zhang</name>
</author>
</analytic>
</biblStruct>
</listBibl>
</div1>
</back>
</TEI>
<pmc article-type="review-article"><pmc-dir>properties open_access</pmc-dir>
<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">16575523</article-id>
<article-id pub-id-type="pmc">7088178</article-id>
<article-id pub-id-type="publisher-id">5438</article-id>
<article-id pub-id-type="doi">10.1007/s10719-006-5438-8</article-id>
<article-categories><subj-group subj-group-type="heading"><subject>Minireview</subject>
</subj-group>
</article-categories>
<title-group><article-title>Structure, function and evolution of the hemagglutinin-esterase proteins of corona- and toroviruses</article-title>
</title-group>
<contrib-group><contrib contrib-type="author" corresp="yes"><name><surname>de Groot</surname>
<given-names>Raoul J.</given-names>
</name>
<address><phone>+31-30-2531463</phone>
<fax>+31-30-2536723</fax>
<email>R.Groot@vet.uu.nl</email>
</address>
<xref ref-type="aff" rid="Aff1"></xref>
</contrib>
<aff id="Aff1"><institution-wrap><institution-id institution-id-type="GRID">grid.5477.1</institution-id>
<institution-id institution-id-type="ISNI">0000000120346234</institution-id>
<institution>Virology Section, Department of Infectious Diseases and Immunology, Faculty of Veterinary Medicine,</institution>
<institution>Utrecht University,</institution>
</institution-wrap>
The Netherlands</aff>
</contrib-group>
<pub-date pub-type="ppub"><year>2006</year>
</pub-date>
<volume>23</volume>
<issue>1</issue>
<fpage>59</fpage>
<lpage>72</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>Virus attachment to host cells is mediated by dedicated virion proteins, which specifically recognize one or, at most, a limited number of cell surface molecules. Receptor binding often involves protein-protein interactions, but carbohydrates may serve as receptor determinants as well. In fact, many different viruses use members of the sialic acid family either as their main receptor or as an initial attachment factor. Sialic acids (Sias) are 9-carbon negatively-charged monosaccharides commonly occurring as terminal residues of glycoconjugates. They come in a large variety and are differentially expressed in cells and tissues. By targeting specific Sia subtypes, viruses achieve host cell selectivity, but only to a certain extent. The Sia of choice might still be abundantly present on non-cell associated molecules, on non-target cells (including cells already infected) and even on virus particles themselves. This poses a hazard, as high-affinity virion binding to any of such “false'' receptors would result in loss of infectivity. Some enveloped RNA viruses deal with this problem by encoding virion-associated receptor-destroying enzymes (RDEs). These enzymes make the attachment to Sia reversible, thus providing the virus with an escape ticket. RDEs occur in two types: neuraminidases and sialate-<italic>O</italic>
-acetylesterases. The latter, originally discovered in influenza C virus, are also found in certain nidoviruses, namely in group 2 coronaviruses and in toroviruses, as well as in infectious salmon anemia virus, an orthomyxovirus of teleosts. Here, the structure, function and evolution of viral sialate-<italic>O</italic>
-acetylesterases is reviewed with main focus on the hemagglutinin-esterases of nidoviruses.</p>
</abstract>
<kwd-group xml:lang="en"><title>Keywords</title>
<kwd>Influenza</kwd>
<kwd>Sialic Acid</kwd>
<kwd>Cell Surface Molecule</kwd>
<kwd>Terminal Residue</kwd>
<kwd>Infectious Salmon Anemia Virus</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>
</pmc>
<affiliations><list></list>
<tree><noCountry><name sortKey="De Groot, Raoul J" sort="De Groot, Raoul J" uniqKey="De Groot R" first="Raoul J." last="De Groot">Raoul J. De Groot</name>
</noCountry>
</tree>
</affiliations>
</record>
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