Role of receptor binding specificity in influenza A virus transmission and pathogenesis
Identifieur interne : 000A24 ( Ncbi/Merge ); précédent : 000A23; suivant : 000A25Role of receptor binding specificity in influenza A virus transmission and pathogenesis
Auteurs : Miranda De Graaf ; Ron A M. FouchierSource :
- The EMBO Journal [ 0261-4189 ] ; 2014.
Abstract
The recent emergence of a novel avian
Url:
DOI: 10.1002/embj.201387442
PubMed: 24668228
PubMed Central: 4194109
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PMC:4194109Le document en format XML
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virus transmission and pathogenesis</title>
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virus transmission and pathogenesis</title>
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<front><div type="abstract" xml:lang="en"><title>Abstract</title>
<p>The recent emergence of a novel avian <styled-content style="fixed-case">A</styled-content>
/<styled-content style="fixed-case">H</styled-content>
7<styled-content style="fixed-case">N</styled-content>
9 influenza virus in poultry and humans in <styled-content style="fixed-case">C</styled-content>
hina, as well as laboratory studies on adaptation and transmission of avian <styled-content style="fixed-case">A</styled-content>
/<styled-content style="fixed-case">H</styled-content>
5<styled-content style="fixed-case">N</styled-content>
1 influenza viruses, has shed new light on influenza virus adaptation to mammals. One of the biological traits required for animal influenza viruses to cross the species barrier that received considerable attention in animal model studies, <italic>in vitro</italic>
assays, and structural analyses is receptor binding specificity. Sialylated glycans present on the apical surface of host cells can function as receptors for the influenza virus hemagglutinin (<styled-content style="fixed-case">HA</styled-content>
) protein. Avian and human influenza viruses typically have a different sialic acid (<styled-content style="fixed-case">SA</styled-content>
)‐binding preference and only few amino acid changes in the <styled-content style="fixed-case">HA</styled-content>
protein can cause a switch from avian to human receptor specificity. Recent experiments using glycan arrays, virus histochemistry, animal models, and structural analyses of <styled-content style="fixed-case">HA</styled-content>
have added a wealth of knowledge on receptor binding specificity. Here, we review recent data on the interaction between influenza virus <styled-content style="fixed-case">HA</styled-content>
and <styled-content style="fixed-case">SA</styled-content>
receptors of the host, and the impact on virus host range, pathogenesis, and transmission. Remaining challenges and future research priorities are also discussed.</p>
</div>
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<front><journal-meta><journal-id journal-id-type="nlm-ta">EMBO J</journal-id>
<journal-id journal-id-type="iso-abbrev">EMBO J</journal-id>
<journal-id journal-id-type="doi">10.1002/(ISSN)1460-2075</journal-id>
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<publisher><publisher-name>John Wiley and Sons Inc.</publisher-name>
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virus transmission and pathogenesis</article-title>
<alt-title alt-title-type="left-running-head">Miranda de Graaf & Ron A M Fouchier</alt-title>
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<contrib-group><contrib id="embj201387442-cr-0001" contrib-type="author"><name><surname>de Graaf</surname>
<given-names>Miranda</given-names>
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<xref ref-type="aff" rid="embj201387442-aff-0001"><sup>1</sup>
</xref>
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<contrib id="embj201387442-cr-0002" contrib-type="author" corresp="yes"><name><surname>Fouchier</surname>
<given-names>Ron A M</given-names>
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<xref ref-type="aff" rid="embj201387442-aff-0001"><sup>1</sup>
</xref>
</contrib>
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<aff id="embj201387442-aff-0001"><label><sup>1</sup>
</label>
<named-content content-type="organisation-division">Department of Viroscience</named-content>
<institution>Erasmus MC</institution>
<named-content content-type="city">Rotterdam</named-content>
<country country="NL">The Netherlands</country>
</aff>
<author-notes><corresp id="correspondenceTo"><label>*</label>
Corresponding author. Tel: +31 10 7044067; Fax: +31 10 7044760; E‐mail: <email>r.fouchier@erasmusmc.nl</email>
</corresp>
</author-notes>
<pub-date pub-type="ppub"><day>16</day>
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<year>2014</year>
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<pub-date pub-type="epub"><day>25</day>
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<volume>33</volume>
<issue>8</issue>
<issue-id pub-id-type="doi">10.1002/embj.v33.8</issue-id>
<fpage>823</fpage>
<lpage>841</lpage>
<history><date date-type="received"><day>19</day>
<month>11</month>
<year>2013</year>
</date>
<date date-type="rev-recd"><day>17</day>
<month>2</month>
<year>2014</year>
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<date date-type="accepted"><day>17</day>
<month>2</month>
<year>2014</year>
</date>
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<permissions><pmc-comment> © 2014 EMBO </pmc-comment>
<copyright-statement content-type="article-copyright">© 2014 The Authors</copyright-statement>
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<abstract id="embj201387442-abs-0001"><title>Abstract</title>
<p>The recent emergence of a novel avian <styled-content style="fixed-case">A</styled-content>
/<styled-content style="fixed-case">H</styled-content>
7<styled-content style="fixed-case">N</styled-content>
9 influenza virus in poultry and humans in <styled-content style="fixed-case">C</styled-content>
hina, as well as laboratory studies on adaptation and transmission of avian <styled-content style="fixed-case">A</styled-content>
/<styled-content style="fixed-case">H</styled-content>
5<styled-content style="fixed-case">N</styled-content>
1 influenza viruses, has shed new light on influenza virus adaptation to mammals. One of the biological traits required for animal influenza viruses to cross the species barrier that received considerable attention in animal model studies, <italic>in vitro</italic>
assays, and structural analyses is receptor binding specificity. Sialylated glycans present on the apical surface of host cells can function as receptors for the influenza virus hemagglutinin (<styled-content style="fixed-case">HA</styled-content>
) protein. Avian and human influenza viruses typically have a different sialic acid (<styled-content style="fixed-case">SA</styled-content>
)‐binding preference and only few amino acid changes in the <styled-content style="fixed-case">HA</styled-content>
protein can cause a switch from avian to human receptor specificity. Recent experiments using glycan arrays, virus histochemistry, animal models, and structural analyses of <styled-content style="fixed-case">HA</styled-content>
have added a wealth of knowledge on receptor binding specificity. Here, we review recent data on the interaction between influenza virus <styled-content style="fixed-case">HA</styled-content>
and <styled-content style="fixed-case">SA</styled-content>
receptors of the host, and the impact on virus host range, pathogenesis, and transmission. Remaining challenges and future research priorities are also discussed.</p>
</abstract>
<kwd-group kwd-group-type="author-generated"><kwd id="embj201387442-kwd-0001"><styled-content style="fixed-case">A</styled-content>
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<funding-group><award-group><funding-source>EU FP7</funding-source>
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<award-id>HHSN266200700010C</award-id>
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<award-group><funding-source>Intra European Marie Curie Fellowship</funding-source>
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<notes><p content-type="self-citation"><mixed-citation publication-type="journal" id="embj201387442-cit-1001"><source>EMBO J</source>
(<year>2014</year>
) <volume>33</volume>
, <fpage>823</fpage>
–<lpage>841</lpage>
<pub-id pub-id-type="pmid">24668228</pub-id>
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</front>
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<tree><noCountry><name sortKey="De Graaf, Miranda" sort="De Graaf, Miranda" uniqKey="De Graaf M" first="Miranda" last="De Graaf">Miranda De Graaf</name>
<name sortKey="Fouchier, Ron A M" sort="Fouchier, Ron A M" uniqKey="Fouchier R" first="Ron A M" last="Fouchier">Ron A M. Fouchier</name>
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