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<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Neuraminidase hemadsorption activity, conserved in avian influenza A viruses, does not influence viral replication in ducks.</title><author><name sortKey="Kobasa, D" sort="Kobasa, D" uniqKey="Kobasa D" first="D" last="Kobasa">D. Kobasa</name></author><author><name sortKey="Rodgers, M E" sort="Rodgers, M E" uniqKey="Rodgers M" first="M E" last="Rodgers">M E Rodgers</name></author><author><name sortKey="Wells, K" sort="Wells, K" uniqKey="Wells K" first="K" last="Wells">K. Wells</name></author><author><name sortKey="Kawaoka, Y" sort="Kawaoka, Y" uniqKey="Kawaoka Y" first="Y" last="Kawaoka">Y. Kawaoka</name></author></titleStmt><publicationStmt><idno type="wicri:source">PMC</idno><idno type="pmid">9261394</idno><idno type="pmc">191950</idno><idno type="url">http://www.ncbi.nlm.nih.gov/pmc/articles/PMC191950</idno><idno type="RBID">PMC:191950</idno><date when="1997">1997</date><idno type="wicri:Area/Pmc/Corpus">000419</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Corpus" wicri:corpus="PMC">000419</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en" level="a" type="main">Neuraminidase hemadsorption activity, conserved in avian influenza A viruses, does not influence viral replication in ducks.</title><author><name sortKey="Kobasa, D" sort="Kobasa, D" uniqKey="Kobasa D" first="D" last="Kobasa">D. Kobasa</name></author><author><name sortKey="Rodgers, M E" sort="Rodgers, M E" uniqKey="Rodgers M" first="M E" last="Rodgers">M E Rodgers</name></author><author><name sortKey="Wells, K" sort="Wells, K" uniqKey="Wells K" first="K" last="Wells">K. Wells</name></author><author><name sortKey="Kawaoka, Y" sort="Kawaoka, Y" uniqKey="Kawaoka Y" first="Y" last="Kawaoka">Y. Kawaoka</name></author></analytic><series><title level="j">Journal of Virology</title><idno type="ISSN">0022-538X</idno><idno type="eISSN">1098-5514</idno><imprint><date when="1997">1997</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><p>The N1 and N9 neuraminidase (NA) subtypes of influenza A viruses exhibit significant hemadsorption activity that localizes to a site distinct from that of the enzymatic active site. To determine the conservation of hemadsorption activity among different NAs, we have examined most of the NA subtypes from avian, swine, equine, and human virus isolates. All subtypes of avian virus NAs examined and one equine virus N8 NA possessed high levels of hemadsorption activity. A swine virus N1 NA exhibited only weak hemadsorption activity, while in human virus N1 and N2 NAs, the activity was detected at a much lower level than in avian virus NAs. NAs which possessed hemadsorption activity for chicken erythrocytes (RBCs) were similarly able to adsorb human RBCs. However, none of the hemadsorption-positive NAs could bind equine, swine, or bovine RBCs, suggesting that RBCs from these species lack molecules, recognized by the NA hemadsorption site, present on human and chicken RBCs. Mutagenesis of the putative hemadsorption site of A/duck/Hong Kong/7/75 N2 NA abolished the high level of hemadsorption activity exhibited by the wild-type protein but also resulted in a 50% reduction of the NA enzymatic activity. A transfectant virus, generated by reverse genetics, containing this mutated NA replicated 10-fold less efficiently in chicken embryo fibroblast cultures than did a transfectant virus expressing the wild-type NA. However, both viruses replicated equally well in Peking ducks. Although conservation of NA hemadsorption activity among avian virus NAs suggests the maintenance of a required function of NA, loss of the activity does not preclude the replication of the virus in an avian host.</p></div></front></TEI><pmc article-type="research-article"><pmc-comment>The publisher of this article does not allow downloading of the full text in XML form.</pmc-comment>
<front><journal-meta><journal-id journal-id-type="nlm-ta">J Virol</journal-id><journal-title>Journal of Virology</journal-title><issn pub-type="ppub">0022-538X</issn><issn pub-type="epub">1098-5514</issn></journal-meta><article-meta><article-id pub-id-type="pmid">9261394</article-id><article-id pub-id-type="pmc">191950</article-id><article-categories><subj-group subj-group-type="heading"><subject>Research Article</subject></subj-group></article-categories><title-group><article-title>Neuraminidase hemadsorption activity, conserved in avian influenza A viruses, does not influence viral replication in ducks.</article-title></title-group><contrib-group><contrib contrib-type="author"><name><surname>Kobasa</surname><given-names>D</given-names></name></contrib><contrib contrib-type="author"><name><surname>Rodgers</surname><given-names>M E</given-names></name></contrib><contrib contrib-type="author"><name><surname>Wells</surname><given-names>K</given-names></name></contrib><contrib contrib-type="author"><name><surname>Kawaoka</surname><given-names>Y</given-names></name></contrib></contrib-group><aff>Department of Virology and Molecular Biology, St. Jude Children's Research Hospital, Memphis, Tennessee 38101, USA.</aff><pub-date pub-type="ppub"><month>9</month><year>1997</year></pub-date><volume>71</volume><issue>9</issue><fpage>6706</fpage><lpage>6713</lpage><abstract><p>The N1 and N9 neuraminidase (NA) subtypes of influenza A viruses exhibit significant hemadsorption activity that localizes to a site distinct from that of the enzymatic active site. To determine the conservation of hemadsorption activity among different NAs, we have examined most of the NA subtypes from avian, swine, equine, and human virus isolates. All subtypes of avian virus NAs examined and one equine virus N8 NA possessed high levels of hemadsorption activity. A swine virus N1 NA exhibited only weak hemadsorption activity, while in human virus N1 and N2 NAs, the activity was detected at a much lower level than in avian virus NAs. NAs which possessed hemadsorption activity for chicken erythrocytes (RBCs) were similarly able to adsorb human RBCs. However, none of the hemadsorption-positive NAs could bind equine, swine, or bovine RBCs, suggesting that RBCs from these species lack molecules, recognized by the NA hemadsorption site, present on human and chicken RBCs. Mutagenesis of the putative hemadsorption site of A/duck/Hong Kong/7/75 N2 NA abolished the high level of hemadsorption activity exhibited by the wild-type protein but also resulted in a 50% reduction of the NA enzymatic activity. A transfectant virus, generated by reverse genetics, containing this mutated NA replicated 10-fold less efficiently in chicken embryo fibroblast cultures than did a transfectant virus expressing the wild-type NA. However, both viruses replicated equally well in Peking ducks. Although conservation of NA hemadsorption activity among avian virus NAs suggests the maintenance of a required function of NA, loss of the activity does not preclude the replication of the virus in an avian host.</p></abstract></article-meta></front></pmc></record>Pour manipuler ce document sous Unix (Dilib)
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