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<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Amino Acids Responsible for the Absolute Sialidase Activity of the Influenza A Virus Neuraminidase: Relationship to Growth in the Duck Intestine</title>
<author><name sortKey="Kobasa, Darwyn" sort="Kobasa, Darwyn" uniqKey="Kobasa D" first="Darwyn" last="Kobasa">Darwyn Kobasa</name>
<affiliation><nlm:aff id="N0x9b7e2b8.0x8b92ee8"></nlm:aff>
</affiliation>
</author>
<author><name sortKey="Wells, Krisna" sort="Wells, Krisna" uniqKey="Wells K" first="Krisna" last="Wells">Krisna Wells</name>
<affiliation><nlm:aff id="N0x9b7e2b8.0x8b92ee8"></nlm:aff>
</affiliation>
</author>
<author><name sortKey="Kawaoka, Yoshihiro" sort="Kawaoka, Yoshihiro" uniqKey="Kawaoka Y" first="Yoshihiro" last="Kawaoka">Yoshihiro Kawaoka</name>
<affiliation><nlm:aff id="N0x9b7e2b8.0x8b92ee8"></nlm:aff>
</affiliation>
<affiliation><nlm:aff id="N0x9b7e2b8.0x8b92ee8"></nlm:aff>
</affiliation>
</author>
</titleStmt>
<publicationStmt><idno type="wicri:source">PMC</idno>
<idno type="pmid">11689658</idno>
<idno type="pmc">114763</idno>
<idno type="url">http://www.ncbi.nlm.nih.gov/pmc/articles/PMC114763</idno>
<idno type="RBID">PMC:114763</idno>
<idno type="doi">10.1128/JVI.75.23.11773-11780.2001</idno>
<date when="2001">2001</date>
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<sourceDesc><biblStruct><analytic><title xml:lang="en" level="a" type="main">Amino Acids Responsible for the Absolute Sialidase Activity of the Influenza A Virus Neuraminidase: Relationship to Growth in the Duck Intestine</title>
<author><name sortKey="Kobasa, Darwyn" sort="Kobasa, Darwyn" uniqKey="Kobasa D" first="Darwyn" last="Kobasa">Darwyn Kobasa</name>
<affiliation><nlm:aff id="N0x9b7e2b8.0x8b92ee8"></nlm:aff>
</affiliation>
</author>
<author><name sortKey="Wells, Krisna" sort="Wells, Krisna" uniqKey="Wells K" first="Krisna" last="Wells">Krisna Wells</name>
<affiliation><nlm:aff id="N0x9b7e2b8.0x8b92ee8"></nlm:aff>
</affiliation>
</author>
<author><name sortKey="Kawaoka, Yoshihiro" sort="Kawaoka, Yoshihiro" uniqKey="Kawaoka Y" first="Yoshihiro" last="Kawaoka">Yoshihiro Kawaoka</name>
<affiliation><nlm:aff id="N0x9b7e2b8.0x8b92ee8"></nlm:aff>
</affiliation>
<affiliation><nlm:aff id="N0x9b7e2b8.0x8b92ee8"></nlm:aff>
</affiliation>
</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="2001">2001</date>
</imprint>
</series>
</biblStruct>
</sourceDesc>
</fileDesc>
<profileDesc><textClass></textClass>
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</teiHeader>
<front><div type="abstract" xml:lang="en"><p>The 1957 human pandemic strain of influenza A virus contained an avian virus hemagglutinin (HA) and neuraminidase (NA), both of which acquired specificity for the human receptor, <italic>N</italic>
-acetylneuraminic acid linked to galactose of cellular glycoconjugates via an α2-6 bond (NeuAcα2-6Gal). Although the NA retained considerable specificity for NeuAcα2-3Gal, its original substrate in ducks, it lost the ability to support viral growth in the duck intestine, suggesting a growth-restrictive change other than a shift in substrate specificity. To test this possibility, we generated a panel of reassortant viruses that expressed the NA genes of human H2N2 viruses isolated from 1957 to 1968 with all other genes from the avian virus A/duck/Hong Kong/278/78 (H9N2). Only the NA of A/Singapore/1/57 supported efficient viral growth in the intestines of orally inoculated ducks. The growth-supporting capacity of the NA correlated with a high level of enzymatic activity, comparable to that found to be associated with avian virus NAs. The specific activities of the A/Ann Arbor/6/60 and A/England/12/62 NAs, which showed greatly restricted abilities to support viral growth in ducks, were only 8 and 5%, respectively, of the NA specific activity for A/Singapore/1/57. Using chimeric constructs based on A/Singapore/1/57 and A/England/12/62 NAs, we localized the determinants of high specific NA activity to a region containing six amino acid substitutions in A/England/12/62: Ser331→Arg, Asp339→Asn, Asn367→Ser, Ser370→Leu, Asn400→Ser, and Pro431→Glu. Five of these six residues (excluding Asn400) were required and sufficient for the full specific activity of the A/Singapore/1/57 NA. Thus, in addition to a change in substrate specificity, a reduction in high specific activity may be required for the adaptation of avian virus NAs to growth in humans. This change is likely needed to maintain an optimal balance between NA activity and the lower affinity shown by human virus HAs for their cellular receptor.</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-id journal-id-type="publisher-id">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>
<publisher><publisher-name>American Society for Microbiology</publisher-name>
</publisher>
</journal-meta>
<article-meta><article-id pub-id-type="pmid">11689658</article-id>
<article-id pub-id-type="pmc">114763</article-id>
<article-id pub-id-type="publisher-id">0727</article-id>
<article-id pub-id-type="doi">10.1128/JVI.75.23.11773-11780.2001</article-id>
<article-categories><subj-group subj-group-type="heading"><subject>Virus-Cell Interactions</subject>
</subj-group>
</article-categories>
<title-group><article-title>Amino Acids Responsible for the Absolute Sialidase Activity of the Influenza A Virus Neuraminidase: Relationship to Growth in the Duck Intestine</article-title>
</title-group>
<contrib-group><contrib contrib-type="author"><name><surname>Kobasa</surname>
<given-names>Darwyn</given-names>
</name>
<xref ref-type="aff" rid="N0x9b7e2b8.0x8b92ee8">1</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Wells</surname>
<given-names>Krisna</given-names>
</name>
<xref ref-type="aff" rid="N0x9b7e2b8.0x8b92ee8">1</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Kawaoka</surname>
<given-names>Yoshihiro</given-names>
</name>
<xref ref-type="aff" rid="N0x9b7e2b8.0x8b92ee8">1</xref>
<xref ref-type="aff" rid="N0x9b7e2b8.0x8b92ee8">2</xref>
<xref ref-type="author-notes" rid="FN150">*</xref>
</contrib>
</contrib-group>
<aff id="N0x9b7e2b8.0x8b92ee8"> Department of Pathobiological Sciences, School of Veterinary Medicine, University of Wisconsin—Madison, Madison, Wisconsin 53706,<sup>1</sup>
and Institute of Medical Science, University of Tokyo, Minato-ku, Tokyo 108-8639, Japan<sup>2</sup>
</aff>
<author-notes><fn id="FN150"><label>*</label>
<p>Corresponding author. Mailing address: Department of Pathobiological Sciences, School of Veterinary Medicine, University of Wisconsin—Madison, Madison, WI 53706. Phone: (608) 265-4925. Fax: (608) 265-5622. E-mail: <email>kawaokay@svm.vetmed.wisc.edu</email>
.</p>
</fn>
</author-notes>
<pub-date pub-type="ppub"><month>12</month>
<year>2001</year>
</pub-date>
<volume>75</volume>
<issue>23</issue>
<fpage>11773</fpage>
<lpage>11780</lpage>
<history><date date-type="received"><day>13</day>
<month>4</month>
<year>2001</year>
</date>
<date date-type="accepted"><day>21</day>
<month>8</month>
<year>2001</year>
</date>
</history>
<copyright-statement>Copyright © 2001, American Society for Microbiology</copyright-statement>
<copyright-year>2001</copyright-year>
<abstract><p>The 1957 human pandemic strain of influenza A virus contained an avian virus hemagglutinin (HA) and neuraminidase (NA), both of which acquired specificity for the human receptor, <italic>N</italic>
-acetylneuraminic acid linked to galactose of cellular glycoconjugates via an α2-6 bond (NeuAcα2-6Gal). Although the NA retained considerable specificity for NeuAcα2-3Gal, its original substrate in ducks, it lost the ability to support viral growth in the duck intestine, suggesting a growth-restrictive change other than a shift in substrate specificity. To test this possibility, we generated a panel of reassortant viruses that expressed the NA genes of human H2N2 viruses isolated from 1957 to 1968 with all other genes from the avian virus A/duck/Hong Kong/278/78 (H9N2). Only the NA of A/Singapore/1/57 supported efficient viral growth in the intestines of orally inoculated ducks. The growth-supporting capacity of the NA correlated with a high level of enzymatic activity, comparable to that found to be associated with avian virus NAs. The specific activities of the A/Ann Arbor/6/60 and A/England/12/62 NAs, which showed greatly restricted abilities to support viral growth in ducks, were only 8 and 5%, respectively, of the NA specific activity for A/Singapore/1/57. Using chimeric constructs based on A/Singapore/1/57 and A/England/12/62 NAs, we localized the determinants of high specific NA activity to a region containing six amino acid substitutions in A/England/12/62: Ser331→Arg, Asp339→Asn, Asn367→Ser, Ser370→Leu, Asn400→Ser, and Pro431→Glu. Five of these six residues (excluding Asn400) were required and sufficient for the full specific activity of the A/Singapore/1/57 NA. Thus, in addition to a change in substrate specificity, a reduction in high specific activity may be required for the adaptation of avian virus NAs to growth in humans. This change is likely needed to maintain an optimal balance between NA activity and the lower affinity shown by human virus HAs for their cellular receptor.</p>
</abstract>
</article-meta>
</front>
</pmc>
</record>
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