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<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Amino Acid Residues Contributing to the Substrate Specificity of the Influenza A Virus Neuraminidase</title>
<author><name sortKey="Kobasa, Darwyn" sort="Kobasa, Darwyn" uniqKey="Kobasa D" first="Darwyn" last="Kobasa">Darwyn Kobasa</name>
<affiliation><nlm:aff id="N0xa097018.0xa440c20"></nlm:aff>
</affiliation>
</author>
<author><name sortKey="Kodihalli, Shantha" sort="Kodihalli, Shantha" uniqKey="Kodihalli S" first="Shantha" last="Kodihalli">Shantha Kodihalli</name>
<affiliation><nlm:aff id="N0xa097018.0xa440c20"></nlm:aff>
</affiliation>
</author>
<author><name sortKey="Luo, Ming" sort="Luo, Ming" uniqKey="Luo M" first="Ming" last="Luo">Ming Luo</name>
<affiliation><nlm:aff id="N0xa097018.0xa440c20"></nlm:aff>
</affiliation>
</author>
<author><name sortKey="Castrucci, Maria R" sort="Castrucci, Maria R" uniqKey="Castrucci M" first="Maria R." last="Castrucci">Maria R. Castrucci</name>
<affiliation><nlm:aff id="N0xa097018.0xa440c20"></nlm:aff>
</affiliation>
</author>
<author><name sortKey="Donatelli, Isabella" sort="Donatelli, Isabella" uniqKey="Donatelli I" first="Isabella" last="Donatelli">Isabella Donatelli</name>
<affiliation><nlm:aff id="N0xa097018.0xa440c20"></nlm:aff>
</affiliation>
</author>
<author><name sortKey="Suzuki, Yasuo" sort="Suzuki, Yasuo" uniqKey="Suzuki Y" first="Yasuo" last="Suzuki">Yasuo Suzuki</name>
<affiliation><nlm:aff id="N0xa097018.0xa440c20"></nlm:aff>
</affiliation>
</author>
<author><name sortKey="Suzuki, Takashi" sort="Suzuki, Takashi" uniqKey="Suzuki T" first="Takashi" last="Suzuki">Takashi Suzuki</name>
<affiliation><nlm:aff id="N0xa097018.0xa440c20"></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="N0xa097018.0xa440c20"></nlm:aff>
</affiliation>
<affiliation><nlm:aff id="N0xa097018.0xa440c20"></nlm:aff>
</affiliation>
</author>
</titleStmt>
<publicationStmt><idno type="wicri:source">PMC</idno>
<idno type="pmid">10400772</idno>
<idno type="pmc">112759</idno>
<idno type="url">http://www.ncbi.nlm.nih.gov/pmc/articles/PMC112759</idno>
<idno type="RBID">PMC:112759</idno>
<date when="1999">1999</date>
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<sourceDesc><biblStruct><analytic><title xml:lang="en" level="a" type="main">Amino Acid Residues Contributing to the Substrate Specificity of the Influenza A Virus Neuraminidase</title>
<author><name sortKey="Kobasa, Darwyn" sort="Kobasa, Darwyn" uniqKey="Kobasa D" first="Darwyn" last="Kobasa">Darwyn Kobasa</name>
<affiliation><nlm:aff id="N0xa097018.0xa440c20"></nlm:aff>
</affiliation>
</author>
<author><name sortKey="Kodihalli, Shantha" sort="Kodihalli, Shantha" uniqKey="Kodihalli S" first="Shantha" last="Kodihalli">Shantha Kodihalli</name>
<affiliation><nlm:aff id="N0xa097018.0xa440c20"></nlm:aff>
</affiliation>
</author>
<author><name sortKey="Luo, Ming" sort="Luo, Ming" uniqKey="Luo M" first="Ming" last="Luo">Ming Luo</name>
<affiliation><nlm:aff id="N0xa097018.0xa440c20"></nlm:aff>
</affiliation>
</author>
<author><name sortKey="Castrucci, Maria R" sort="Castrucci, Maria R" uniqKey="Castrucci M" first="Maria R." last="Castrucci">Maria R. Castrucci</name>
<affiliation><nlm:aff id="N0xa097018.0xa440c20"></nlm:aff>
</affiliation>
</author>
<author><name sortKey="Donatelli, Isabella" sort="Donatelli, Isabella" uniqKey="Donatelli I" first="Isabella" last="Donatelli">Isabella Donatelli</name>
<affiliation><nlm:aff id="N0xa097018.0xa440c20"></nlm:aff>
</affiliation>
</author>
<author><name sortKey="Suzuki, Yasuo" sort="Suzuki, Yasuo" uniqKey="Suzuki Y" first="Yasuo" last="Suzuki">Yasuo Suzuki</name>
<affiliation><nlm:aff id="N0xa097018.0xa440c20"></nlm:aff>
</affiliation>
</author>
<author><name sortKey="Suzuki, Takashi" sort="Suzuki, Takashi" uniqKey="Suzuki T" first="Takashi" last="Suzuki">Takashi Suzuki</name>
<affiliation><nlm:aff id="N0xa097018.0xa440c20"></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="N0xa097018.0xa440c20"></nlm:aff>
</affiliation>
<affiliation><nlm:aff id="N0xa097018.0xa440c20"></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="1999">1999</date>
</imprint>
</series>
</biblStruct>
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<front><div type="abstract" xml:lang="en"><p>Influenza A viruses possess two glycoprotein spikes on the virion surface: hemagglutinin (HA), which binds to oligosaccharides containing terminal sialic acid, and neuraminidase (NA), which removes terminal sialic acid from oligosaccharides. Hence, the interplay between these receptor-binding and receptor-destroying functions assumes major importance in viral replication. In contrast to the well-characterized role of HA in host range restriction of influenza viruses, there is only limited information on the role of NA substrate specificity in viral replication among different animal species. We therefore investigated the substrate specificities of NA for linkages between <italic>N</italic>
-acetyl sialic acid and galactose (NeuAcα2-3Gal and NeuAcα2-6Gal) and for different molecular species of sialic acids (<italic>N</italic>
-acetyl and <italic>N</italic>
-glycolyl sialic acids) in influenza A viruses isolated from human, avian, and pig hosts. Substrate specificity assays showed that all viruses had similar specificities for NeuAcα2-3Gal, while the activities for NeuAcα2-6Gal ranged from marginal, as represented by avian and early N2 human viruses, to high (although only one-third the activity for NeuAcα2-3Gal), as represented by swine and more recent N2 human viruses. Using site-specific mutagenesis, we identified in the earliest human virus with a detectable increase in NeuAcα2-6Gal specificity a change at position 275 (from isoleucine to valine) that enhanced the specificity for this substrate. Valine at position 275 was maintained in all later human viruses as well as swine viruses. A similar examination of <italic>N</italic>
-glycolylneuraminic acid (NeuGc) specificity showed that avian viruses and most human viruses had low to moderate activity for this substrate, with the exception of most human viruses isolated between 1967 and 1969, whose NeuGc specificity was as high as that of swine viruses. The amino acid at position 431 was found to determine the level of NeuGc specificity of NA: lysine conferred high NeuGc specificity, while proline, glutamine, and glutamic acid were associated with lower NeuGc specificity. Both residues 275 and 431 lie close to the enzymatic active site but are not directly involved in the reaction mechanism. This finding suggests that the adaptation of NA to different substrates occurs by a mechanism of amino acid substitutions that subtly alter the conformation of NA in and around the active site to facilitate the binding of different species of sialic acid.</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">10400772</article-id>
<article-id pub-id-type="pmc">112759</article-id>
<article-id pub-id-type="publisher-id">0146</article-id>
<article-categories><subj-group subj-group-type="heading"><subject>Pathogenesis and Immunity</subject>
</subj-group>
</article-categories>
<title-group><article-title>Amino Acid Residues Contributing to the Substrate Specificity of the Influenza A Virus Neuraminidase</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="N0xa097018.0xa440c20">1</xref>
<xref ref-type="author-notes" rid="FN151">†</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Kodihalli</surname>
<given-names>Shantha</given-names>
</name>
<xref ref-type="aff" rid="N0xa097018.0xa440c20">1</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Luo</surname>
<given-names>Ming</given-names>
</name>
<xref ref-type="aff" rid="N0xa097018.0xa440c20">2</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Castrucci</surname>
<given-names>Maria R.</given-names>
</name>
<xref ref-type="aff" rid="N0xa097018.0xa440c20">3</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Donatelli</surname>
<given-names>Isabella</given-names>
</name>
<xref ref-type="aff" rid="N0xa097018.0xa440c20">3</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Suzuki</surname>
<given-names>Yasuo</given-names>
</name>
<xref ref-type="aff" rid="N0xa097018.0xa440c20">4</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Suzuki</surname>
<given-names>Takashi</given-names>
</name>
<xref ref-type="aff" rid="N0xa097018.0xa440c20">4</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Kawaoka</surname>
<given-names>Yoshihiro</given-names>
</name>
<xref ref-type="aff" rid="N0xa097018.0xa440c20">1</xref>
<xref ref-type="aff" rid="N0xa097018.0xa440c20">5</xref>
<xref ref-type="author-notes" rid="FN150">*</xref>
</contrib>
</contrib-group>
<aff id="N0xa097018.0xa440c20"> Department of Virology and Molecular Biology, St. Jude Children’s Research Hospital, Memphis, Tennessee 38101<sup>1</sup>
; Center for Macromolecular Crystallography, Department of Microbiology, University of Alabama at Birmingham, Birmingham, Alabama 35294<sup>2</sup>
; Department of Virology, Istituto Superiore di Sanita, Rome, Italy<sup>3</sup>
; Department of Biochemistry, School of Pharmaceutical Science, University of Shizuoka, Shizuoka 422, Japan<sup>4</sup>
; and Department of Pathobiological Sciences, School of Veterinary Medicine, University of Wisconsin, Madison, Wisconsin 53706<sup>5</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, 2015 Linden Drive West, Madison, WI 53706. Phone: (608) 265-4925. Fax: (608) 265-5622. E-mail: <email>kawaokay@svm.vetmed.wisc.edu</email>
.</p>
</fn>
<fn id="FN151"><label>†</label>
<p>Present address: DVP/OVRR/CBER/FDA, 29 Lincoln Drive, Bethesda, MD 20892.</p>
</fn>
</author-notes>
<pub-date pub-type="ppub"><month>8</month>
<year>1999</year>
</pub-date>
<volume>73</volume>
<issue>8</issue>
<fpage>6743</fpage>
<lpage>6751</lpage>
<history><date date-type="received"><day>29</day>
<month>1</month>
<year>1999</year>
</date>
<date date-type="accepted"><day>4</day>
<month>5</month>
<year>1999</year>
</date>
</history>
<copyright-statement>Copyright © 1999, American Society for Microbiology</copyright-statement>
<copyright-year>1999</copyright-year>
<abstract><p>Influenza A viruses possess two glycoprotein spikes on the virion surface: hemagglutinin (HA), which binds to oligosaccharides containing terminal sialic acid, and neuraminidase (NA), which removes terminal sialic acid from oligosaccharides. Hence, the interplay between these receptor-binding and receptor-destroying functions assumes major importance in viral replication. In contrast to the well-characterized role of HA in host range restriction of influenza viruses, there is only limited information on the role of NA substrate specificity in viral replication among different animal species. We therefore investigated the substrate specificities of NA for linkages between <italic>N</italic>
-acetyl sialic acid and galactose (NeuAcα2-3Gal and NeuAcα2-6Gal) and for different molecular species of sialic acids (<italic>N</italic>
-acetyl and <italic>N</italic>
-glycolyl sialic acids) in influenza A viruses isolated from human, avian, and pig hosts. Substrate specificity assays showed that all viruses had similar specificities for NeuAcα2-3Gal, while the activities for NeuAcα2-6Gal ranged from marginal, as represented by avian and early N2 human viruses, to high (although only one-third the activity for NeuAcα2-3Gal), as represented by swine and more recent N2 human viruses. Using site-specific mutagenesis, we identified in the earliest human virus with a detectable increase in NeuAcα2-6Gal specificity a change at position 275 (from isoleucine to valine) that enhanced the specificity for this substrate. Valine at position 275 was maintained in all later human viruses as well as swine viruses. A similar examination of <italic>N</italic>
-glycolylneuraminic acid (NeuGc) specificity showed that avian viruses and most human viruses had low to moderate activity for this substrate, with the exception of most human viruses isolated between 1967 and 1969, whose NeuGc specificity was as high as that of swine viruses. The amino acid at position 431 was found to determine the level of NeuGc specificity of NA: lysine conferred high NeuGc specificity, while proline, glutamine, and glutamic acid were associated with lower NeuGc specificity. Both residues 275 and 431 lie close to the enzymatic active site but are not directly involved in the reaction mechanism. This finding suggests that the adaptation of NA to different substrates occurs by a mechanism of amino acid substitutions that subtly alter the conformation of NA in and around the active site to facilitate the binding of different species of sialic acid.</p>
</abstract>
</article-meta>
</front>
</pmc>
</record>
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