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<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Antibody Epitopes on the Neuraminidase of a Recent H3N2 Influenza Virus (A/Memphis/31/98)</title><author><name sortKey="Gulati, Upma" sort="Gulati, Upma" uniqKey="Gulati U" first="Upma" last="Gulati">Upma Gulati</name><affiliation><nlm:aff id="aff0">Department of Biochemistry and Molecular Biology, University of Oklahoma Health Sciences Center, Oklahoma City, Oklahoma 73104</nlm:aff></affiliation></author><author><name sortKey="Hwang, Chi Ching" sort="Hwang, Chi Ching" uniqKey="Hwang C" first="Chi-Ching" last="Hwang">Chi-Ching Hwang</name><affiliation><nlm:aff id="aff0">Department of Biochemistry and Molecular Biology, University of Oklahoma Health Sciences Center, Oklahoma City, Oklahoma 73104</nlm:aff></affiliation></author><author><name sortKey="Venkatramani, Lalitha" sort="Venkatramani, Lalitha" uniqKey="Venkatramani L" first="Lalitha" last="Venkatramani">Lalitha Venkatramani</name><affiliation><nlm:aff id="aff0">Department of Biochemistry and Molecular Biology, University of Oklahoma Health Sciences Center, Oklahoma City, Oklahoma 73104</nlm:aff></affiliation></author><author><name sortKey="Gulati, Shelly" sort="Gulati, Shelly" uniqKey="Gulati S" first="Shelly" last="Gulati">Shelly Gulati</name><affiliation><nlm:aff id="aff0">Department of Biochemistry and Molecular Biology, University of Oklahoma Health Sciences Center, Oklahoma City, Oklahoma 73104</nlm:aff></affiliation></author><author><name sortKey="Stray, Stephen J" sort="Stray, Stephen J" uniqKey="Stray S" first="Stephen J." last="Stray">Stephen J. Stray</name><affiliation><nlm:aff id="aff0">Department of Biochemistry and Molecular Biology, University of Oklahoma Health Sciences Center, Oklahoma City, Oklahoma 73104</nlm:aff></affiliation></author><author><name sortKey="Lee, Janis T" sort="Lee, Janis T" uniqKey="Lee J" first="Janis T." last="Lee">Janis T. Lee</name><affiliation><nlm:aff id="aff0">Department of Biochemistry and Molecular Biology, University of Oklahoma Health Sciences Center, Oklahoma City, Oklahoma 73104</nlm:aff></affiliation></author><author><name sortKey="Laver, W Graeme" sort="Laver, W Graeme" uniqKey="Laver W" first="W. Graeme" last="Laver">W. Graeme Laver</name><affiliation><nlm:aff id="aff0">Department of Biochemistry and Molecular Biology, University of Oklahoma Health Sciences Center, Oklahoma City, Oklahoma 73104</nlm:aff></affiliation></author><author><name sortKey="Bochkarev, Alexey" sort="Bochkarev, Alexey" uniqKey="Bochkarev A" first="Alexey" last="Bochkarev">Alexey Bochkarev</name><affiliation><nlm:aff id="aff0">Department of Biochemistry and Molecular Biology, University of Oklahoma Health Sciences Center, Oklahoma City, Oklahoma 73104</nlm:aff></affiliation></author><author><name sortKey="Zlotnick, Adam" sort="Zlotnick, Adam" uniqKey="Zlotnick A" first="Adam" last="Zlotnick">Adam Zlotnick</name><affiliation><nlm:aff id="aff0">Department of Biochemistry and Molecular Biology, University of Oklahoma Health Sciences Center, Oklahoma City, Oklahoma 73104</nlm:aff></affiliation></author><author><name sortKey="Air, Gillian M" sort="Air, Gillian M" uniqKey="Air G" first="Gillian M." last="Air">Gillian M. Air</name><affiliation><nlm:aff id="aff0">Department of Biochemistry and Molecular Biology, University of Oklahoma Health Sciences Center, Oklahoma City, Oklahoma 73104</nlm:aff></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PMC</idno><idno type="pmid">12414967</idno><idno type="pmc">136895</idno><idno type="url">http://www.ncbi.nlm.nih.gov/pmc/articles/PMC136895</idno><idno type="RBID">PMC:136895</idno><idno type="doi">10.1128/JVI.76.23.12274-12280.2002</idno><date when="2002">2002</date><idno type="wicri:Area/Pmc/Corpus">000376</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Corpus" wicri:corpus="PMC">000376</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en" level="a" type="main">Antibody Epitopes on the Neuraminidase of a Recent H3N2 Influenza Virus (A/Memphis/31/98)</title><author><name sortKey="Gulati, Upma" sort="Gulati, Upma" uniqKey="Gulati U" first="Upma" last="Gulati">Upma Gulati</name><affiliation><nlm:aff id="aff0">Department of Biochemistry and Molecular Biology, University of Oklahoma Health Sciences Center, Oklahoma City, Oklahoma 73104</nlm:aff></affiliation></author><author><name sortKey="Hwang, Chi Ching" sort="Hwang, Chi Ching" uniqKey="Hwang C" first="Chi-Ching" last="Hwang">Chi-Ching Hwang</name><affiliation><nlm:aff id="aff0">Department of Biochemistry and Molecular Biology, University of Oklahoma Health Sciences Center, Oklahoma City, Oklahoma 73104</nlm:aff></affiliation></author><author><name sortKey="Venkatramani, Lalitha" sort="Venkatramani, Lalitha" uniqKey="Venkatramani L" first="Lalitha" last="Venkatramani">Lalitha Venkatramani</name><affiliation><nlm:aff id="aff0">Department of Biochemistry and Molecular Biology, University of Oklahoma Health Sciences Center, Oklahoma City, Oklahoma 73104</nlm:aff></affiliation></author><author><name sortKey="Gulati, Shelly" sort="Gulati, Shelly" uniqKey="Gulati S" first="Shelly" last="Gulati">Shelly Gulati</name><affiliation><nlm:aff id="aff0">Department of Biochemistry and Molecular Biology, University of Oklahoma Health Sciences Center, Oklahoma City, Oklahoma 73104</nlm:aff></affiliation></author><author><name sortKey="Stray, Stephen J" sort="Stray, Stephen J" uniqKey="Stray S" first="Stephen J." last="Stray">Stephen J. Stray</name><affiliation><nlm:aff id="aff0">Department of Biochemistry and Molecular Biology, University of Oklahoma Health Sciences Center, Oklahoma City, Oklahoma 73104</nlm:aff></affiliation></author><author><name sortKey="Lee, Janis T" sort="Lee, Janis T" uniqKey="Lee J" first="Janis T." last="Lee">Janis T. Lee</name><affiliation><nlm:aff id="aff0">Department of Biochemistry and Molecular Biology, University of Oklahoma Health Sciences Center, Oklahoma City, Oklahoma 73104</nlm:aff></affiliation></author><author><name sortKey="Laver, W Graeme" sort="Laver, W Graeme" uniqKey="Laver W" first="W. Graeme" last="Laver">W. Graeme Laver</name><affiliation><nlm:aff id="aff0">Department of Biochemistry and Molecular Biology, University of Oklahoma Health Sciences Center, Oklahoma City, Oklahoma 73104</nlm:aff></affiliation></author><author><name sortKey="Bochkarev, Alexey" sort="Bochkarev, Alexey" uniqKey="Bochkarev A" first="Alexey" last="Bochkarev">Alexey Bochkarev</name><affiliation><nlm:aff id="aff0">Department of Biochemistry and Molecular Biology, University of Oklahoma Health Sciences Center, Oklahoma City, Oklahoma 73104</nlm:aff></affiliation></author><author><name sortKey="Zlotnick, Adam" sort="Zlotnick, Adam" uniqKey="Zlotnick A" first="Adam" last="Zlotnick">Adam Zlotnick</name><affiliation><nlm:aff id="aff0">Department of Biochemistry and Molecular Biology, University of Oklahoma Health Sciences Center, Oklahoma City, Oklahoma 73104</nlm:aff></affiliation></author><author><name sortKey="Air, Gillian M" sort="Air, Gillian M" uniqKey="Air G" first="Gillian M." last="Air">Gillian M. Air</name><affiliation><nlm:aff id="aff0">Department of Biochemistry and Molecular Biology, University of Oklahoma Health Sciences Center, Oklahoma City, Oklahoma 73104</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="2002">2002</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><p>We have characterized monoclonal antibodies raised against the neuraminidase (NA) of a Sydney-like influenza virus (A/Memphis/31/98, H3N2) in a reassortant virus A/NWS/33<sub>HA</sub>-A/Mem/31/98<sub>NA</sub> (H1N2) and nine escape mutants selected by these monoclonal antibodies. Five of the antibodies use the same heavy chain VDJ genes and may not be independent. Another antibody, Mem5, uses the same V<sub>H</sub> and J genes with a different D gene and different isotype. Sequence changes in escape mutants selected by these antibodies occur in two loops of the NA, at amino acid 198, 199, 220, or 221. These amino acids are located on the opposite side of the NA monomer to the major epitopes found in N9 and early N2 NAs. Escape mutants with a change at 198 have reduced NA activity compared to the wild-type virus. Asp198 points toward the substrate binding pocket, and we had previously found that a site-directed mutation of this amino acid resulted in a loss of enzyme activity (M. R. Lentz, R. G. Webster, and G. M. Air, Biochemistry <bold>26:</bold>5351-5358, 1987). Mutations at residue 199, 220, or 221 did not alter the NA activity significantly compared to that of wild-type NA. A 3.5-Å structure of Mem5 Fab complexed with the Mem/98 NA shows that the Mem5 antibody binds at the sites of escape mutation selected by the other antibodies.</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">jvi</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">12414967</article-id><article-id pub-id-type="pmc">136895</article-id><article-id pub-id-type="publisher-id">1093</article-id><article-id pub-id-type="doi">10.1128/JVI.76.23.12274-12280.2002</article-id><article-categories><subj-group subj-group-type="heading"><subject>Structure and Assembly</subject></subj-group></article-categories><title-group><article-title>Antibody Epitopes on the Neuraminidase of a Recent H3N2 Influenza Virus (A/Memphis/31/98)</article-title></title-group><contrib-group><contrib contrib-type="author"><name><surname>Gulati</surname><given-names>Upma</given-names></name><xref ref-type="aff" rid="aff0"></xref></contrib><contrib contrib-type="author"><name><surname>Hwang</surname><given-names>Chi-Ching</given-names></name><xref ref-type="aff" rid="aff0"></xref><xref ref-type="fn" rid="fn1">†</xref></contrib><contrib contrib-type="author"><name><surname>Venkatramani</surname><given-names>Lalitha</given-names></name><xref ref-type="aff" rid="aff0"></xref></contrib><contrib contrib-type="author"><name><surname>Gulati</surname><given-names>Shelly</given-names></name><xref ref-type="aff" rid="aff0"></xref></contrib><contrib contrib-type="author"><name><surname>Stray</surname><given-names>Stephen J.</given-names></name><xref ref-type="aff" rid="aff0"></xref></contrib><contrib contrib-type="author"><name><surname>Lee</surname><given-names>Janis T.</given-names></name><xref ref-type="aff" rid="aff0"></xref></contrib><contrib contrib-type="author"><name><surname>Laver</surname><given-names>W. Graeme</given-names></name><xref ref-type="aff" rid="aff0"></xref><xref ref-type="fn" rid="fn2">‡</xref></contrib><contrib contrib-type="author"><name><surname>Bochkarev</surname><given-names>Alexey</given-names></name><xref ref-type="aff" rid="aff0"></xref></contrib><contrib contrib-type="author"><name><surname>Zlotnick</surname><given-names>Adam</given-names></name><xref ref-type="aff" rid="aff0"></xref></contrib><contrib contrib-type="author"><name><surname>Air</surname><given-names>Gillian M.</given-names></name><xref ref-type="aff" rid="aff0"></xref><xref ref-type="corresp" rid="cor1">*</xref></contrib></contrib-group><aff id="aff0">Department of Biochemistry and Molecular Biology, University of Oklahoma Health Sciences Center, Oklahoma City, Oklahoma 73104</aff><author-notes><fn id="cor1"><label>*</label><p>Corresponding author. Mailing address: Department of Biochemistry and Molecular Biology, University of Oklahoma Health Sciences Center, Oklahoma City, OK 73104. Phone: (405) 271-2227, ext. 1250. Fax: (405) 271-3205. E-mail: <email>gillian-air@ouhsc.edu</email>.</p></fn><fn id="fn1"><label>†</label><p>Present address: Department of Biochemistry, Kaohsiung Medical University, Kaohsiung 80731, Taiwan.</p></fn><fn id="fn2"><label>‡</label><p>Present address: Barton Highway, Murrumbateman, New South Wales 2582, Australia.</p></fn></author-notes><pub-date pub-type="ppub"><month>12</month><year>2002</year></pub-date><volume>76</volume><issue>23</issue><fpage>12274</fpage><lpage>12280</lpage><history><date date-type="received"><day>30</day><month>5</month><year>2002</year></date><date date-type="accepted"><day>23</day><month>8</month><year>2002</year></date></history><copyright-statement>Copyright © 2002, American Society for Microbiology</copyright-statement><copyright-year>2002</copyright-year><abstract><p>We have characterized monoclonal antibodies raised against the neuraminidase (NA) of a Sydney-like influenza virus (A/Memphis/31/98, H3N2) in a reassortant virus A/NWS/33<sub>HA</sub>-A/Mem/31/98<sub>NA</sub> (H1N2) and nine escape mutants selected by these monoclonal antibodies. Five of the antibodies use the same heavy chain VDJ genes and may not be independent. Another antibody, Mem5, uses the same V<sub>H</sub> and J genes with a different D gene and different isotype. Sequence changes in escape mutants selected by these antibodies occur in two loops of the NA, at amino acid 198, 199, 220, or 221. These amino acids are located on the opposite side of the NA monomer to the major epitopes found in N9 and early N2 NAs. Escape mutants with a change at 198 have reduced NA activity compared to the wild-type virus. Asp198 points toward the substrate binding pocket, and we had previously found that a site-directed mutation of this amino acid resulted in a loss of enzyme activity (M. R. Lentz, R. G. Webster, and G. M. Air, Biochemistry <bold>26:</bold>5351-5358, 1987). Mutations at residue 199, 220, or 221 did not alter the NA activity significantly compared to that of wild-type NA. A 3.5-Å structure of Mem5 Fab complexed with the Mem/98 NA shows that the Mem5 antibody binds at the sites of escape mutation selected by the other antibodies.</p></abstract></article-meta></front></pmc></record>Pour manipuler ce document sous Unix (Dilib)
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