Amino acid determinants conferring stable sialidase activity at low pH for H5N1 influenza A virus neuraminidase
Identifieur interne : 000752 ( Pmc/Checkpoint ); précédent : 000751; suivant : 000753Amino acid determinants conferring stable sialidase activity at low pH for H5N1 influenza A virus neuraminidase
Auteurs : Tadanobu Takahashi [États-Unis, Japon] ; Chairul A. Nidom [Indonésie] ; Mai Thi Quynh Le [Viêt Nam] ; Takashi Suzuki [Japon] ; Yoshihiro Kawaoka [États-Unis, Japon]Source :
- FEBS Open Bio [ 2211-5463 ] ; 2012.
Abstract
Avian influenza A viruses (IAVs) and human 1918, 1957, and 1968 pandemic IAVs all have neuraminidases (NAs) that are stable at low pH sialidase activity, yet most human epidemic IAVs do not. We examined the pH stability of H5N1 highly pathogenic avian IAV (HPAI) NAs and identified amino acids responsible for conferring stability at low pH. We found that, unlike other avian viruses, most H5N1 IAVs isolated since 2003 had NAs that were unstable at low pH, similar to human epidemic IAVs. These H5N1 viruses are thus already human virus-like and, therefore, have the frequent infections of humans.
Url:
DOI: 10.1016/j.fob.2012.08.007
PubMed: 23650608
PubMed Central: 3642167
Affiliations:
- Indonésie, Japon, Viêt Nam, États-Unis
- Région de Kantō, Wisconsin
- Madison (Wisconsin), Tokyo
- Université de Tokyo, Université du Wisconsin à Madison
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We examined the pH stability of H5N1 highly pathogenic avian IAV (HPAI) NAs and identified amino acids responsible for conferring stability at low pH. We found that, unlike other avian viruses, most H5N1 IAVs isolated since 2003 had NAs that were unstable at low pH, similar to human epidemic IAVs. These H5N1 viruses are thus already human virus-like and, therefore, have the frequent infections of humans.</p></div></front><back><div1 type="bibliography"><listBibl><biblStruct></biblStruct><biblStruct><analytic><author><name sortKey="Basler, C F" uniqKey="Basler C">C.F. Basler</name></author><author><name sortKey="Aguilar, P V" uniqKey="Aguilar P">P.V. Aguilar</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Uchida, Y" uniqKey="Uchida Y">Y. Uchida</name></author><author><name sortKey="Chaichoune, K" uniqKey="Chaichoune K">K. Chaichoune</name></author><author><name sortKey="Wiriyarat, W" uniqKey="Wiriyarat W">W. 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<front><journal-meta><journal-id journal-id-type="nlm-ta">FEBS Open Bio</journal-id><journal-id journal-id-type="iso-abbrev">FEBS Open Bio</journal-id><journal-title-group><journal-title>FEBS Open Bio</journal-title></journal-title-group><issn pub-type="epub">2211-5463</issn><publisher><publisher-name>Elsevier</publisher-name></publisher></journal-meta><article-meta><article-id pub-id-type="pmid">23650608</article-id><article-id pub-id-type="pmc">3642167</article-id><article-id pub-id-type="publisher-id">FOB46</article-id><article-id pub-id-type="doi">10.1016/j.fob.2012.08.007</article-id><article-categories><subj-group subj-group-type="heading"><subject>Article</subject></subj-group></article-categories><title-group><article-title>Amino acid determinants conferring stable sialidase activity at low pH for H5N1 influenza A virus neuraminidase</article-title></title-group><contrib-group><contrib contrib-type="author"><name><surname>Takahashi</surname><given-names>Tadanobu</given-names></name><xref rid="aff0001" ref-type="aff">a</xref><xref rid="aff0002" ref-type="aff">b</xref></contrib><contrib contrib-type="author"><name><surname>Nidom</surname><given-names>Chairul A.</given-names></name><xref rid="aff0003" ref-type="aff">c</xref></contrib><contrib contrib-type="author"><name><surname>Quynh Le</surname><given-names>Mai thi</given-names></name><xref rid="aff0004" ref-type="aff">d</xref></contrib><contrib contrib-type="author"><name><surname>Suzuki</surname><given-names>Takashi</given-names></name><email>suzukit@u-shizuoka-ken.ac.jp</email><xref rid="aff0002" ref-type="aff">b</xref><xref rid="cor0001" ref-type="corresp">*</xref></contrib><contrib contrib-type="author"><name><surname>Kawaoka</surname><given-names>Yoshihiro</given-names></name><email>kawaokay@svm.vetmed.wisc.edu</email><xref rid="aff0001" ref-type="aff">a</xref><xref rid="aff0005" ref-type="aff">e</xref><xref rid="aff0006" ref-type="aff">f</xref><xref rid="cor0001" ref-type="corresp">*</xref></contrib></contrib-group><aff id="aff0001"><label>a</label>Influenza Research Institute, Department of Pathobiological Sciences, School of Veterinary Medicine, University of Wisconsin-Madison, Madison, WI, USA</aff><aff id="aff0002"><label>b</label>Department of Biochemistry, School of Pharmaceutical Sciences, University of Shizuoka, and Global COE Program for Innovation in Human Health Sciences, Japan</aff><aff id="aff0003"><label>c</label>Faculty of Veterinary Medicine, Tropical Disease Centre, Airlangga University, Surabaya, Indonesia</aff><aff id="aff0004"><label>d</label>National Institute of Hygiene and Epidemiology, Hanoi, Viet Nam</aff><aff id="aff0005"><label>e</label>Division of Virology, Department of Microbiology and Immunology and International Research Center for Infectious Diseases, Institute of Medical Science, University of Tokyo, Shirokanedai, Minato-ku, Tokyo, Japan</aff><aff id="aff0006"><label>f</label>ERATO Infection-Induced Host Responses Project, Japan Science and Technology Agency, Saitama, Japan</aff><author-notes><corresp id="cor0001"><label>*</label>Takashi Suzuki; Department of Biochemistry, School of Pharmaceutical Sciences, University of Shizuoka, Shizuoka 422-8526, Japan (T. Suzuki),Yoshihiro Kawaoka; Influenza Research Institute, Department of Pathobiological Sciences, School of Veterinary Medicine, University of Wisconsin, Madison, Wisconsin 53711, USA (Y. Kawaoka). Tel.: +81 54 264 5725; fax: +81 54 264 5723 (T. Suzuki), Tel.: +1 608 265 4925; fax: +1 608 262 9641 (Y. Kawaoka). <email>suzukit@u-shizuoka-ken.ac.jp</email><email>kawaokay@svm.vetmed.wisc.edu</email></corresp></author-notes><pub-date pub-type="pmc-release"><day>5</day><month>9</month><year>2012</year></pub-date><pmc-comment> PMC Release delay is 0 months and 0 days and was based on .</pmc-comment>
<pub-date pub-type="epub"><day>5</day><month>9</month><year>2012</year></pub-date><pub-date pub-type="collection"><year>2012</year></pub-date><volume>2</volume><fpage>261</fpage><lpage>266</lpage><history><date date-type="received"><day>25</day><month>6</month><year>2012</year></date><date date-type="rev-recd"><day>29</day><month>8</month><year>2012</year></date><date date-type="accepted"><day>29</day><month>8</month><year>2012</year></date></history><permissions><copyright-statement>© 2012 Published by Elsevier B.V. on behalf of Federation of European Biochemical Societies.</copyright-statement><copyright-year>2012</copyright-year><copyright-holder>Federation of European Biochemical Societies</copyright-holder><license><license-p>This is an open-access article distributed under the terms of the Creative Commons Attribution-NonCommercial-No Derivative Works License, which permits non- commercial use, distribution, and reproduction in any medium, provided the original author and source are credited.</license-p></license></permissions><abstract><p>Avian influenza A viruses (IAVs) and human 1918, 1957, and 1968 pandemic IAVs all have neuraminidases (NAs) that are stable at low pH sialidase activity, yet most human epidemic IAVs do not. We examined the pH stability of H5N1 highly pathogenic avian IAV (HPAI) NAs and identified amino acids responsible for conferring stability at low pH. We found that, unlike other avian viruses, most H5N1 IAVs isolated since 2003 had NAs that were unstable at low pH, similar to human epidemic IAVs. These H5N1 viruses are thus already human virus-like and, therefore, have the frequent infections of humans.</p></abstract><abstract abstract-type="graphical"><title>Highlights</title><p>▸ All neuraminidases (NAs) of avian influenza A viruses (IAVs) are stable at low pH. ▸ Human 1918, 1957, and 1968 pandemic IAVs also have NAs that are stable at low pH. ▸ Most human epidemic IAVs have NAs that are unstable at low pH. ▸ The NAs of most H5N1 IAVs isolated since 2003 are unstable at low pH. ▸ Instability of H5N1 IAV NAs at low pH might explain frequent human infections.</p></abstract><kwd-group><title>Keywords</title><kwd>Avian influenza A virus</kwd><kwd>H5N1</kwd><kwd>Highly pathogenic</kwd><kwd>Low-pH stability</kwd><kwd>Neuraminidase</kwd><kwd>Sialidase</kwd></kwd-group><kwd-group><title>Abbreviations</title><kwd>FBS, fetal bovine serum</kwd><kwd>HA, hemagglutinin</kwd><kwd>HPAI, highly pathogenic avian influenza A virus</kwd><kwd>IAV, influenza A virus</kwd><kwd>NA, neuraminidase</kwd><kwd>PBS, phosphate-buffered saline</kwd><kwd>TGF-β, transforming growth factor-beta</kwd></kwd-group></article-meta></front><floats-group><fig id="fig0001"><label>Fig. 1</label><caption><p>The low-pH stabilities of the sialidase activities of H5N1 HPAI NAs, human H1N1 IAV NAs, and non-H5N1 avian IAV NAs. Sialidase activities of NA-expressing cells transfected with each NA gene were measured at pH 4.0 (filled columns), 5.0 (gray columns) and 6.0 (open columns). Sialidase activities are expressed as a percentage of each activity at pH 6.0. The NA genes used were derived from H5N1 HPAIs isolated from humans (A), aquatic birds (B), chickens (C), other avian IAVs (D) and from human H1N1 IAVs (E).</p></caption><graphic xlink:href="gr1"></graphic></fig><fig id="fig0002"><label>Fig. 2</label><caption><p>Identification of amino acid residues responsible for the low-pH stability of DKG/1 NA and HK/213 NA. Sialidase activities were measured as described in the legend to Fig. 1. A, Low-pH stabilities of chimeric NAs. B, Low-pH stabilities of chimeric NAs with the Y155H or H155Y mutation at position 155. C, Low-pH stabilities of mutated DKG/1 NAs. D, Low-pH stabilities of mutated HK/213 NAs.</p></caption><graphic xlink:href="gr2"></graphic></fig><fig id="fig0003"><label>Fig. 3</label><caption><p>Locations of the amino acid residues responsible for the low-pH stabilities of H5N1 HPAI NAs. One subunit of the NA homotetramer structure (2HTY. pdb, VN/1203) is shown in gray. In the surface model of NA, red and purple indicate the active site and the calcium ion-binding site, respectively. The residues at positions 155 and 341 are colored in green and blue, respectively (DKG/1 NA numbering). Pictures were generated by using the Pymol Molecular Graphics System Ver. 1.1r1 (DeLano Scientific LLC).</p></caption><graphic xlink:href="gr3"></graphic></fig><table-wrap id="tbl0001" position="float"><label>Table 1</label><caption><p>Amino acid comparison of the NA globular domains between DKG/1 and HK/213.</p></caption><table frame="hsides" rules="groups"><tbody><tr><td align="center"><inline-graphic xlink:href="fx1.gif"></inline-graphic></td></tr></tbody></table><table-wrap-foot><fn><p><sup>a</sup>Amino acid position is based on DKG/1 NA numbering.</p><p><sup>b</sup>Positions in the NA amino acid sequence involved in creating the chimeric NAs.</p><p><sup>c</sup>Boxed amino acids are responsible for the low-pH stability of DKG/1 NA and HK/213 NA.</p></fn></table-wrap-foot></table-wrap></floats-group></pmc><affiliations><list><country><li>Indonésie</li><li>Japon</li><li>Viêt Nam</li><li>États-Unis</li></country><region><li>Région de Kantō</li><li>Wisconsin</li></region><settlement><li>Madison (Wisconsin)</li><li>Tokyo</li></settlement><orgName><li>Université de Tokyo</li><li>Université du Wisconsin à Madison</li></orgName></list><tree><country name="États-Unis"><region name="Wisconsin"><name sortKey="Takahashi, Tadanobu" sort="Takahashi, Tadanobu" uniqKey="Takahashi T" first="Tadanobu" last="Takahashi">Tadanobu Takahashi</name></region><name sortKey="Kawaoka, Yoshihiro" sort="Kawaoka, Yoshihiro" uniqKey="Kawaoka Y" first="Yoshihiro" last="Kawaoka">Yoshihiro Kawaoka</name></country><country name="Japon"><noRegion><name sortKey="Takahashi, Tadanobu" sort="Takahashi, Tadanobu" uniqKey="Takahashi T" first="Tadanobu" last="Takahashi">Tadanobu Takahashi</name></noRegion><name sortKey="Kawaoka, Yoshihiro" sort="Kawaoka, Yoshihiro" uniqKey="Kawaoka Y" first="Yoshihiro" last="Kawaoka">Yoshihiro Kawaoka</name><name sortKey="Kawaoka, Yoshihiro" sort="Kawaoka, Yoshihiro" uniqKey="Kawaoka Y" first="Yoshihiro" last="Kawaoka">Yoshihiro Kawaoka</name><name sortKey="Suzuki, Takashi" sort="Suzuki, Takashi" uniqKey="Suzuki T" first="Takashi" last="Suzuki">Takashi Suzuki</name></country><country name="Indonésie"><noRegion><name sortKey="Nidom, Chairul A" sort="Nidom, Chairul A" uniqKey="Nidom C" first="Chairul A." last="Nidom">Chairul A. Nidom</name></noRegion></country><country name="Viêt Nam"><noRegion><name sortKey="Quynh Le, Mai Thi" sort="Quynh Le, Mai Thi" uniqKey="Quynh Le M" first="Mai Thi" last="Quynh Le">Mai Thi Quynh Le</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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