The structural variability of the influenza A hemagglutinin receptor-binding site
Identifieur interne : 000185 ( Pmc/Checkpoint ); précédent : 000184; suivant : 000186The structural variability of the influenza A hemagglutinin receptor-binding site
Auteurs : Michal Lazniewski [Pologne] ; Wayne K. Dawson [Pologne] ; Teresa Szczepi Ska [Pologne] ; Dariusz Plewczynski [Pologne]Source :
- Briefings in Functional Genomics [ 2041-2649 ] ; 2017.
Abstract
Hemagglutinin (HA) is a transmembrane protein of the influenza A virus and a key component in its life cycle. The protein allows the virus to enter a host cell by recognizing specific glycans attached to transmembrane proteins of the host, which leads to viral endocytosis. In recent years, significant progress has been made in understanding the structural relationship between changes in the HA receptor-binding site (RBS) and the sialylated glycans that bind them. Several mutations were identified in the HA RBS that allows the virus to change host tropism. Their impact on binding the analogs of human and avian receptors was determined with X-ray crystallography. In this article, we provide a short overview of the HA protein structure and briefly discuss the adaptive mutations introduced to different HA subtypes.
Url:
DOI: 10.1093/bfgp/elx042
PubMed: 29253080
PubMed Central: 6252403
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Dawson</name><affiliation wicri:level="1"><nlm:aff id="aff1">University of Warsaw, Center of New Technologies (CeNT), Warsaw, Poland</nlm:aff><country xml:lang="fr">Pologne</country><wicri:regionArea>University of Warsaw, Center of New Technologies (CeNT), Warsaw</wicri:regionArea><wicri:noRegion>Warsaw</wicri:noRegion></affiliation><affiliation><nlm:aff id="aff3">Bio-information Lab in Yayoi campus at the University of Tokyo</nlm:aff></affiliation></author><author><name sortKey="Szczepi Ska, Teresa" sort="Szczepi Ska, Teresa" uniqKey="Szczepi Ska T" first="Teresa" last="Szczepi Ska">Teresa Szczepi Ska</name><affiliation wicri:level="1"><nlm:aff id="aff4">Professor Dariusz Plewczyński Laboratory at Center of New Technologies, Warsaw, Poland</nlm:aff><country xml:lang="fr">Pologne</country><wicri:regionArea>Professor Dariusz Plewczyński Laboratory at Center of New Technologies, Warsaw</wicri:regionArea><wicri:noRegion>Warsaw</wicri:noRegion></affiliation></author><author><name sortKey="Plewczynski, Dariusz" sort="Plewczynski, Dariusz" uniqKey="Plewczynski D" first="Dariusz" last="Plewczynski">Dariusz Plewczynski</name><affiliation wicri:level="1"><nlm:aff id="aff1">University of Warsaw, Center of New Technologies (CeNT), Warsaw, Poland</nlm:aff><country xml:lang="fr">Pologne</country><wicri:regionArea>University of Warsaw, Center of New Technologies (CeNT), Warsaw</wicri:regionArea><wicri:noRegion>Warsaw</wicri:noRegion></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PMC</idno><idno type="pmid">29253080</idno><idno type="pmc">6252403</idno><idno type="url">http://www.ncbi.nlm.nih.gov/pmc/articles/PMC6252403</idno><idno type="RBID">PMC:6252403</idno><idno type="doi">10.1093/bfgp/elx042</idno><date when="2017">2017</date><idno type="wicri:Area/Pmc/Corpus">000932</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Corpus" wicri:corpus="PMC">000932</idno><idno type="wicri:Area/Pmc/Curation">000932</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Curation">000932</idno><idno type="wicri:Area/Pmc/Checkpoint">000185</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Checkpoint">000185</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en" level="a" type="main">The structural variability of the influenza A hemagglutinin receptor-binding site</title><author><name sortKey="Lazniewski, Michal" sort="Lazniewski, Michal" uniqKey="Lazniewski M" first="Michal" last="Lazniewski">Michal Lazniewski</name><affiliation wicri:level="1"><nlm:aff id="aff1">University of Warsaw, Center of New Technologies (CeNT), Warsaw, Poland</nlm:aff><country xml:lang="fr">Pologne</country><wicri:regionArea>University of Warsaw, Center of New Technologies (CeNT), Warsaw</wicri:regionArea><wicri:noRegion>Warsaw</wicri:noRegion></affiliation><affiliation wicri:level="1"><nlm:aff id="aff2">Department of Physical Chemistry in the Faculty of Pharmacy at the Medical University of Warsaw, Poland</nlm:aff><country xml:lang="fr">Pologne</country><wicri:regionArea>Department of Physical Chemistry in the Faculty of Pharmacy at the Medical University of Warsaw</wicri:regionArea></affiliation></author><author><name sortKey="Dawson, Wayne K" sort="Dawson, Wayne K" uniqKey="Dawson W" first="Wayne K" last="Dawson">Wayne K. Dawson</name><affiliation wicri:level="1"><nlm:aff id="aff1">University of Warsaw, Center of New Technologies (CeNT), Warsaw, Poland</nlm:aff><country xml:lang="fr">Pologne</country><wicri:regionArea>University of Warsaw, Center of New Technologies (CeNT), Warsaw</wicri:regionArea><wicri:noRegion>Warsaw</wicri:noRegion></affiliation><affiliation><nlm:aff id="aff3">Bio-information Lab in Yayoi campus at the University of Tokyo</nlm:aff></affiliation></author><author><name sortKey="Szczepi Ska, Teresa" sort="Szczepi Ska, Teresa" uniqKey="Szczepi Ska T" first="Teresa" last="Szczepi Ska">Teresa Szczepi Ska</name><affiliation wicri:level="1"><nlm:aff id="aff4">Professor Dariusz Plewczyński Laboratory at Center of New Technologies, Warsaw, Poland</nlm:aff><country xml:lang="fr">Pologne</country><wicri:regionArea>Professor Dariusz Plewczyński Laboratory at Center of New Technologies, Warsaw</wicri:regionArea><wicri:noRegion>Warsaw</wicri:noRegion></affiliation></author><author><name sortKey="Plewczynski, Dariusz" sort="Plewczynski, Dariusz" uniqKey="Plewczynski D" first="Dariusz" last="Plewczynski">Dariusz Plewczynski</name><affiliation wicri:level="1"><nlm:aff id="aff1">University of Warsaw, Center of New Technologies (CeNT), Warsaw, Poland</nlm:aff><country xml:lang="fr">Pologne</country><wicri:regionArea>University of Warsaw, Center of New Technologies (CeNT), Warsaw</wicri:regionArea><wicri:noRegion>Warsaw</wicri:noRegion></affiliation></author></analytic><series><title level="j">Briefings in Functional Genomics</title><idno type="ISSN">2041-2649</idno><idno type="eISSN">2041-2657</idno><imprint><date when="2017">2017</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><title>Abstract</title><p>Hemagglutinin (HA) is a transmembrane protein of the influenza A virus and a key component in its life cycle. The protein allows the virus to enter a host cell by recognizing specific glycans attached to transmembrane proteins of the host, which leads to viral endocytosis. In recent years, significant progress has been made in understanding the structural relationship between changes in the HA receptor-binding site (RBS) and the sialylated glycans that bind them. Several mutations were identified in the HA RBS that allows the virus to change host tropism. Their impact on binding the analogs of human and avian receptors was determined with X-ray crystallography. 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<front><journal-meta><journal-id journal-id-type="nlm-ta">Brief Funct Genomics</journal-id><journal-id journal-id-type="iso-abbrev">Brief Funct Genomics</journal-id><journal-id journal-id-type="publisher-id">bfgp</journal-id><journal-title-group><journal-title>Briefings in Functional Genomics</journal-title></journal-title-group><issn pub-type="ppub">2041-2649</issn><issn pub-type="epub">2041-2657</issn><publisher><publisher-name>Oxford University Press</publisher-name></publisher></journal-meta><article-meta><article-id pub-id-type="pmid">29253080</article-id><article-id pub-id-type="pmc">6252403</article-id><article-id pub-id-type="doi">10.1093/bfgp/elx042</article-id><article-id pub-id-type="publisher-id">elx042</article-id><article-categories><subj-group subj-group-type="heading"><subject>Paper</subject></subj-group></article-categories><title-group><article-title>The structural variability of the influenza A hemagglutinin receptor-binding site</article-title></title-group><contrib-group><contrib contrib-type="author"><name><surname>Lazniewski</surname><given-names>Michal</given-names></name><pmc-comment>m.lazniewski@cent.uw.edu.pl </pmc-comment>
<xref ref-type="aff" rid="aff1">1</xref><xref ref-type="aff" rid="aff2">2</xref><xref ref-type="corresp" rid="cor1"></xref></contrib><contrib contrib-type="author"><contrib-id contrib-id-type="orcid" authenticated="false">http://orcid.org/0000-0001-7751-7778</contrib-id><name><surname>Dawson</surname><given-names>Wayne K</given-names></name><xref ref-type="aff" rid="aff1">1</xref><xref ref-type="aff" rid="aff3">3</xref></contrib><contrib contrib-type="author"><name><surname>Szczepińska</surname><given-names>Teresa</given-names></name><xref ref-type="aff" rid="aff4">4</xref></contrib><contrib contrib-type="author"><name><surname>Plewczynski</surname><given-names>Dariusz</given-names></name><pmc-comment>dariuszplewczynski@cent.uw.edu.pl </pmc-comment>
<xref ref-type="aff" rid="aff1">1</xref><xref ref-type="corresp" rid="cor1"></xref></contrib></contrib-group><aff id="aff1"><label>1</label>University of Warsaw, Center of New Technologies (CeNT), Warsaw, Poland</aff><aff id="aff2"><label>2</label>Department of Physical Chemistry in the Faculty of Pharmacy at the Medical University of Warsaw, Poland</aff><aff id="aff3"><label>3</label>Bio-information Lab in Yayoi campus at the University of Tokyo</aff><aff id="aff4"><label>4</label>Professor Dariusz Plewczyński Laboratory at Center of New Technologies, Warsaw, Poland</aff><author-notes><corresp id="cor1">Corresponding authors. Michal Lazniewski, Laboratory of Functional and Structural Genomics, Centre of New Technologies, University of Warsaw, Banacha 2c, Warsaw 02-097, Poland. E-mail: <email>m.lazniewski@cent.uw.edu.pl</email>, Dariusz Plewczynski, Laboratory of Functional and Structural Genomics, Centre of New Technologies, University of Warsaw, Banacha 2c, Warsaw 02-097, Poland. E-mail: <email>dariuszplewczynski@cent.uw.edu.pl</email></corresp></author-notes><pub-date pub-type="collection"><month>11</month><year>2018</year></pub-date><pub-date pub-type="epub" iso-8601-date="2017-12-13"><day>13</day><month>12</month><year>2017</year></pub-date><pub-date pub-type="pmc-release"><day>13</day><month>12</month><year>2017</year></pub-date><pmc-comment> PMC Release delay is 0 months and 0 days and was based on the
<volume>17</volume><issue>6</issue><fpage>415</fpage><lpage>427</lpage><permissions><copyright-statement>© The Author(s) 2017. Published by Oxford University Press.</copyright-statement><copyright-year>2017</copyright-year><license license-type="cc-by-nc" xlink:href="http://creativecommons.org/licenses/by-nc/4.0/"><license-p>This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (<ext-link ext-link-type="uri" xlink:href="http://creativecommons.org/licenses/by-nc/4.0/">http://creativecommons.org/licenses/by-nc/4.0/</ext-link>), which permits non-commercial re-use, distribution, and reproduction in any medium, provided the original work is properly cited. For commercial re-use, please contact journals.permissions@oup.com</license-p></license></permissions><self-uri xlink:href="elx042.pdf"></self-uri><abstract><title>Abstract</title><p>Hemagglutinin (HA) is a transmembrane protein of the influenza A virus and a key component in its life cycle. The protein allows the virus to enter a host cell by recognizing specific glycans attached to transmembrane proteins of the host, which leads to viral endocytosis. In recent years, significant progress has been made in understanding the structural relationship between changes in the HA receptor-binding site (RBS) and the sialylated glycans that bind them. Several mutations were identified in the HA RBS that allows the virus to change host tropism. Their impact on binding the analogs of human and avian receptors was determined with X-ray crystallography. In this article, we provide a short overview of the HA protein structure and briefly discuss the adaptive mutations introduced to different HA subtypes.</p></abstract><kwd-group kwd-group-type="author"><kwd>influenza A virus</kwd><kwd>hemagglutinin</kwd><kwd>host tropism</kwd><kwd>adaptive mutations</kwd></kwd-group><funding-group><award-group award-type="grant"><funding-source><named-content content-type="funder-name">Polish National Science Centre</named-content><named-content content-type="funder-identifier">10.13039/501100004281</named-content></funding-source><award-id>2014/15/B/ST6/05082</award-id><award-id>2013/09/B/NZ2/00121</award-id></award-group><award-group award-type="grant"><funding-source><named-content content-type="funder-name">Foundation for Polish Science</named-content><named-content content-type="funder-identifier">10.13039/501100001870</named-content></funding-source><award-id>TEAM</award-id></award-group><award-group award-type="grant"><funding-source><named-content content-type="funder-name">‘Nucleome Positioning System for Spatiotemporal Genome Organization and Regulation’ within 4DNucleome NIH program</named-content></funding-source><award-id>1U54DK107967-01</award-id></award-group></funding-group><counts><page-count count="13"></page-count></counts></article-meta></front></pmc><affiliations><list><country><li>Pologne</li></country></list><tree><country name="Pologne"><noRegion><name sortKey="Lazniewski, Michal" sort="Lazniewski, Michal" uniqKey="Lazniewski M" first="Michal" last="Lazniewski">Michal Lazniewski</name></noRegion><name sortKey="Dawson, Wayne K" sort="Dawson, Wayne K" uniqKey="Dawson W" first="Wayne K" last="Dawson">Wayne K. Dawson</name><name sortKey="Lazniewski, Michal" sort="Lazniewski, Michal" uniqKey="Lazniewski M" first="Michal" last="Lazniewski">Michal Lazniewski</name><name sortKey="Plewczynski, Dariusz" sort="Plewczynski, Dariusz" uniqKey="Plewczynski D" first="Dariusz" last="Plewczynski">Dariusz Plewczynski</name><name sortKey="Szczepi Ska, Teresa" sort="Szczepi Ska, Teresa" uniqKey="Szczepi Ska T" first="Teresa" last="Szczepi Ska">Teresa Szczepi Ska</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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