Links to Exploration step
Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Fitness costs limit influenza A virus hemagglutinin glycosylation as an immune evasion strategy</title><author><name sortKey="Das, Suman R" sort="Das, Suman R" uniqKey="Das S" first="Suman R." last="Das">Suman R. Das</name><affiliation><nlm:aff id="aff1">Laboratory of Viral Diseases, National Institute of Allergy and Infectious Diseases,<institution>National Institutes of Health</institution>, Bethesda, MD 20892;</nlm:aff></affiliation><affiliation><nlm:aff wicri:cut="; and" id="aff2">Emory Vaccine Center,<institution>Emory University</institution>, Atlanta, GA 30322</nlm:aff></affiliation></author><author><name sortKey="Hensley, Scott E" sort="Hensley, Scott E" uniqKey="Hensley S" first="Scott E." last="Hensley">Scott E. Hensley</name><affiliation><nlm:aff id="aff1">Laboratory of Viral Diseases, National Institute of Allergy and Infectious Diseases,<institution>National Institutes of Health</institution>, Bethesda, MD 20892;</nlm:aff></affiliation></author><author><name sortKey="David, Alexandre" sort="David, Alexandre" uniqKey="David A" first="Alexandre" last="David">Alexandre David</name><affiliation><nlm:aff id="aff1">Laboratory of Viral Diseases, National Institute of Allergy and Infectious Diseases,<institution>National Institutes of Health</institution>, Bethesda, MD 20892;</nlm:aff></affiliation></author><author><name sortKey="Schmidt, Loren" sort="Schmidt, Loren" uniqKey="Schmidt L" first="Loren" last="Schmidt">Loren Schmidt</name><affiliation><nlm:aff id="aff1">Laboratory of Viral Diseases, National Institute of Allergy and Infectious Diseases,<institution>National Institutes of Health</institution>, Bethesda, MD 20892;</nlm:aff></affiliation></author><author><name sortKey="Gibbs, James S" sort="Gibbs, James S" uniqKey="Gibbs J" first="James S." last="Gibbs">James S. Gibbs</name><affiliation><nlm:aff id="aff1">Laboratory of Viral Diseases, National Institute of Allergy and Infectious Diseases,<institution>National Institutes of Health</institution>, Bethesda, MD 20892;</nlm:aff></affiliation></author><author><name sortKey="Puigb, Pere" sort="Puigb, Pere" uniqKey="Puigb P" first="Pere" last="Puigb">Pere Puigb</name><affiliation><nlm:aff id="aff3">National Center for Biotechnology Information, National Library of Medicine,<institution>National Institutes of Health</institution>, Bethesda, MD 20894</nlm:aff></affiliation></author><author><name sortKey="Ince, William L" sort="Ince, William L" uniqKey="Ince W" first="William L." last="Ince">William L. Ince</name><affiliation><nlm:aff id="aff1">Laboratory of Viral Diseases, National Institute of Allergy and Infectious Diseases,<institution>National Institutes of Health</institution>, Bethesda, MD 20892;</nlm:aff></affiliation></author><author><name sortKey="Bennink, Jack R" sort="Bennink, Jack R" uniqKey="Bennink J" first="Jack R." last="Bennink">Jack R. Bennink</name><affiliation><nlm:aff id="aff1">Laboratory of Viral Diseases, National Institute of Allergy and Infectious Diseases,<institution>National Institutes of Health</institution>, Bethesda, MD 20892;</nlm:aff></affiliation></author><author><name sortKey="Yewdell, Jonathan W" sort="Yewdell, Jonathan W" uniqKey="Yewdell J" first="Jonathan W." last="Yewdell">Jonathan W. Yewdell</name><affiliation><nlm:aff id="aff1">Laboratory of Viral Diseases, National Institute of Allergy and Infectious Diseases,<institution>National Institutes of Health</institution>, Bethesda, MD 20892;</nlm:aff></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PMC</idno><idno type="pmid">22106257</idno><idno type="pmc">3251056</idno><idno type="url">http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3251056</idno><idno type="RBID">PMC:3251056</idno><idno type="doi">10.1073/pnas.1108754108</idno><date when="2011">2011</date><idno type="wicri:Area/Pmc/Corpus">000752</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Corpus" wicri:corpus="PMC">000752</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en" level="a" type="main">Fitness costs limit influenza A virus hemagglutinin glycosylation as an immune evasion strategy</title><author><name sortKey="Das, Suman R" sort="Das, Suman R" uniqKey="Das S" first="Suman R." last="Das">Suman R. Das</name><affiliation><nlm:aff id="aff1">Laboratory of Viral Diseases, National Institute of Allergy and Infectious Diseases,<institution>National Institutes of Health</institution>, Bethesda, MD 20892;</nlm:aff></affiliation><affiliation><nlm:aff wicri:cut="; and" id="aff2">Emory Vaccine Center,<institution>Emory University</institution>, Atlanta, GA 30322</nlm:aff></affiliation></author><author><name sortKey="Hensley, Scott E" sort="Hensley, Scott E" uniqKey="Hensley S" first="Scott E." last="Hensley">Scott E. Hensley</name><affiliation><nlm:aff id="aff1">Laboratory of Viral Diseases, National Institute of Allergy and Infectious Diseases,<institution>National Institutes of Health</institution>, Bethesda, MD 20892;</nlm:aff></affiliation></author><author><name sortKey="David, Alexandre" sort="David, Alexandre" uniqKey="David A" first="Alexandre" last="David">Alexandre David</name><affiliation><nlm:aff id="aff1">Laboratory of Viral Diseases, National Institute of Allergy and Infectious Diseases,<institution>National Institutes of Health</institution>, Bethesda, MD 20892;</nlm:aff></affiliation></author><author><name sortKey="Schmidt, Loren" sort="Schmidt, Loren" uniqKey="Schmidt L" first="Loren" last="Schmidt">Loren Schmidt</name><affiliation><nlm:aff id="aff1">Laboratory of Viral Diseases, National Institute of Allergy and Infectious Diseases,<institution>National Institutes of Health</institution>, Bethesda, MD 20892;</nlm:aff></affiliation></author><author><name sortKey="Gibbs, James S" sort="Gibbs, James S" uniqKey="Gibbs J" first="James S." last="Gibbs">James S. Gibbs</name><affiliation><nlm:aff id="aff1">Laboratory of Viral Diseases, National Institute of Allergy and Infectious Diseases,<institution>National Institutes of Health</institution>, Bethesda, MD 20892;</nlm:aff></affiliation></author><author><name sortKey="Puigb, Pere" sort="Puigb, Pere" uniqKey="Puigb P" first="Pere" last="Puigb">Pere Puigb</name><affiliation><nlm:aff id="aff3">National Center for Biotechnology Information, National Library of Medicine,<institution>National Institutes of Health</institution>, Bethesda, MD 20894</nlm:aff></affiliation></author><author><name sortKey="Ince, William L" sort="Ince, William L" uniqKey="Ince W" first="William L." last="Ince">William L. Ince</name><affiliation><nlm:aff id="aff1">Laboratory of Viral Diseases, National Institute of Allergy and Infectious Diseases,<institution>National Institutes of Health</institution>, Bethesda, MD 20892;</nlm:aff></affiliation></author><author><name sortKey="Bennink, Jack R" sort="Bennink, Jack R" uniqKey="Bennink J" first="Jack R." last="Bennink">Jack R. Bennink</name><affiliation><nlm:aff id="aff1">Laboratory of Viral Diseases, National Institute of Allergy and Infectious Diseases,<institution>National Institutes of Health</institution>, Bethesda, MD 20892;</nlm:aff></affiliation></author><author><name sortKey="Yewdell, Jonathan W" sort="Yewdell, Jonathan W" uniqKey="Yewdell J" first="Jonathan W." last="Yewdell">Jonathan W. Yewdell</name><affiliation><nlm:aff id="aff1">Laboratory of Viral Diseases, National Institute of Allergy and Infectious Diseases,<institution>National Institutes of Health</institution>, Bethesda, MD 20892;</nlm:aff></affiliation></author></analytic><series><title level="j">Proceedings of the National Academy of Sciences of the United States of America</title><idno type="ISSN">0027-8424</idno><idno type="eISSN">1091-6490</idno><imprint><date when="2011">2011</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><p>Here, we address the question of why the influenza A virus hemagglutinin (HA) does not escape immunity by hyperglycosylation. Uniquely among dozens of monoclonal antibodies specific for A/Puerto Rico/8/34, escape from H28-A2 neutralization requires substitutions introducing N-linked glycosylation at residue 131 or 144 in the globular domain. This escape decreases viral binding to cellular receptors, which must be compensated for by additional substitutions in HA or neuraminidase that enable viral replication. Sequence analysis of circulating H1 influenza viruses confirms the in vivo relevance of our findings: natural occurrence of glycosylation at residue 131 is always accompanied by a compensatory mutation known to increase HA receptor avidity. In vaccinated mice challenged with WT vs. H28-A2 escape mutants, the selective advantage conferred by glycan-mediated global reduction in antigenicity is trumped by the costs of diminished receptor avidity. These findings show that, although N-linked glycosylation can broadly diminish HA antigenicity, fitness costs restrict its deployment in immune evasion.</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">Proc Natl Acad Sci U S A</journal-id><journal-id journal-id-type="hwp">pnas</journal-id><journal-id journal-id-type="pmc">pnas</journal-id><journal-id journal-id-type="publisher-id">PNAS</journal-id><journal-title-group><journal-title>Proceedings of the National Academy of Sciences of the United States of America</journal-title></journal-title-group><issn pub-type="ppub">0027-8424</issn><issn pub-type="epub">1091-6490</issn><publisher><publisher-name>National Academy of Sciences</publisher-name></publisher></journal-meta><article-meta><article-id pub-id-type="pmid">22106257</article-id><article-id pub-id-type="pmc">3251056</article-id><article-id pub-id-type="publisher-id">201108754</article-id><article-id pub-id-type="doi">10.1073/pnas.1108754108</article-id><article-categories><subj-group subj-group-type="heading"><subject>PNAS Plus</subject></subj-group><subj-group subj-group-type="heading"><subject>Biological Sciences</subject><subj-group><subject>Microbiology</subject></subj-group></subj-group><series-title>PNAS Plus</series-title></article-categories><title-group><article-title>Fitness costs limit influenza A virus hemagglutinin glycosylation as an immune evasion strategy</article-title></title-group><contrib-group><contrib contrib-type="author"><name><surname>Das</surname><given-names>Suman R.</given-names></name><xref ref-type="aff" rid="aff1"><sup>a</sup></xref><xref ref-type="aff" rid="aff2"><sup>b</sup></xref><xref ref-type="author-notes" rid="fn1"><sup>1</sup></xref></contrib><contrib contrib-type="author"><name><surname>Hensley</surname><given-names>Scott E.</given-names></name><xref ref-type="aff" rid="aff1"><sup>a</sup></xref><xref ref-type="author-notes" rid="fn2"><sup>2</sup></xref></contrib><contrib contrib-type="author"><name><surname>David</surname><given-names>Alexandre</given-names></name><xref ref-type="aff" rid="aff1"><sup>a</sup></xref></contrib><contrib contrib-type="author"><name><surname>Schmidt</surname><given-names>Loren</given-names></name><xref ref-type="aff" rid="aff1"><sup>a</sup></xref></contrib><contrib contrib-type="author"><name><surname>Gibbs</surname><given-names>James S.</given-names></name><xref ref-type="aff" rid="aff1"><sup>a</sup></xref></contrib><contrib contrib-type="author"><name><surname>Puigbò</surname><given-names>Pere</given-names></name><xref ref-type="aff" rid="aff3"><sup>c</sup></xref></contrib><contrib contrib-type="author"><name><surname>Ince</surname><given-names>William L.</given-names></name><xref ref-type="aff" rid="aff1"><sup>a</sup></xref></contrib><contrib contrib-type="author"><name><surname>Bennink</surname><given-names>Jack R.</given-names></name><xref ref-type="aff" rid="aff1"><sup>a</sup></xref></contrib><contrib contrib-type="author"><name><surname>Yewdell</surname><given-names>Jonathan W.</given-names></name><xref ref-type="aff" rid="aff1"><sup>a</sup></xref><xref ref-type="corresp" rid="cor1"><sup>3</sup></xref></contrib><aff id="aff1"><sup>a</sup>Laboratory of Viral Diseases, National Institute of Allergy and Infectious Diseases,<institution>National Institutes of Health</institution>, Bethesda, MD 20892;</aff><aff id="aff2"><sup>b</sup>Emory Vaccine Center,<institution>Emory University</institution>, Atlanta, GA 30322; and</aff><aff id="aff3"><sup>c</sup>National Center for Biotechnology Information, National Library of Medicine,<institution>National Institutes of Health</institution>, Bethesda, MD 20894</aff></contrib-group><author-notes><corresp id="cor1"><sup>3</sup>To whom correspondence should be addressed. E-mail: <email>jyewdell@niaid.nih.gov</email>.</corresp><fn fn-type="edited-by"><p>Edited by Peter Palese, Mount Sinai School of Medicine, New York, NY, and approved October 21, 2011 (received for review June 16, 2011)</p></fn><fn fn-type="con"><p>Author contributions: S.R.D., J.R.B., and J.W.Y. designed research; S.R.D., S.E.H., A.D., L.S., J.S.G., P.P., W.L.I., and J.W.Y. performed research; S.R.D. contributed new reagents/analytic tools; S.R.D., S.E.H., A.D., L.S., J.S.G., P.P., W.L.I., J.R.B., and J.W.Y. analyzed data; and S.R.D., J.R.B., and J.W.Y. wrote the paper.</p></fn><fn id="fn1" fn-type="present-address"><p><sup>1</sup>Present address: Infectious Diseases Group, J. Craig Venter Institute, Rockville, MD 20852.</p></fn><fn id="fn2" fn-type="present-address"><p><sup>2</sup>Present address: Immunology Program, The Wistar Institute, Philadelphia, PA 19130.</p></fn><fn fn-type="conflict"><p>The authors declare no conflict of interest.</p></fn></author-notes><pub-date pub-type="ppub"><day>20</day><month>12</month><year>2011</year></pub-date><pub-date pub-type="epub"><day>21</day><month>11</month><year>2011</year></pub-date><volume>108</volume><issue>51</issue><fpage>E1417</fpage><lpage>E1422</lpage><page-range>E1417–E1422</page-range><self-uri content-type="pdf" xlink:type="simple" xlink:href="pnas.201108754.pdf"></self-uri><self-uri content-type="author-summary-pdf" xlink:type="simple" xlink:href="pnas.201108754_summary.pdf"></self-uri><abstract id="d32e209"><p>Here, we address the question of why the influenza A virus hemagglutinin (HA) does not escape immunity by hyperglycosylation. Uniquely among dozens of monoclonal antibodies specific for A/Puerto Rico/8/34, escape from H28-A2 neutralization requires substitutions introducing N-linked glycosylation at residue 131 or 144 in the globular domain. This escape decreases viral binding to cellular receptors, which must be compensated for by additional substitutions in HA or neuraminidase that enable viral replication. Sequence analysis of circulating H1 influenza viruses confirms the in vivo relevance of our findings: natural occurrence of glycosylation at residue 131 is always accompanied by a compensatory mutation known to increase HA receptor avidity. In vaccinated mice challenged with WT vs. H28-A2 escape mutants, the selective advantage conferred by glycan-mediated global reduction in antigenicity is trumped by the costs of diminished receptor avidity. These findings show that, although N-linked glycosylation can broadly diminish HA antigenicity, fitness costs restrict its deployment in immune evasion.</p></abstract><kwd-group><kwd>antigenic drift</kwd><kwd>viral evolution</kwd></kwd-group><custom-meta-group><custom-meta><meta-name>author-summary</meta-name><meta-value><xref ref-type="other" rid="author-summary"></xref></meta-value></custom-meta></custom-meta-group></article-meta></front></pmc></record>Pour manipuler ce document sous Unix (Dilib)
EXPLOR_STEP=$WICRI_ROOT/Sante/explor/H2N2V1/Data/Pmc/Corpus
HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 000752 | SxmlIndent | more
Ou
HfdSelect -h $EXPLOR_AREA/Data/Pmc/Corpus/biblio.hfd -nk 000752 | SxmlIndent | more
Pour mettre un lien sur cette page dans le réseau Wicri
{{Explor lien
|wiki= Sante
|area= H2N2V1
|flux= Pmc
|étape= Corpus
|type= RBID
|clé=
|texte=
}}
| This area was generated with Dilib version V0.6.33. |  |