Playing Hide and Seek: How Glycosylation of the Influenza Virus Hemagglutinin Can Modulate the Immune Response to Infection
Identifieur interne : 000E34 ( Pmc/Curation ); précédent : 000E33; suivant : 000E35Playing Hide and Seek: How Glycosylation of the Influenza Virus Hemagglutinin Can Modulate the Immune Response to Infection
Auteurs : Michelle D. Tate ; Emma R. Job ; Yi-Mo Deng ; Vithiagaran Gunalan ; Sebastian Maurer-Stroh [Singapour] ; Patrick C. ReadingSource :
- Viruses [ 1999-4915 ] ; 2014.
Abstract
Seasonal influenza A viruses (IAV) originate from pandemic IAV and have undergone changes in antigenic structure, including addition of glycans to the hemagglutinin (HA) glycoprotein. The viral HA is the major target recognized by neutralizing antibodies and glycans have been proposed to shield antigenic sites on HA, thereby promoting virus survival in the face of widespread vaccination and/or infection. However, addition of glycans can also interfere with the receptor binding properties of HA and this must be compensated for by additional mutations, creating a fitness barrier to accumulation of glycosylation sites. In addition, glycans on HA are also recognized by phylogenetically ancient lectins of the innate immune system and the benefit provided by evasion of humoral immunity is balanced by attenuation of infection. Therefore, a fine balance must exist regarding the optimal pattern of HA glycosylation to offset competing pressures associated with recognition by innate defenses, evasion of humoral immunity and maintenance of virus fitness. In this review, we examine HA glycosylation patterns of IAV associated with pandemic and seasonal influenza and discuss recent advancements in our understanding of interactions between IAV glycans and components of innate and adaptive immunity.
Url:
DOI: 10.3390/v6031294
PubMed: 24638204
PubMed Central: 3970151
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<front><div type="abstract" xml:lang="en"><p>Seasonal influenza A viruses (IAV) originate from pandemic IAV and have undergone changes in antigenic structure, including addition of glycans to the hemagglutinin (HA) glycoprotein. The viral HA is the major target recognized by neutralizing antibodies and glycans have been proposed to shield antigenic sites on HA, thereby promoting virus survival in the face of widespread vaccination and/or infection. However, addition of glycans can also interfere with the receptor binding properties of HA and this must be compensated for by additional mutations, creating a fitness barrier to accumulation of glycosylation sites. In addition, glycans on HA are also recognized by phylogenetically ancient lectins of the innate immune system and the benefit provided by evasion of humoral immunity is balanced by attenuation of infection. Therefore, a fine balance must exist regarding the optimal pattern of HA glycosylation to offset competing pressures associated with recognition by innate defenses, evasion of humoral immunity and maintenance of virus fitness. In this review, we examine HA glycosylation patterns of IAV associated with pandemic and seasonal influenza and discuss recent advancements in our understanding of interactions between IAV glycans and components of innate and adaptive immunity.</p>
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<pmc article-type="review-article"><pmc-dir>properties open_access</pmc-dir>
<front><journal-meta><journal-id journal-id-type="nlm-ta">Viruses</journal-id>
<journal-id journal-id-type="iso-abbrev">Viruses</journal-id>
<journal-id journal-id-type="publisher-id">viruses</journal-id>
<journal-title-group><journal-title>Viruses</journal-title>
</journal-title-group>
<issn pub-type="epub">1999-4915</issn>
<publisher><publisher-name>MDPI</publisher-name>
</publisher>
</journal-meta>
<article-meta><article-id pub-id-type="pmid">24638204</article-id>
<article-id pub-id-type="pmc">3970151</article-id>
<article-id pub-id-type="doi">10.3390/v6031294</article-id>
<article-id pub-id-type="publisher-id">viruses-06-01294</article-id>
<article-categories><subj-group subj-group-type="heading"><subject>Review</subject>
</subj-group>
</article-categories>
<title-group><article-title>Playing Hide and Seek: How Glycosylation of the Influenza Virus Hemagglutinin Can Modulate the Immune Response to Infection </article-title>
</title-group>
<contrib-group><contrib contrib-type="author"><name><surname>Tate</surname>
<given-names>Michelle D.</given-names>
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<xref ref-type="aff" rid="af1-viruses-06-01294">1</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Job</surname>
<given-names>Emma R.</given-names>
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<xref ref-type="aff" rid="af2-viruses-06-01294">2</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Deng</surname>
<given-names>Yi-Mo</given-names>
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<xref ref-type="aff" rid="af3-viruses-06-01294">3</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Gunalan</surname>
<given-names>Vithiagaran</given-names>
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<xref ref-type="aff" rid="af4-viruses-06-01294">4</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Maurer-Stroh</surname>
<given-names>Sebastian</given-names>
</name>
<xref ref-type="aff" rid="af4-viruses-06-01294">4</xref>
<xref ref-type="aff" rid="af5-viruses-06-01294">5</xref>
<xref ref-type="aff" rid="af6-viruses-06-01294">6</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Reading</surname>
<given-names>Patrick C.</given-names>
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<xref ref-type="aff" rid="af2-viruses-06-01294">2</xref>
<xref ref-type="aff" rid="af3-viruses-06-01294">3</xref>
<xref rid="c1-viruses-06-01294" ref-type="corresp">*</xref>
</contrib>
</contrib-group>
<aff id="af1-viruses-06-01294"><label>1</label>
Centre for Innate Immunity and Infectious Diseases, Monash Institute of Medical Research, Monash University, Clayton, Victoria, 3168, Australia; E-Mail:<email>michelle.tate@monash.edu</email>
</aff>
<aff id="af2-viruses-06-01294"><label>2</label>
Department of Microbiology and Immunology, The University of Melbourne, at the Peter Doherty Institute for Infection and Immunity, Victoria 3010, Australia; E-Mail:<email>e.job@student.unimelb.edu.au</email>
</aff>
<aff id="af3-viruses-06-01294"><label>3</label>
WHO Collaborating Centre for Reference and Research on Influenza, Victorian Infectious Diseases Reference Laboratory, at the Peter Doherty Institute for Infection and Immunity, Victoria 3010, Australia; E-Mail:<email>yi-mo.deng@influenzacentre.org</email>
</aff>
<aff id="af4-viruses-06-01294"><label>4</label>
Bioinformatics Institute, Agency for Science, Technology and Research, 138671, Singapore; E-Mails:<email>vithiagarang@bii.a-star.edu.sg</email>
(V.G.);<email>sebastianms@bii.a-star.edu.sg</email>
(S.M.-S.)</aff>
<aff id="af5-viruses-06-01294"><label>5</label>
School of Biological Sciences, Nanyang Technological University, 639798, Singapore</aff>
<aff id="af6-viruses-06-01294"><label>6</label>
National Public Health Laboratory, Communicable Diseases Division, Ministry of Health, 169854, Singapore</aff>
<author-notes><corresp id="c1-viruses-06-01294"><label>*</label>
Author to whom correspondence should be addressed; E-Mail: <email>preading@unimelb.edu.au</email>
or <email>Patrick.Reading@influenzacentre.org</email>
; Tel.: +61-38344-3437; Fax: +61-39347-1540.</corresp>
</author-notes>
<pub-date pub-type="epub"><day>14</day>
<month>3</month>
<year>2014</year>
</pub-date>
<pub-date pub-type="collection"><month>3</month>
<year>2014</year>
</pub-date>
<volume>6</volume>
<issue>3</issue>
<fpage>1294</fpage>
<lpage>1316</lpage>
<history><date date-type="received"><day>23</day>
<month>12</month>
<year>2013</year>
</date>
<date date-type="rev-recd"><day>03</day>
<month>3</month>
<year>2014</year>
</date>
<date date-type="accepted"><day>07</day>
<month>3</month>
<year>2014</year>
</date>
</history>
<permissions><copyright-statement>© 2014 by the authors; licensee MDPI, Basel, Switzerland.</copyright-statement>
<copyright-year>2014</copyright-year>
<license><license-p><pmc-comment>CREATIVE COMMONS</pmc-comment>
This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution license (<ext-link ext-link-type="uri" xlink:href="http://creativecommons.org/licenses/by/3.0/">http://creativecommons.org/licenses/by/3.0/</ext-link>
).</license-p>
</license>
</permissions>
<abstract><p>Seasonal influenza A viruses (IAV) originate from pandemic IAV and have undergone changes in antigenic structure, including addition of glycans to the hemagglutinin (HA) glycoprotein. The viral HA is the major target recognized by neutralizing antibodies and glycans have been proposed to shield antigenic sites on HA, thereby promoting virus survival in the face of widespread vaccination and/or infection. However, addition of glycans can also interfere with the receptor binding properties of HA and this must be compensated for by additional mutations, creating a fitness barrier to accumulation of glycosylation sites. In addition, glycans on HA are also recognized by phylogenetically ancient lectins of the innate immune system and the benefit provided by evasion of humoral immunity is balanced by attenuation of infection. Therefore, a fine balance must exist regarding the optimal pattern of HA glycosylation to offset competing pressures associated with recognition by innate defenses, evasion of humoral immunity and maintenance of virus fitness. In this review, we examine HA glycosylation patterns of IAV associated with pandemic and seasonal influenza and discuss recent advancements in our understanding of interactions between IAV glycans and components of innate and adaptive immunity.</p>
</abstract>
<kwd-group><kwd>influenza virus</kwd>
<kwd>glycosylation</kwd>
<kwd>immune evasion</kwd>
<kwd>lectin</kwd>
</kwd-group>
</article-meta>
</front>
</pmc>
</record>
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