Putative amino acid determinants of the emergence of the 2009 influenza A (H1N1) virus in the human population.
Identifieur interne : 000486 ( Hal/Curation ); précédent : 000485; suivant : 000487Putative amino acid determinants of the emergence of the 2009 influenza A (H1N1) virus in the human population.
Auteurs : Daphna Meroz [Israël] ; Sun-Woo Yoon [États-Unis] ; Mariette Ducatez [États-Unis] ; Thomas P. Fabrizio [États-Unis] ; Richard J. Webby [États-Unis] ; Tomer Hertz [États-Unis] ; Nir Ben-Tal [Israël]Source :
- Proceedings of the National Academy of Sciences of the United States of America [ 0027-8424 ] ; 2011.
Abstract
The emergence of the unique H1N1 influenza A virus in 2009 resulted in a pandemic that has spread to over 200 countries. The constellation of molecular factors leading to the emergence of this strain is still unclear. Using a computational approach, we identified molecular determinants that may discriminate the hemagglutinin protein of the 2009 human pandemic H1N1 (pH1N1) strain from that of other H1N1 strains. As expected, positions discriminating the pH1N1 from seasonal human strains were located in or near known H1N1 antigenic sites, thus camouflaging the pH1N1 strain from immune recognition. For example, the alteration S145K (an antigenic position) was found as a characteristic of the pH1N1 strain. We also detected positions in the hemagglutinin protein differentiating classical swine viruses from pH1N1. These positions were mostly located in and around the receptor-binding pocket, possibly influencing binding affinity to the human cell. Such alterations may be liable in part for the virus's efficient infection and adaptation to humans. For instance, 133(A) and 149 were identified as discriminative positions. Significantly, we showed that the substitutions R133(A)K and R149K, predicted to be pH1N1 characteristics, each altered virus binding to erythrocytes and conferred virulence to A/swine/NC/18161/02 in mice, reinforcing the computational findings. Our findings provide a structural explanation for the deficient immunity of humans to the pH1N1 strain. Moreover, our analysis points to unique molecular factors that may have facilitated the emergence of this swine variant in humans, in contrast to other swine variants that failed.
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DOI: 10.1073/pnas.1014854108
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<front><div type="abstract" xml:lang="en"> <p>The emergence of the unique H1N1 influenza A virus in 2009 resulted in a pandemic that has spread to over 200 countries. The constellation of molecular factors leading to the emergence of this strain is still unclear. Using a computational approach, we identified molecular determinants that may discriminate the hemagglutinin protein of the 2009 human pandemic H1N1 (pH1N1) strain from that of other H1N1 strains. As expected, positions discriminating the pH1N1 from seasonal human strains were located in or near known H1N1 antigenic sites, thus camouflaging the pH1N1 strain from immune recognition. For example, the alteration S145K (an antigenic position) was found as a characteristic of the pH1N1 strain. We also detected positions in the hemagglutinin protein differentiating classical swine viruses from pH1N1. These positions were mostly located in and around the receptor-binding pocket, possibly influencing binding affinity to the human cell. Such alterations may be liable in part for the virus's efficient infection and adaptation to humans. For instance, 133(A) and 149 were identified as discriminative positions. Significantly, we showed that the substitutions R133(A)K and R149K, predicted to be pH1N1 characteristics, each altered virus binding to erythrocytes and conferred virulence to A/swine/NC/18161/02 in mice, reinforcing the computational findings. Our findings provide a structural explanation for the deficient immunity of humans to the pH1N1 strain. Moreover, our analysis points to unique molecular factors that may have facilitated the emergence of this swine variant in humans, in contrast to other swine variants that failed.</p>
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<surname>Ben-Tal</surname>
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<idno type="halauthorid">1718737</idno>
<affiliation ref="#struct-63133"></affiliation>
</author>
</analytic>
<monogr> <idno type="halJournalId" status="VALID">7969</idno>
<idno type="issn">0027-8424</idno>
<idno type="eissn">1091-6490</idno>
<title level="j">Proceedings of the National Academy of Sciences of the United States of America </title>
<imprint> <publisher>National Academy of Sciences</publisher>
<biblScope unit="volume">108</biblScope>
<biblScope unit="issue">33</biblScope>
<biblScope unit="pp">13522-7</biblScope>
<date type="datePub">2011</date>
</imprint>
</monogr>
<idno type="doi">10.1073/pnas.1014854108</idno>
<idno type="prodinra">178196</idno>
<idno type="pubmed">21808039</idno>
<idno type="wos">000293895100038</idno>
<ref type="seeAlso" target="http://www.pnas.org">http://www.pnas.org</ref>
<ref type="publisher">http://www.pnas.org</ref>
</biblStruct>
</sourceDesc>
<profileDesc> <langUsage> <language ident="en">English</language>
</langUsage>
<textClass> <classCode scheme="halDomain" n="sdv.spee">Life Sciences [q-bio]/Santé publique et épidémiologie</classCode>
<classCode scheme="halDomain" n="sdv.mp">Life Sciences [q-bio]/Microbiology and Parasitology</classCode>
<classCode scheme="halDomain" n="sdv.ba">Life Sciences [q-bio]/Animal biology</classCode>
<classCode scheme="halTypology" n="ART">Journal articles</classCode>
</textClass>
<abstract xml:lang="en"> <p>The emergence of the unique H1N1 influenza A virus in 2009 resulted in a pandemic that has spread to over 200 countries. The constellation of molecular factors leading to the emergence of this strain is still unclear. Using a computational approach, we identified molecular determinants that may discriminate the hemagglutinin protein of the 2009 human pandemic H1N1 (pH1N1) strain from that of other H1N1 strains. As expected, positions discriminating the pH1N1 from seasonal human strains were located in or near known H1N1 antigenic sites, thus camouflaging the pH1N1 strain from immune recognition. For example, the alteration S145K (an antigenic position) was found as a characteristic of the pH1N1 strain. We also detected positions in the hemagglutinin protein differentiating classical swine viruses from pH1N1. These positions were mostly located in and around the receptor-binding pocket, possibly influencing binding affinity to the human cell. Such alterations may be liable in part for the virus's efficient infection and adaptation to humans. For instance, 133(A) and 149 were identified as discriminative positions. Significantly, we showed that the substitutions R133(A)K and R149K, predicted to be pH1N1 characteristics, each altered virus binding to erythrocytes and conferred virulence to A/swine/NC/18161/02 in mice, reinforcing the computational findings. Our findings provide a structural explanation for the deficient immunity of humans to the pH1N1 strain. Moreover, our analysis points to unique molecular factors that may have facilitated the emergence of this swine variant in humans, in contrast to other swine variants that failed.</p>
</abstract>
</profileDesc>
</hal>
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