Recent avian H5N1 viruses exhibit increased propensity for acquiring human receptor specificity.
Identifieur interne : 000249 ( PubMed/Corpus ); précédent : 000248; suivant : 000250Recent avian H5N1 viruses exhibit increased propensity for acquiring human receptor specificity.
Auteurs : James Stevens ; Ola Blixt ; Li-Mei Chen ; Ruben O. Donis ; James C. Paulson ; Ian A. WilsonSource :
- Journal of molecular biology [ 1089-8638 ] ; 2008.
English descriptors
- KwdEn :
- Animals, Birds (virology), Hemagglutinin Glycoproteins, Influenza Virus (chemistry), Hemagglutinin Glycoproteins, Influenza Virus (genetics), Humans, Influenza A Virus, H5N1 Subtype (metabolism), Insecta, Ligands, Models, Molecular, Mutation (genetics), Phylogeny, Polysaccharides (chemistry), Polysaccharides (metabolism), Protein Structure, Secondary, Receptors, Virus (metabolism), Virus Diseases (virology).
- MESH :
- chemical , chemistry : Hemagglutinin Glycoproteins, Influenza Virus, Polysaccharides.
- chemical , genetics : Hemagglutinin Glycoproteins, Influenza Virus.
- genetics : Mutation.
- metabolism : Influenza A Virus, H5N1 Subtype, Polysaccharides, Receptors, Virus.
- virology : Birds, Virus Diseases.
- Animals, Humans, Insecta, Ligands, Models, Molecular, Phylogeny, Protein Structure, Secondary.
Abstract
Adaptation of avian influenza viruses for replication and transmission in the human host is believed to require mutations in the hemagglutinin glycoprotein (HA) which enable binding to human alpha2-6 sialosides and concomitant reduction in affinity for avian alpha2-3 linked sialosides. Here, we show by glycan microarray analyses that the two mutations responsible for such specificity changes in 1957 H2N2 and 1968 H3N2 pandemic viruses, when inserted into recombinant HAs or intact viruses of some recent avian H5N1 isolates (clade 2.2), impart such attributes. This propensity to adapt to human receptors is primarily dependent on arginine at position 193 within the receptor-binding site, as well as loss of a vicinal glycosylation site. Widespread occurrence of these susceptible H5N1 clade 2.2 influenza strains has already occurred in Europe, the Middle East, and Africa. Thus, these avian strains should be considered high-risk, because of their significantly lower threshold for acquiring human receptor specificity and, therefore, warrant increased surveillance and further study.
DOI: 10.1016/j.jmb.2008.04.016
PubMed: 18672252
Links to Exploration step
pubmed:18672252Le document en format XML
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Donis</name></author><author><name sortKey="Paulson, James C" sort="Paulson, James C" uniqKey="Paulson J" first="James C" last="Paulson">James C. Paulson</name></author><author><name sortKey="Wilson, Ian A" sort="Wilson, Ian A" uniqKey="Wilson I" first="Ian A" last="Wilson">Ian A. Wilson</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2008">2008</date><idno type="RBID">pubmed:18672252</idno><idno type="pmid">18672252</idno><idno type="doi">10.1016/j.jmb.2008.04.016</idno><idno type="wicri:Area/PubMed/Corpus">000249</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">000249</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Recent avian H5N1 viruses exhibit increased propensity for acquiring human receptor specificity.</title><author><name sortKey="Stevens, James" sort="Stevens, James" uniqKey="Stevens J" first="James" last="Stevens">James Stevens</name><affiliation><nlm:affiliation>Department of Molecular Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA. james.stevens@cdc.hhs.gov</nlm:affiliation></affiliation></author><author><name sortKey="Blixt, Ola" sort="Blixt, Ola" uniqKey="Blixt O" first="Ola" last="Blixt">Ola Blixt</name></author><author><name sortKey="Chen, Li Mei" sort="Chen, Li Mei" uniqKey="Chen L" first="Li-Mei" last="Chen">Li-Mei Chen</name></author><author><name sortKey="Donis, Ruben O" sort="Donis, Ruben O" uniqKey="Donis R" first="Ruben O" last="Donis">Ruben O. Donis</name></author><author><name sortKey="Paulson, James C" sort="Paulson, James C" uniqKey="Paulson J" first="James C" last="Paulson">James C. Paulson</name></author><author><name sortKey="Wilson, Ian A" sort="Wilson, Ian A" uniqKey="Wilson I" first="Ian A" last="Wilson">Ian A. Wilson</name></author></analytic><series><title level="j">Journal of molecular biology</title><idno type="eISSN">1089-8638</idno><imprint><date when="2008" type="published">2008</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Animals</term><term>Birds (virology)</term><term>Hemagglutinin Glycoproteins, Influenza Virus (chemistry)</term><term>Hemagglutinin Glycoproteins, Influenza Virus (genetics)</term><term>Humans</term><term>Influenza A Virus, H5N1 Subtype (metabolism)</term><term>Insecta</term><term>Ligands</term><term>Models, Molecular</term><term>Mutation (genetics)</term><term>Phylogeny</term><term>Polysaccharides (chemistry)</term><term>Polysaccharides (metabolism)</term><term>Protein Structure, Secondary</term><term>Receptors, Virus (metabolism)</term><term>Virus Diseases (virology)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Hemagglutinin Glycoproteins, Influenza Virus</term><term>Polysaccharides</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Hemagglutinin Glycoproteins, Influenza Virus</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Mutation</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Influenza A Virus, H5N1 Subtype</term><term>Polysaccharides</term><term>Receptors, Virus</term></keywords><keywords scheme="MESH" qualifier="virology" xml:lang="en"><term>Birds</term><term>Virus Diseases</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Humans</term><term>Insecta</term><term>Ligands</term><term>Models, Molecular</term><term>Phylogeny</term><term>Protein Structure, Secondary</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Adaptation of avian influenza viruses for replication and transmission in the human host is believed to require mutations in the hemagglutinin glycoprotein (HA) which enable binding to human alpha2-6 sialosides and concomitant reduction in affinity for avian alpha2-3 linked sialosides. Here, we show by glycan microarray analyses that the two mutations responsible for such specificity changes in 1957 H2N2 and 1968 H3N2 pandemic viruses, when inserted into recombinant HAs or intact viruses of some recent avian H5N1 isolates (clade 2.2), impart such attributes. This propensity to adapt to human receptors is primarily dependent on arginine at position 193 within the receptor-binding site, as well as loss of a vicinal glycosylation site. Widespread occurrence of these susceptible H5N1 clade 2.2 influenza strains has already occurred in Europe, the Middle East, and Africa. Thus, these avian strains should be considered high-risk, because of their significantly lower threshold for acquiring human receptor specificity and, therefore, warrant increased surveillance and further study.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">18672252</PMID><DateCompleted><Year>2008</Year><Month>09</Month><Day>15</Day></DateCompleted><DateRevised><Year>2018</Year><Month>11</Month><Day>13</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1089-8638</ISSN><JournalIssue CitedMedium="Internet"><Volume>381</Volume><Issue>5</Issue><PubDate><Year>2008</Year><Month>Sep</Month><Day>19</Day></PubDate></JournalIssue><Title>Journal of molecular biology</Title><ISOAbbreviation>J. Mol. Biol.</ISOAbbreviation></Journal><ArticleTitle>Recent avian H5N1 viruses exhibit increased propensity for acquiring human receptor specificity.</ArticleTitle><Pagination><MedlinePgn>1382-94</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1016/j.jmb.2008.04.016</ELocationID><Abstract><AbstractText>Adaptation of avian influenza viruses for replication and transmission in the human host is believed to require mutations in the hemagglutinin glycoprotein (HA) which enable binding to human alpha2-6 sialosides and concomitant reduction in affinity for avian alpha2-3 linked sialosides. Here, we show by glycan microarray analyses that the two mutations responsible for such specificity changes in 1957 H2N2 and 1968 H3N2 pandemic viruses, when inserted into recombinant HAs or intact viruses of some recent avian H5N1 isolates (clade 2.2), impart such attributes. This propensity to adapt to human receptors is primarily dependent on arginine at position 193 within the receptor-binding site, as well as loss of a vicinal glycosylation site. Widespread occurrence of these susceptible H5N1 clade 2.2 influenza strains has already occurred in Europe, the Middle East, and Africa. Thus, these avian strains should be considered high-risk, because of their significantly lower threshold for acquiring human receptor specificity and, therefore, warrant increased surveillance and further study.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Stevens</LastName><ForeName>James</ForeName><Initials>J</Initials><AffiliationInfo><Affiliation>Department of Molecular Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA. james.stevens@cdc.hhs.gov</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Blixt</LastName><ForeName>Ola</ForeName><Initials>O</Initials></Author><Author ValidYN="Y"><LastName>Chen</LastName><ForeName>Li-Mei</ForeName><Initials>LM</Initials></Author><Author ValidYN="Y"><LastName>Donis</LastName><ForeName>Ruben O</ForeName><Initials>RO</Initials></Author><Author ValidYN="Y"><LastName>Paulson</LastName><ForeName>James 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