Influenza H1N1 A/Solomon Island/3/06 Virus Receptor Binding Specificity Correlates with Virus Pathogenicity, Antigenicity, and Immunogenicity in Ferrets ▿
Identifieur interne : 000E64 ( Main/Exploration ); précédent : 000E63; suivant : 000E65Influenza H1N1 A/Solomon Island/3/06 Virus Receptor Binding Specificity Correlates with Virus Pathogenicity, Antigenicity, and Immunogenicity in Ferrets ▿
Auteurs : Qi Xu [États-Unis] ; Weijia Wang [États-Unis] ; Xing Cheng [États-Unis] ; James Zengel [États-Unis] ; Hong Jin [États-Unis]Source :
- Journal of Virology [ 0022-538X ] ; 2010.
Abstract
Influenza viruses attach to cells via a sialic acid moiety (sialic acid receptor) that is α2-3 linked or α2-6 linked to galactose (α2-3SAL or α2-6SAL); sialic acid acts as a receptor for the virus. Using lectin staining, we demonstrated that the α2-6SAL configuration is predominant in the respiratory tract of ferrets, including trachea, bronchus, and lung alveolus tissues. Recombinant wild-type (rWT) influenza A/Solomon Island/3/06 (SI06) (H1N1) viruses were constructed to assess the impact of the hemagglutinin (HA) variations (amino acids 190 or 226) identified in natural variants on virus replication in the upper and lower respiratory tract of ferrets, as well as virus antigenicity and immunogenicity. A single amino acid change at residue 226 (from Gln to Arg) in the HA of SI06 resulted in the complete loss of binding to α2-6SAL and a concomitant loss of the virus's ability to replicate in the lower respiratory tract of ferrets. In contrast, the virus with Gln226 in the HA protein has a receptor binding preference for α2-6SAL and replicates efficiently in the lungs. There was a good correlation between viral replication in the lungs of ferrets and disease symptoms. In addition, we also showed that the 190 and 226 residues affected viral antigenicity and immunogenicity. Our data emphasize the necessity of thoroughly assessing wild-type influenza viruses for their suitability as reference strains and for carefully selecting the HA antigen for vaccine production during annual influenza vaccine evaluation processes.
Url:
DOI: 10.1128/JVI.02489-09
PubMed: 20200248
PubMed Central: 2863823
Affiliations:
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rid="fn2">▿</xref> </title><author><name sortKey="Xu, Qi" sort="Xu, Qi" uniqKey="Xu Q" first="Qi" last="Xu">Qi Xu</name><affiliation wicri:level="2"><nlm:aff id="aff0">MedImmune, 319 North Bernardo Avenue, Mountain View, California 94043</nlm:aff><country xml:lang="fr">États-Unis</country><placeName><region type="state">Californie</region></placeName><wicri:cityArea>MedImmune, 319 North Bernardo Avenue, Mountain View</wicri:cityArea></affiliation></author><author><name sortKey="Wang, Weijia" sort="Wang, Weijia" uniqKey="Wang W" first="Weijia" last="Wang">Weijia Wang</name><affiliation wicri:level="2"><nlm:aff id="aff0">MedImmune, 319 North Bernardo Avenue, Mountain View, California 94043</nlm:aff><country xml:lang="fr">États-Unis</country><placeName><region type="state">Californie</region></placeName><wicri:cityArea>MedImmune, 319 North Bernardo Avenue, Mountain View</wicri:cityArea></affiliation></author><author><name sortKey="Cheng, Xing" sort="Cheng, Xing" uniqKey="Cheng X" first="Xing" last="Cheng">Xing Cheng</name><affiliation wicri:level="2"><nlm:aff id="aff0">MedImmune, 319 North Bernardo Avenue, Mountain View, California 94043</nlm:aff><country xml:lang="fr">États-Unis</country><placeName><region type="state">Californie</region></placeName><wicri:cityArea>MedImmune, 319 North Bernardo Avenue, Mountain View</wicri:cityArea></affiliation></author><author><name sortKey="Zengel, James" sort="Zengel, James" uniqKey="Zengel J" first="James" last="Zengel">James Zengel</name><affiliation wicri:level="2"><nlm:aff id="aff0">MedImmune, 319 North Bernardo Avenue, Mountain View, California 94043</nlm:aff><country xml:lang="fr">États-Unis</country><placeName><region type="state">Californie</region></placeName><wicri:cityArea>MedImmune, 319 North Bernardo Avenue, Mountain View</wicri:cityArea></affiliation></author><author><name sortKey="Jin, Hong" sort="Jin, Hong" uniqKey="Jin H" first="Hong" last="Jin">Hong Jin</name><affiliation wicri:level="2"><nlm:aff id="aff0">MedImmune, 319 North Bernardo Avenue, Mountain View, California 94043</nlm:aff><country xml:lang="fr">États-Unis</country><placeName><region type="state">Californie</region></placeName><wicri:cityArea>MedImmune, 319 North Bernardo Avenue, Mountain View</wicri:cityArea></affiliation></author></analytic><series><title level="j">Journal of Virology</title><idno type="ISSN">0022-538X</idno><idno type="eISSN">1098-5514</idno><imprint><date when="2010">2010</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><p>Influenza viruses attach to cells via a sialic acid moiety (sialic acid receptor) that is α2-3 linked or α2-6 linked to galactose (α2-3SAL or α2-6SAL); sialic acid acts as a receptor for the virus. Using lectin staining, we demonstrated that the α2-6SAL configuration is predominant in the respiratory tract of ferrets, including trachea, bronchus, and lung alveolus tissues. Recombinant wild-type (rWT) influenza A/Solomon Island/3/06 (SI06) (H1N1) viruses were constructed to assess the impact of the hemagglutinin (HA) variations (amino acids 190 or 226) identified in natural variants on virus replication in the upper and lower respiratory tract of ferrets, as well as virus antigenicity and immunogenicity. A single amino acid change at residue 226 (from Gln to Arg) in the HA of SI06 resulted in the complete loss of binding to α2-6SAL and a concomitant loss of the virus's ability to replicate in the lower respiratory tract of ferrets. In contrast, the virus with Gln226 in the HA protein has a receptor binding preference for α2-6SAL and replicates efficiently in the lungs. There was a good correlation between viral replication in the lungs of ferrets and disease symptoms. In addition, we also showed that the 190 and 226 residues affected viral antigenicity and immunogenicity. Our data emphasize the necessity of thoroughly assessing wild-type influenza viruses for their suitability as reference strains and for carefully selecting the HA antigen for vaccine production during annual influenza vaccine evaluation processes.</p></div></front></TEI><affiliations><list><country><li>États-Unis</li></country><region><li>Californie</li></region></list><tree><country name="États-Unis"><region name="Californie"><name sortKey="Xu, Qi" sort="Xu, Qi" uniqKey="Xu Q" first="Qi" last="Xu">Qi Xu</name></region><name sortKey="Cheng, Xing" sort="Cheng, Xing" uniqKey="Cheng X" first="Xing" last="Cheng">Xing Cheng</name><name sortKey="Jin, Hong" sort="Jin, Hong" uniqKey="Jin H" first="Hong" last="Jin">Hong Jin</name><name sortKey="Wang, Weijia" sort="Wang, Weijia" uniqKey="Wang W" first="Weijia" last="Wang">Weijia Wang</name><name sortKey="Zengel, James" sort="Zengel, James" uniqKey="Zengel J" first="James" last="Zengel">James Zengel</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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