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J Virol. Influenza H1N1 A/Solomon Island/3/06 virus receptor binding specificity correlates with virus pathogenicity, antigenicity and immunogenicity in ferrets.
Influenza H1N1 A/Solomon Island/3/06 virus receptor binding specificity correlates with virus pathogenicity, antigenicity and immunogenicity in ferrets. (J Virol., abstract, edited)
15. J Virol. 2010 Mar 3. [Epub ahead of print]
Influenza H1N1 A/Solomon Island/3/06 virus receptor binding specificity correlates with virus pathogenicity, antigenicity and immunogenicity in ferrets.
Xu Q, Wang W, Cheng X, Zengel J, Jin H. - MedImmune, 319 North Bernardo Ave, Mountain View, CA 94043.
Influenza viruses attach to cells via a sialic acid moiety (sialic acid receptor) that is alpha2-3 linked, or alpha2-6 linked, to galactose (alpha2-3SAL or alpha2-6SAL); sialic acid acts as a receptor for the virus. By lectin staining, we demonstrated that the alpha2-6SAL configuration is predominant in the respiratory tract of ferret including trachea, bronchi, and lung alveoli 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, 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 alpha2-6SAL, and 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 receptor binding preference for alpha2-6SAL 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 impacted viral antigenicity and immunogenicity. Our data emphasizes 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.
PMID: 20200248 [PubMed - as supplied by publisher]
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15. J Virol. 2010 Mar 3. [Epub ahead of print]
Influenza H1N1 A/Solomon Island/3/06 virus receptor binding specificity correlates with virus pathogenicity, antigenicity and immunogenicity in ferrets.
Xu Q, Wang W, Cheng X, Zengel J, Jin H. - MedImmune, 319 North Bernardo Ave, Mountain View, CA 94043.
Influenza viruses attach to cells via a sialic acid moiety (sialic acid receptor) that is alpha2-3 linked, or alpha2-6 linked, to galactose (alpha2-3SAL or alpha2-6SAL); sialic acid acts as a receptor for the virus. By lectin staining, we demonstrated that the alpha2-6SAL configuration is predominant in the respiratory tract of ferret including trachea, bronchi, and lung alveoli 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, 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 alpha2-6SAL, and 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 receptor binding preference for alpha2-6SAL 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 impacted viral antigenicity and immunogenicity. Our data emphasizes 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.
PMID: 20200248 [PubMed - as supplied by publisher]
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