tetano
Editor, Senior Moderator
J Virol. 2011 Dec 21. [Epub ahead of print]
The receptor binding specificity of the live attenuated influenza H2 and H6 vaccine viruses contributes to vaccine immunogenicity and protection in ferrets.
Chen Z, Zhou H, Kim L, Jin H.
Source
MedImmune LLC, 319 North Bernardo Avenue, Mountain View, CA 94043, USA.
Abstract
To prepare for influenza pandemics that may be caused by the H2 and H6 subtype influenza viruses, live attenuated influenza H2 and H6 vaccines (LAIV) are being developed and evaluated. The H2 and H6 vaccine candidates with different receptor binding preference specified by amino acid substitutions at residues 226 and 228 were generated and evaluated for their growth in embryonated chicken eggs, their immunogenicity and protection against wild-type virus challenge in the ferret model. The viruses containing Q226 and G228 in the HA protein bound to the avian-like α2,3-sialic acid (SA) receptor and replicated efficiently in chicken eggs. The viruses with L226 and G228 bound preferentially to the human-like α2,6-SA receptor. The viruses containing L226 and S228 displayed dual binding to both α2,3-SA and α2,6-SA receptors and replicated efficiently in eggs. The strains containing the L226/G228 or L226/S228 that preferentially bound to α2,6-SA receptors replicated more efficiently in the upper respiratory tract of ferrets, induced higher levels of neutralizing antibody, and conferred greater protection against wild-type virus challenge infection compared to the strain with the Q226/G228 residues. Our data suggest that pandemic vaccines with receptor binding preference to both avian- and human-like receptors might be desired for efficient viral replication in eggs and for inducing protective immune responses in humans.
PMID:
22190726
[PubMed - as supplied by publisher]
http://www.ncbi.nlm.nih.gov/pubmed/22190726
The receptor binding specificity of the live attenuated influenza H2 and H6 vaccine viruses contributes to vaccine immunogenicity and protection in ferrets.
Chen Z, Zhou H, Kim L, Jin H.
Source
MedImmune LLC, 319 North Bernardo Avenue, Mountain View, CA 94043, USA.
Abstract
To prepare for influenza pandemics that may be caused by the H2 and H6 subtype influenza viruses, live attenuated influenza H2 and H6 vaccines (LAIV) are being developed and evaluated. The H2 and H6 vaccine candidates with different receptor binding preference specified by amino acid substitutions at residues 226 and 228 were generated and evaluated for their growth in embryonated chicken eggs, their immunogenicity and protection against wild-type virus challenge in the ferret model. The viruses containing Q226 and G228 in the HA protein bound to the avian-like α2,3-sialic acid (SA) receptor and replicated efficiently in chicken eggs. The viruses with L226 and G228 bound preferentially to the human-like α2,6-SA receptor. The viruses containing L226 and S228 displayed dual binding to both α2,3-SA and α2,6-SA receptors and replicated efficiently in eggs. The strains containing the L226/G228 or L226/S228 that preferentially bound to α2,6-SA receptors replicated more efficiently in the upper respiratory tract of ferrets, induced higher levels of neutralizing antibody, and conferred greater protection against wild-type virus challenge infection compared to the strain with the Q226/G228 residues. Our data suggest that pandemic vaccines with receptor binding preference to both avian- and human-like receptors might be desired for efficient viral replication in eggs and for inducing protective immune responses in humans.
PMID:
22190726
[PubMed - as supplied by publisher]
http://www.ncbi.nlm.nih.gov/pubmed/22190726