Restrictions to the adaptation of influenza a virus h5 hemagglutinin to the human host.
The binding specificities of a panel of avian influenza virus subtype H5 hemagglutinin (HA) proteins bearing mutations at key residues in the receptor binding site were investigated. The results demonstrate that two simultaneous mutations in the receptor binding site resulted in H5 HA binding in a pattern similar to that shown by human viruses. Coexpression of the ion channel protein, M2, from most avian and human strains tested protected H5 HA conformation during trafficking, indicating that no genetic barrier to the reassortment of the H5 surface antigen gene with internal genes of human viruses existed at this level.
Harvey
Ruth
R
School of Animal and Microbial Sciences, University of Reading, Reading RG6 6AJ, United Kingdom.
Martin
Andrew C R
AC
Zambon
Maria
M
Barclay
Wendy S
WS
D000222:Adaptation, Physiological / Q000235:genetics; D000818:Animals; D001665:Binding Sites / Q000235:genetics; D004912:Erythrocytes / Q000378:metabolism; D019267:Hemagglutinin Glycoproteins, Influenza Virus / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism; D006801:Humans; D009980:Influenza A virus / Q000145:classification / Q000235:genetics / Q000472:pathogenicity*; D008958:Models, Molecular; D017354:Point Mutation; D011956:Receptors, Cell Surface / Q000378:metabolism*; D013045:Species Specificity
D019267:Hemagglutinin Glycoproteins, Influenza Virus; D011956:Receptors, Cell Surface; C109963:hemagglutinin, avian influenza A virus; C092488:sialic acid receptor