Additional glycosylation at the receptor binding site of the hemagglutinin (HA) for H5 and H7 viruses may be an adaptation to poultry hosts, but does it influence pathogenicity?
Sequence analysis of the hemagglutinin (HA) gene of H5 and H7 viruses was used to determine phylogenetic relationships between high-pathogenicity avian influenza (HPAI) and low-pathogenicity avian influenza (LPAI) viruses from avian influenza (AI) outbreaks in Norfolk in 1979 and 1991 and Italy in 1999-2000. A common feature within these groups of viruses was the acquisition of additional glycosylation sites near the receptor binding site of the HA. Passage of H5 viruses through 14-day-old embryonated fowls' eggs readily selected viruses with additional glycosylation of HA1. Although additional glycosylation may not correlate with increased pathogenicity for fowl, it may predispose viruses to become highly pathogenic.
Banks
J
J
Veterinary Laboratories Agency Weybridge, Woodham Lane, New Haw, Addlestone, Surrey, KT15 3NB, UK.
Plowright
L
L
D000818:Animals; D001665:Binding Sites; D002642:Chick Embryo; D002645:Chickens; D004196:Disease Outbreaks / Q000662:veterinary; D005843:Geography; D006031:Glycosylation; D019267:Hemagglutinin Glycoproteins, Influenza Virus / Q000378:metabolism*; D009980:Influenza A virus / Q000145:classification*; D005585:Influenza in Birds / Q000453:epidemiology / Q000821:virology*; D007558:Italy / Q000453:epidemiology; D010802:Phylogeny
D019267:Hemagglutinin Glycoproteins, Influenza Virus