The amino acid sequence of the haemagglutinin of A/equine/Miami/63 (H3N8), the prototype influenza virus of the H3 subtype from horses, is deduced from the nucleotide sequence of virus RNA and compared with the sequences of haemagglutinins of viruses of this subtype isolated from humans [X-31 (H3N2)] and from birds [A/duck/Ukraine/63 (H3N8)] and with the sequence of the haemagglutinin of A/equine/Fontainebleau/79 (H3N8) a virus isolated from a recent outbreak of equine influenza. The amino acid sequence differences detected are discussed with reference to the structure of the molecules, their antigenicity and antigenic drift in influenza viruses isolated from horses.
DanielsR. S.,
DouglasA. R.,
SkehelJ. J.,
WileyD. C.1983; Analyses of the antigenicity of influenza haemagglutinin at the pH optimum for virus-mediated membrane fusion. Journal of General Virology 64:1657–1662
FangR.,
Min JouW.,
HuylebroeckD.,
DevosR.,
FiersW.1981; Complete structure of A/duck/Ukraine/63 influenza haemagglutinin gene: animal virus as progenitor of human H3 Hong Kong 1968 influenza haemagglutinin. Cell 25:315–323
HinshawV. S.,
NaeveC. W.,
WebsterR. G.,
DouglasA.,
SkehelJ. J.,
BryansJ.1983; Analysis of antigenic variation in equine 2 influenza A viruses. Bulletin of the World Health Organization 61:153–158
LaverW. G.,
WebsterR. G.1973; Studies on the origin of pandemic influenza. III. Evidence implicating duck and equine influenza viruses as possible progenitors of the Hong Kong strain of human influenza. Virology 51:383–391
Min JouW.,
VerhoeyenM.,
DevosR.,
SamanE.,
FangR.,
HuylebroeckD.,
FiersW.1980; Complete structure of the haemagglutinin gene from the human influenza A/Victoria/3/75 (H3N2) strain as determined from cloned DNA. Cell 19:683–696
RogersG. N.,
PaulsonJ. C.1983; Receptor determinants of human and animal influenza virus isolates: differences in receptor specificity of the H3 haemagglutinin based on species of origin. Virology 127:361–373
RogersG. N.,
PaulsonJ. C.,
DanielsR. S.,
SkehelJ. J.,
WilsonI. A.,
WileyD. C.1983; Single amino acid substitutions in the influenza haemagglutinin change the specificity of receptor binding. Nature, London 304:76–78
SangerF.,
NicklenS.,
CoulsonA. R.1977; DNA sequencing with chain-terminating inhibitors. Proceedings of the National Academy of Sciences, U.S.A 74:5463–5467
SkehelJ. J.,
DanielsR. S.,
DouglasA. R.,
WileyD. C.1983; Antigenic and amino acid sequence variations in the haemagglutinins of type A influenza viruses recently isolated from human subjects. Bulletin of the World Health Organization 61:671–676
VerhoeyenM.,
FangR.,
Min JouW.,
DevosR.,
HuylebroeckD.,
SamanE.,
FiersW.1980; Antigenic drift between the haemagglutinin of the Hong Kong influenza strains A/Aichi/2/68 and A/Victoria/3/75. Nature, London 286:771–776
WaddellG. H.,
TeiglandM. B.,
SigelM. M.1963; A new influenza virus associated with equine respiratory disease. Journal of the American Veterinary Medical Association 143:587–590
WardC. W.,
DopheideT. A.1981; Evolution of the Hong Kong influenza A sub-type. Structural relationship between the haemagglutinin from A/duck/Ukraine/63 (Hav 7) and the Hong Kong (H3) haemagglutinins. Biochemical Journal 195:337–340
WaterfieldM. D.,
GethingM. J.,
ScraceG.,
SkehelJ. J.1980; The carbohydrate side chains and disulphide bonds of the haemagglutinin of the influenza virus A/Japan/305/57 (H2N1). In Structure and Variation in Influenza Viruses pp 11–20 Edited by
LaverW. G.,
AirG.
New York: Elsevier;
World Health Organization Memorandum1980; A revision of the system of nomenclature for influenza viruses. Bulletin of the World Health Organization 58:585–591