Substitution of amino acid residue in influenza A virus hemagglutinin affects recognition of sialyl-oligosaccharides containing N-glycolylneuraminic acid
H. Masuda et al., Substitution of amino acid residue in influenza A virus hemagglutinin affects recognition of sialyl-oligosaccharides containing N-glycolylneuraminic acid, FEBS LETTER, 464(1-2), 1999, pp. 71-74
Sialic acids are essential components of cell surface receptors used by inf
luenza viruses. To determine the molecular mechanisms of viral recognition
of two major species of sialic acids, N-acetylneuraminic acid (Neu5Ac) and
N-glycolylneuraminic acid (Neu5Gc), we tested the binding reactivity of nin
e human H3 influenza A viruses to sialylglycolipids containing type II suga
r chain and different molecular species of terminal sialic acids, All human
H3 viruses tested except A/Memphis/1/71 bound both Neu5Ac and Neu5Gc, Nucl
eotide sequence analysis suggests that amino acids at 143, 155, and 158 are
linked to the viral recognition of Neu5Gc. (C) 1999 Federation of European
Biochemical Societies.