Substitution of amino acid residue in influenza A virus hemagglutinin affects recognition of sialyl-oligosaccharides containing N-glycolylneuraminic acid

Citation
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
Citations number
31
Categorie Soggetti
Biochemistry & Biophysics
Journal title
FEBS LETTERS
ISSN journal
00145793 → ACNP
Volume
464
Issue
1-2
Year of publication
1999
Pages
71 - 74
Database
ISI
SICI code
0014-5793(199912)464:1-2<71:SOAARI>2.0.ZU;2-E
Abstract
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.