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

被引：41

作者：

Masuda, H

Suzuki, T

Sugiyama, Y

Horiike, G

Murakami, K

Miyamoto, D

Hidari, KIPJ

Ito, T

Kida, H

Kiso, M

Fukunaga, K

Ohuchi, M

Toyoda, T

Ishihama, A

Kawaoka, Y

Suzuki, Y ^{[1
]}

机构：

[1] Univ Shizuoka, Sch Pharmaceut Sci, Dept Biochem, Shizuoka 4228526, Japan

[2] Tottori Univ, Fac Agr, Dept Vet Publ Hlth, Tottori 6808553, Japan

[3] Hokkaido Univ, Grad Sch Vet Med, Dept Dis Control, Sapporo, Hokkaido 0600818, Japan

[4] Gifu Univ, Dept Appl Bioorgan Chem, Gifu 5011193, Japan

[5] Kawasaki Med Sch, Dept Microbiol, Kurashiki, Okayama 7010192, Japan

[6] Kurume Univ, Sch Med, Dept Virol, Kurume, Fukuoka 8300011, Japan

[7] Natl Inst Genet, Dept Mol Genet, Mishima, Shizuoka 4118540, Japan

[8] Univ Wisconsin, Sch Vet Med, Dept Pathobiol Sci, Madison, WI 53706 USA

来源：

FEBS LETTERS | 1999年 / 464卷 / 1-2期

关键词：

influenza virus; hemagglutinin; sialic acid; sialyl-oligosaccharide; N-glycolylneuraminic acid;

D O I：

10.1016/S0014-5793(99)01575-6

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Sialic acids are essential components of cell surface receptors used by influenza 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 nine human H3 influenza A viruses to sialylglycolipids containing type II sugar chain and different molecular species of terminal sialic acids, All human H3 viruses tested except A/Memphis/1/71 bound both Neu5Ac and Neu5Gc, Nucleotide 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.

引用

页码：71 / 74

页数：4

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