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

FEBS Letters

Fukunaga, Kyoko⁷  Ohuchi, Masanobu²  Miyamoto, Daisei⁶  Toyoda, Tetsuya⁴  Suzuki, Takashi⁶  Suzuki, Yasuo⁶  Ito, Toshihiro³  Jwa Hidari, Kazuya I.-P.⁶  Ishihama, Akira¹  Kiso, Makoto⁷  Kawaoka, Yoshihiro⁸  Horiike, Goh⁶  Murakami, Kohji⁶  Sugiyama, Yoshikuni⁶  Kida, Hiroshi⁵  Masuda, Hiroyuki⁶ 

[1] Department of Molecular Genetics, National Institute of Genetics, Mishima 411-8540, Japan;Department of Microbiology, Kawasaki Medical School, Kurashiki 701-0192, Japan;Department of Veterinary Public Health, Faculty of Agriculture, Tottori University, Tottori 680-8553, Japan;Department of Virology, Kurume University, School of Medicine, Kurume 830-0011, Japan;Department of Disease Control, Graduate School of Veterinary Medicine, Hokkaido University, Sapporo 060-0818, Japan;Department of Biochemistry, University of Shizuoka, School of Pharmaceutical Sciences, Shizuoka 422-8526, Japan;Department of Applied Bioorganic Chemistry, Gifu University, Gifu 501-1193, Japan;Department of Pathobiological Science, School of Veterinary Medicine, University of Wisconsin-Madison, Madison, WI 53706, USA

关键词: Influenza virus;    Hemagglutinin;    Sialic acid;    Sialyl-oligosaccharide;    N-Glycolylneuraminic acid;    HA;    hemagglutinin;    HAU;    hemagglutination unit;    Neu5Ac;    5-N-acetylneuraminic acid;    Neu5Gc;    5-N-glycolylneuraminic acid;    TLC;    thin-layer chromatography;    RBS;    receptor binding site;   

DOI  :  10.1016/S0014-5793(99)01575-6

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 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.

【 授权许可】

Unknown