Human influenza virus recognition of sialyloligosaccharides

FEBS Letters

Matrosovich, M.N.³  Tuzikov, A.B.⁴  Bovin, N.V.⁴  Nifant'ev, N.E.²  Sakharov, A.M.²  Gambaryan, A.S.³  Piskarev, V.E.¹  Yamskov, I.A.¹ 

[1] Institute of Food Substanses, Russian Academy of Sciences, Vavilov st. 28, 117813 Moscow, Russian Federation;Zelinsky Institute of Organic Chemistry, Russian Academy of Sciences, Leninsky pr., 47, 117 913 Moscow, Russian Federation;M.P. Chumakov Institute of Poliomyelitis and Viral Encephalitides, Russian Academy of Medical Sciences, 142 782, Moscow Region, Russian Federation;Shemyakin Institute of Bio-Organic Chemistry, Russian Academy of Sciences, Miklukho-Maklaya, 16/10, 117 871 Moscow, Russian Federation

关键词: Influenza virus;    Sialic acid;    Sialyloligosaccharides;    Sialyl-Lewis;    Sialyl-Lewis;    Protein-carbohydrate recognition;    HA;    hemagglutinin;    Neu5Ac;    5-N-acetylneuraminic acid;    RBS;    virus receptor binding site;    TLC;    thin-layer chromatography;   

DOI  :  10.1016/0014-5793(95)00488-U

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 utilized by influenza viruses. To evaluate the recognition of asialic sugar parts of the receptor, three representative strains of human influenza A and B viruses were tested for their binding of a panel of sialyloligosaccharides. The highest affinity binding carbohydrate determinants recognized by the viruses in a context of different core structures were Neu5Acα2-3Gal for the type B virus, Neu5Acα2-6Gal for the H3 subtype virus, and Neu5Acα2-6Ga/β1-4GlcNAc for the H1 subtype virus. Penultimate to these determinants parts of sialyloligosaccharides studied either contributed less significantly to the binding affinity, or interfered with the binding.

【 授权许可】

Unknown