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Identification of amino acid residues of influenza A virus H3 HA contributing to the recognition of molecular species of sialic acid |
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| Authors: | Tadanobu Takahashi Asako Hashimoto Mami Maruyama Makoto Kiso Yoshihiro Kawaoka Yasuo Suzuki Takashi Suzuki |
| Affiliation: | a Department of Biochemistry, University of Shizuoka, School of Pharmaceutical Sciences, Shizuoka 422-8526, Japan b CREST, Japan Science and Technology Agency, Saitama 332-0012, Japan c Global COE Program for Innovation in Human Health Sciences, Shizuoka 422-8526, Japan d Department of Applied Bioorganic Chemistry, Faculty of Applied Biological Sciences, Gifu University, Gifu 501-1193, Japan e International Research Centre for Infectious Diseases, Institute of Medical Science, University of Tokyo, Tokyo 108-8639, Japan f Department of Pathobiological Sciences, University of Wisconsin, Madison, WI, USA g Health Science Hills, and Department of Biomedical Sciences, College of Life and Health Sciences, Chubu University, Aichi 487-8501, Japan |
| Abstract: | To identify a determinant of human H3 hemagglutinin (HA) amino acid residues linked to the recognition of molecular species of sialic acid, we generated six mutant viruses possessing either the wild-type HA gene from A/Memphis/1/71 (H3N2) or a genetically single-mutated HA gene at position 137, 144, 155, 158 or 193 from a genetic backbone of A/WSN/33 (H1N1) by reverse genetics. We evaluated the binding ability with four types of synthetic sialylglycolipids. The results indicate that the amino acid substitutions Thr155 to Tyr and Glu158 to Gly in H3 HA facilitate virus binding to N-glycolylneuraminic acid. |
| Keywords: | HA, hemagglutinin HAU, hemagglutination unit IAV, influenza A virus Neu5Ac, 5-N-acetylneuraminic acid Neu5Gc, 5-N-glycolylneuraminic acid TLC, thin-layer chromatography |
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