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E190V substitution of H6 hemagglutinin is one of key factors for binding to sulfated sialylated glycan receptor and infection to chickens |
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| Authors: | Yuto Kikutani Masatoshi Okamatsu Shoko Nishihara Sayaka Takase-Yoden Takahiro Hiono Robert P de Vries Ryan McBride Keita Matsuno Hiroshi Kida Yoshihiro Sakoda |
| Institution: | 1. Department of Disease Control, Laboratory of Microbiology, Faculty of Veterinary Medicine, Hokkaido University, Sapporo, Hokkaido, Japan;2. Department of Bioinformatics, Graduate School of Engineering, Tokyo, Japan;3. Department of Disease Control, Laboratory of Microbiology, Faculty of Veterinary Medicine, Hokkaido University, Sapporo, Hokkaido, Japan
Glycoscience & Glycotechnology Research Group, Biotechnology Research Institute for Drug Discovery, National Institute of Advanced Industrial Science & Technology, Tsukuba, Ibaraki, Japan;4. Department of Chemical Biology & Drug Discovery, Utrecht Institute for Pharmaceutical Sciences, Utrecht University, Utrecht, The Netherlands;5. Departments of Molecular Medicine and Immunology and Microbial Science, The Scripps Research Institute, La Jolla, California, USA;6. Department of Disease Control, Laboratory of Microbiology, Faculty of Veterinary Medicine, Hokkaido University, Sapporo, Hokkaido, Japan Global Station for Zoonosis Control, Global Institute for Collaborative Research and Education (GI-CoRE), Hokkaido University, Sapporo, Hokkaido, Japan;7. Global Station for Zoonosis Control, Global Institute for Collaborative Research and Education (GI-CoRE), Hokkaido University, Sapporo, Hokkaido, Japan Research Center for Zoonosis Control, Hokkaido University, Sapporo, Hokkaido, Japan |
| Abstract: | Avian influenza viruses (AIVs) recognize sialic acid linked α2,3 to galactose (SAα2,3Gal) glycans as receptors. In this study, the interactions between hemagglutinins (HAs) of AIVs and sulfated SAα2,3Gal glycans were analyzed to clarify the molecular basis of interspecies transmission of AIVs from ducks to chickens. It was revealed that E190V and N192D substitutions of the HA increased the recovery of viruses derived from an H6 duck virus isolate, A/duck/Hong Kong/960/1980 (H6N2), in chickens. Recombinant HAs from an H6 chicken virus, A/chicken/Tainan/V156/1999 (H6N1), bound to sulfated SAα2,3Gal glycans, whereas the HAs from an H6 duck virus did not. Binding preference of mutant HAs revealed that an E190V substitution is critical for the recognition of sulfated SAα2,3Gal glycans. These results suggest that the binding of the HA from H6 AIVs to sulfated SAα2,3Gal glycans explains a part of mechanisms of interspecies transmission of AIVs from ducks to chickens. |
| Keywords: | avian influenza virus hemagglutinin interspecies transmission sialic acid receptor sulfated glycans |