2024-03-29T09:47:36Zhttps://eprints.lib.hokudai.ac.jp/dspace-oai/requestoai:eprints.lib.hokudai.ac.jp:2115/810082022-11-17T02:08:08Zhdl_2115_64361hdl_2115_64360E190V substitution of H6 hemagglutinin is one of key factors for binding to sulfated sialylated glycan receptor and infection to chickensKikutani, YutoOkamatsu, MasatoshiNishihara, ShokoTakase, SayakaHiono, Takahirode Vries, P. RobertMcBride, RyanMatsuno, KeitaKida, HiroshiSakoda, Yoshihiroavian influenza virushemagglutinininterspecies transmissionsialic acid receptorsulfated glycans649Avian influenza viruses (AIVs) recognize sialic acid linked alpha 2,3 to galactose (SA alpha 2,3Gal) glycans as receptors. In this study, the interactions between hemagglutinins (HAs) of AIVs and sulfated SA alpha 2,3Gal 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 SA alpha 2,3Gal 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 SA alpha 2,3Gal glycans. These results suggest that the binding of the HA from H6 AIVs to sulfated SA alpha 2,3Gal glycans explains a part of mechanisms of interspecies transmission of AIVs from ducks to chickens.John Wiley & SonsJournal Articleapplication/pdfapplication/vnd.openxmlformats-officedocument.spreadsheetml.sheetapplication/vnd.openxmlformats-officedocument.spreadsheetml.sheetapplication/vnd.ms-excelhttp://hdl.handle.net/2115/81008https://eprints.lib.hokudai.ac.jp/dspace/bitstream/2115/81008/1/Manuscript_Final_Kikutani.pdfhttps://eprints.lib.hokudai.ac.jp/dspace/bitstream/2115/81008/2/Supplemental%20Table%201.xlsxhttps://eprints.lib.hokudai.ac.jp/dspace/bitstream/2115/81008/4/Supplemental%20Table%203.xlsxhttps://eprints.lib.hokudai.ac.jp/dspace/bitstream/2115/81008/3/Supplymental%20Table%202.xls0385-56001348-0421AA00738350Microbiology and immunology6443043122020-04-16enginfo:pmid/31943329info:doi/10.1111/1348-0421.12773This is the peer reviewed version of the following article: Kikutani Y, OkamatsuM, Nishihara S, et al. E190V substitution of H6hemagglutinin is one of key factors for binding tosulfated sialylated glycan receptor and infection tochickens.Microbiology and Immunology. 2020;1–9, which has been published in final form at https://doi.org/10.1111/1348-0421.12773. This article may be used for non-commercial purposes in accordance with Wiley Terms and Conditions for Use of Self-Archived Versions.author