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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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Please use this identifier to cite or link to this item:http://hdl.handle.net/2115/81008

Title: E190V substitution of H6 hemagglutinin is one of key factors for binding to sulfated sialylated glycan receptor and infection to chickens
Authors: Kikutani, Yuto1 Browse this author
Okamatsu, Masatoshi2 Browse this author →KAKEN DB
Nishihara, Shoko3 Browse this author
Takase, Sayaka4 Browse this author →KAKEN DB
Hiono, Takahiro5 Browse this author →KAKEN DB
de Vries, P. Robert6 Browse this author
McBride, Ryan7 Browse this author
Matsuno, Keita8 Browse this author →KAKEN DB
Kida, Hiroshi9 Browse this author →KAKEN DB
Sakoda, Yoshihiro10 Browse this author →KAKEN DB
Authors(alt): Yoden, Sayaka4
Keywords: avian influenza virus
hemagglutinin
interspecies transmission
sialic acid receptor
sulfated glycans
Issue Date: 16-Apr-2020
Publisher: John Wiley & Sons
Journal Title: Microbiology and immunology
Volume: 64
Issue: 4
Start Page: 304
End Page: 312
Publisher DOI: 10.1111/1348-0421.12773
PMID: 31943329
Abstract: Avian 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.
Rights: This 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.
Type: article (author version)
URI: http://hdl.handle.net/2115/81008
Appears in Collections:国際連携研究教育局 : GI-CoRE (Global Institution for Collaborative Research and Education : GI-CoRE) > 雑誌発表論文等 (Peer-reviewed Journal Articles, etc)

Submitter: 迫田 義博

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