E190V substitution of H6 hemagglutinin is one of key factors for binding to sulfated sialylated glycan receptor and infection to chickens

Yuto Kikutani; Masatoshi Okamatsu; Shoko Nishihara; Sayaka Takase-Yoden; Takahiro Hiono; Robert P. de Vries; Ryan McBride; Keita Matsuno; Hiroshi Kida; Yoshihiro Sakoda

doi:10.1111/1348-0421.12773

E190V substitution of H6 hemagglutinin is one of key factors for binding to sulfated sialylated glycan receptor and infection to chickens

Yuto Kikutani, Masatoshi Okamatsu, Shoko Nishihara, Sayaka Takase-Yoden, Takahiro Hiono, Robert P. de Vries, Ryan McBride, Keita Matsuno, Hiroshi Kida, Yoshihiro Sakoda^*

^*Corresponding author for this work

Research output: Contribution to journal › Article › Academic › peer-review

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.

Original language	English
Pages (from-to)	304-312
Number of pages	9
Journal	Microbiology and Immunology
Volume	64
Issue number	4
DOIs	https://doi.org/10.1111/1348-0421.12773
Publication status	Published - 1 Apr 2020

Funding

We thank Kazue Oka and Mayumi Endo, Laboratory of Microbiology, Department of Disease Control, Faculty of Veterinary Medicine, Hokkaido University, for their technical support for this study. We thank Tokyo Chemical Industry Co., Ltd. for the preparation of glycans. We thank Dr James Paulson at The Scripps Research Institute for discussions and help with analyses of virus samples on the custom glycan microarray. This research was mainly supported by the Japanese Initiative for Progress of Research on Infectious Disease for Global Epidemics (J‐PRIDE) (Grant No. JP17fm0208026) from the Japan Agency for Medical Research and Development (AMED). The Japan Initiative for Global Research Network on Infectious Diseases (J‐GRID) (Grant No. JP17fm0108008) from AMED also partially supported this research. Glycan array studies were supported in part by NIH grant AI114730. Robert P. de Vries is a recipient of Rubicon and VENI grants from the Netherlands Organization for Scientific Research (NWO).

Keywords

avian influenza virus
hemagglutinin
interspecies transmission
sialic acid receptor
sulfated glycans

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1348-0421.12773Final published version, 607 KBLicence: Taverne

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title = "E190V substitution of H6 hemagglutinin is one of key factors for binding to sulfated sialylated glycan receptor and infection to chickens",

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.",

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AU - Takase-Yoden, Sayaka

AU - Hiono, Takahiro

AU - de Vries, Robert P.

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AU - Kida, Hiroshi

AU - Sakoda, Yoshihiro

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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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