Amino acid residues at positions 222 and 227 of the hemagglutinin together with the neuraminidase determine binding of H5 avian influenza viruses to sialyl Lewis X

Hiono, Takahiro; Okamatsu, Masatoshi; Igarashi, Manabu; McBride, Ryan; de Vries, Robert P.; Peng, Wenjie; Paulson, James C.; Sakoda, Yoshihiro; Kida, Hiroshi

Amino acid residues at positions 222 and 227 of the hemagglutinin together with the neuraminidase determine binding of H5 avian influenza viruses to sialyl Lewis X

Hiono, Takahiro; Okamatsu, Masatoshi; Igarashi, Manabu et al.

Archives of Virology, 2016, 161(2), 307-316

Permalink : https://hdl.handle.net/2115/64424

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アクセス権	open access
URI	https://hdl.handle.net/2115/64424
タイトル	Amino acid residues at positions 222 and 227 of the hemagglutinin together with the neuraminidase determine binding of H5 avian influenza viruses to sialyl Lewis X
著者	Hiono, Takahiro ; Okamatsu, Masatoshi ; Igarashi, Manabu ; McBride, Ryan ; de Vries, Robert P. ; Peng, Wenjie ; Paulson, James C. ; Sakoda, Yoshihiro ; Kida, Hiroshi
著者名 Hiono, Takahiro
e-Rad_Researcher 00507163 著者名 Okamatsu, Masatoshi
e-Rad_Researcher 10374240 著者名 Igarashi, Manabu
著者名 McBride, Ryan
著者名 de Vries, Robert P.
著者名 Peng, Wenjie
著者名 Paulson, James C.
e-Rad_Researcher 40333637 著者名 Sakoda, Yoshihiro
e-Rad_Researcher 10109506 著者名 Kida, Hiroshi
言語	英語
キーワード	influenza A virus
	hemagglutinin
	receptor specificity
	fucosylation
	sialyl Lewis X
発行日	2016-02
出版者	Springer
収録物名	Archives of Virology
巻(号)	161(2)
ページ	307-316
抄録	Influenza viruses isolated from ducks are rarely able to infect chickens; it is therefore postulated that these viruses need to adapt in some way to be able to be transmitted to chickens in nature. Previous studies revealed that sialyl Lewis X (3'SLeX), which is fucosylated alpha 2,3 sialoside, was predominantly detected on the epithelial cells of the chicken trachea, whereas this glycan structure is not found in the duck intestinal tract. To clarify the mechanisms of the interspecies transmission of influenza viruses between ducks and chickens, we compared the receptor specificity of low-pathogenic avian influenza viruses isolated from these two species. Glycan-binding analysis of the recombinant hemagglutinin (HA) of a chicken influenza virus, A/chicken/Ibaraki/1/2005 (H5N2), revealed a binding preference to alpha 1,3 fucosylated sialosides. On the other hand, the HA of a duck influenza virus, A/duck/Mongolia/54/2001 (H5N2) (Dk/MNG), particularly bound to non-fucosylated alpha 2,3 sialosides such as 3'-sialyllactosamine (3'SLacNAc). Computational analysis along with binding analysis of the mutant HAs revealed that this glycan-binding specificity of the HA was determined by amino acid residues at positions 222 and 227. Inconsistent with the glycan-binding specificity of the recombinant HA protein, virions of Dk/MNG bound to both 3'SLacNAc and 3'SLeX. Glycan-binding analysis in the presence of a neuraminidase (NA) inhibitor revealed that the NA conferred binding to 3'SLeX to virions of Dk/MNG. The present results reveal the molecular basis of the interaction between fucosylated alpha 2,3 sialosides and influenza viruses.
資源タイプ	学術雑誌論文
出版タイプ	Accepted Manuscript
権利情報	The final publication is available at Springer via http://dx.doi.org/10.1007/s00705-015-2660-3
PISSN	0304-8608
EISSN	1432-8798
NCID	AA00548901
関連情報 (isVersionOf)	出版社版DOI https://doi.org/10.1007/s00705-015-2660-3