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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

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Please use this identifier to cite or link to this item:http://hdl.handle.net/2115/64424

Title: 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
Authors: Hiono, Takahiro Browse this author
Okamatsu, Masatoshi Browse this author →KAKEN DB
Igarashi, Manabu Browse this author →KAKEN DB
McBride, Ryan Browse this author
de Vries, Robert P. Browse this author
Peng, Wenjie Browse this author
Paulson, James C. Browse this author
Sakoda, Yoshihiro Browse this author →KAKEN DB
Kida, Hiroshi Browse this author →KAKEN DB
Keywords: influenza A virus
hemagglutinin
receptor specificity
fucosylation
sialyl Lewis X
Issue Date: Feb-2016
Publisher: Springer
Journal Title: Archives of Virology
Volume: 161
Issue: 2
Start Page: 307
End Page: 316
Publisher DOI: 10.1007/s00705-015-2660-3
Abstract: 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.
Rights: The final publication is available at Springer via http://dx.doi.org/10.1007/s00705-015-2660-3
Type: article (author version)
URI: http://hdl.handle.net/2115/64424
Appears in Collections:人獣共通感染症リサーチセンター (Research Center for Zoonosis Control) > 雑誌発表論文等 (Peer-reviewed Journal Articles, etc)

Submitter: 喜田 宏

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