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Sequence analysis and receptor specificity of the hemagglutinin of a recent influenza H2N2 virus isolated from chicken in North America

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Abstract

Influenza viruses bind host cells following an interaction between the viral hemagglutinin (HA) protein and host cell sialylated glycoproteins and glycolipids. Differences in binding affinities of the HAs for different types of sialic acid linkages (α2-3 vs. α2-6) contribute to determining the host range of an influenza virus. The ability of an avian influenza virus HA to bind the human form of the receptor may be one requirement for an avian virus to propagate in the human population. In this paper, we describe the characterization of the HA from an H2N2 virus isolated from a Pennsylvania chicken farm in 2004. Sequence analysis revealed that this HA is a member of the Eurasian clade, and receptor binding studies show that it maintains its specificity for the avian influenza virus α2-3 linked sialic acid receptor.

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Abbreviations

A/ck/PA/2004:

A/chicken/Pennsylvania/2004

BSA:

bovine serum albumin

CRBC:

chicken red blood cells

DMEM:

Dulbecco's modified Eagle's medium

FBS:

fetal bovine serum

Gal:

galactose

HA:

hemagglutinin

GFP:

green fluorescence protein

Gln:

glutamine

Gly:

glycine

NVSL:

National Veterinary Services Laboratory

PBS:

phosphate buffer saline

RT-PCR:

reverse transcription-PCR

Sia:

sialic acid

VCNA:

Vibrio cholerae neuraminidase

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Correspondence to Adolfo García-Sastre.

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Glaser, L., Zamarin, D., Acland, H.M. et al. Sequence analysis and receptor specificity of the hemagglutinin of a recent influenza H2N2 virus isolated from chicken in North America. Glycoconj J 23, 93–99 (2006). https://doi.org/10.1007/s10719-006-5441-0

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  • DOI: https://doi.org/10.1007/s10719-006-5441-0

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