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

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 (alpha2-3 vs. alpha2-6) 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 alpha2-3 linked sialic acid receptor.

• Authors: Laurel Glaser, Dmitriy Zamarin, Helen M Acland, Erica Spackman, Peter Palese, Adolfo García-Sastre, Deepanker Tewari
• Journal: Glycoconjugate journal (Glycoconj J) Vol. 23 Issue 1-2 Pg. 93-9 (Feb 2006) ISSN: 0282-0080 [Print] United States
• PMID: 16575526 (Publication Type: Journal Article, Research Support, N.I.H., Extramural)

Chemical References

• Hemagglutinin Glycoproteins, Influenza Virus
• Receptors, Cell Surface
• Receptors, Virus
• sialic acid receptor

Topics

• Amino Acid Sequence
• Animals
• Base Sequence
• Chickens (virology)
• Hemagglutinin Glycoproteins, Influenza Virus (chemistry, metabolism)
• Influenza A Virus, H2N2 Subtype (chemistry, immunology)
• Molecular Sequence Data
• Pennsylvania
• Phylogeny
• Receptors, Cell Surface (metabolism)
• Receptors, Virus (metabolism)