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Title: SEQUENCE ANALYSIS AND RECEPTOR SPECIFICITY OF THE HEMAGGLUTININ OF A RECENT INFLUENZA H2N2 VIRUS ISOLATED FROM CHICKEN IN NORTH AMERICA

Author
item GLASER, LAUREL - MT SINAI - NEW YORK, NY
item ZAMARIN, DMITRIY - MT SINAI - NEW YORK, NY
item ACLAND, HELEN - PA DEPT OF AGRI - PA
item Spackman, Erica
item PALESE, PETER - MT SINAI - NEW YORK, NY
item GARCIA-SASTRE, ADOLFO - MT SINAI - NEW YORK, NY
item TEWARI, DEEPANKER - PA DEPT OF AGRI - PA

Submitted to: Glycoconjugate
Publication Type: Peer Reviewed Journal
Publication Acceptance Date: 6/30/2005
Publication Date: 4/9/2006
Citation: Glaser, L., Zamarin, D., Acland, H.M., Spackman, E., Palese, P., Garcia-Sastre, A., Tewari, D. 2006. Sequence analysis and receptor specificity of the hemagglutinin of a recent influenza h2n2 virus isolated from chicken in north america. Glycoconjugate. 23:93-99.

Interpretive Summary: In 2002 an H2N2 subtype influenza virus was isolated from chickens on a farm in Pennsylvania. Because H2N2 is an influenza virus subtype that has historically infected humans, this isolate was tested to determine if the receptor had binding properties of an avian or human virus. The virus was determined to have properties consistent with a wild bird type virus. This was supported by the genetics of the virus which were also consistent with a wild bird type virus.

Technical 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.