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Journal of Virology, August 2008, p. 8204-8209, Vol. 82, No. 16
0022-538X/08/$08.00+0     doi:10.1128/JVI.00718-08
Copyright © 2008, American Society for Microbiology. All Rights Reserved.

Amino Acid 226 in the Hemagglutinin of H4N6 Influenza Virus Determines Binding Affinity for {alpha}2,6-Linked Sialic Acid and Infectivity Levels in Primary Swine and Human Respiratory Epithelial Cells {triangledown}

Allen C. Bateman,1 Marc G. Busch,1 Alexander I. Karasin,1 Nicolai Bovin,2 and Christopher W. Olsen1*

Department of Pathobiological Sciences, School of Veterinary Medicine, University of Wisconsin-Madison, Madison, Wisconsin,1 Russian Academy of Sciences, Shemyakin and Ovchinnikov Institute of Bioorganic Chemistry, Moscow, Russia2

Received 1 April 2008/ Accepted 29 May 2008

Avian lineage H4N6 influenza viruses previously isolated from pigs differ at hemagglutinin amino acids 226 and 228 from H4 subtype viruses isolated from birds. Using a parental H4N6 swine isolate and hemagglutinin mutant viruses (at residues 226 and/or 228), we determined that viruses which contain L226 had a higher affinity for sialic acid {alpha}2,6 galactose (SA{alpha}2,6Gal) and a higher infectivity level for primary swine and human respiratory epithelial cells, whereas viruses which contain Q226 had lower SA{alpha}2,6Gal affinity and lower infectivity levels for both types of cells. Using specific neuraminidases, we found that irrespective of their relative binding preferences, all of the influenza viruses examined utilized SA{alpha}2,6Gal to infect swine and human cells.


* Corresponding author. Mailing address: School of Veterinary Medicine, University of Wisconsin-Madison, 2015 Linden Drive, Madison, WI 53706. Phone: (608) 263-5819. Fax: (608) 890-1774. E-mail: olsenc{at}svm.vetmed.wisc.edu

{triangledown} Published ahead of print on 11 June 2008.


Journal of Virology, August 2008, p. 8204-8209, Vol. 82, No. 16
0022-538X/08/$08.00+0     doi:10.1128/JVI.00718-08
Copyright © 2008, American Society for Microbiology. All Rights Reserved.