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Journal of Virology, September 2005, p. 11533-11536, Vol. 79, No. 17
0022-538X/05/$08.00+0     doi:10.1128/JVI.79.17.11533-11536.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.

A Single Amino Acid Substitution in 1918 Influenza Virus Hemagglutinin Changes Receptor Binding Specificity

Department of Microbiology, Mount Sinai School of Medicine, One Gustave Levy Place, Box 1124, New York, New York 10029,¹ Department of Molecular Biology,² Skaggs Institute for Chemical Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, California 92037,³ Department of Molecular Pathology, Armed Forces Institute of Pathology, Rockville, Maryland 20850,⁴ Influenza Branch, Division of Viral and Rickettsial Diseases, Centers for Disease Control and Prevention, Atlanta, Georgia 30333⁵

Received 19 April 2005/ Accepted 15 June 2005

The receptor binding specificity of influenza viruses may be important for host restriction of human and avian viruses. Here, we show that the hemagglutinin (HA) of the virus that caused the 1918 influenza pandemic has strain-specific differences in its receptor binding specificity. The A/South Carolina/1/18 HA preferentially binds the 2,6 sialic acid (human) cellular receptor, whereas the A/New York/1/18 HA, which differs by only one amino acid, binds both the 2,6 and the 2,3 sialic acid (avian) cellular receptors. Compared to the conserved consensus sequence in the receptor binding site of avian HAs, only a single amino acid at position 190 was changed in the A/New York/1/18 HA. Mutation of this single amino acid back to the avian consensus resulted in a preference for the avian receptor.

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