Previous Article | Next Article ![]()
Journal of Virology, August 2007, p. 8341-8345, Vol. 81, No. 15
0022-538X/07/$08.00+0 doi:10.1128/JVI.00718-07
Copyright © 2007, American Society for Microbiology. All Rights Reserved.
2-3-Linked Sialic Acids That Are Distinct from Those Bound by H5 Avian Influenza Virus Hemagglutinin
Department of Biochemistry and Molecular Biology, University of Oklahoma Health Sciences Center, Oklahoma City, Oklahoma,1 Department of Biochemistry and Consortium for Functional Glycomics Core H, Emory University School of Medicine, Atlanta, Georgia2
Received 3 April 2007/ Accepted 9 May 2007
We investigated the binding of human parainfluenza virus types 1 and 3 (hPIV1 and hPIV3, respectively) to the glycan array of the Consortium for Functional Glycomics and binding and their release from erythrocytes under conditions where neuraminidase is inactive or active. hPIV1 and hPIV3 bind modifications of Neu5Ac
2-3Galß1-4GlcNAc, including the sialyl-Lewisx motif and structures containing 6-sulfogalactose. hPIV1 and hPIV3 thus bind typical N-linked glycans, in contrast to avian influenza virus H5 hemagglutinin (J. Stevens, O. Blixt, T. M. Tumpey, J. K. Taubenberger, J. C. Paulson, and I. A. Wilson, Science 312:404-410, 2006), which binds less-common motifs. While the receptor is not the sole determinant of tropism, hPIV or H5 influenza virus infection of specific cells that express receptors may contribute to their different pathologies.
Published ahead of print on 23 May 2007.
This article has been cited by other articles:
Copyright © 2009 by the American Society for Microbiology. For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»