Amonsen M, Smith DF, Cummings RD, Air GM. Human parainfluenza viruses hPIV1 and hPIV3 bind oligosaccharides with {alpha}2-3 linked sialic acid that are distinct from those bound by H5 avian influenza hemagglutinin. J Virol. 2007 May 23
We investigated binding of human parainfluenza viruses (hPIV) types 1 and 3 to the Glycan Array of the Consortium for Functional Glycomics, and binding and release from erythrocytes under conditions where neuraminidase is inactive or active. hPIV1 and hPIV3 bind modifications of Neu5Acalpha2-3Galbeta1-4GlcNAc, including the sialyl-Lewis(x) motif and structures containing 6-sulfogalactose. hPIV-1 and hPIV-3 thus bind typical N-linked glycans in contrast to avian influenza H5 hemagglutinin (15) which binds less common motifs. While the receptor is not the sole determinant of tropism, hPIV or H5 influenza infection of specific cells that express receptors may contribute to their different pathologies.
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