Abstract |
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 Neu5Acalpha2-3Galbeta1-4GlcNAc, including the sialyl-Lewis(x) 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.
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Authors | Mary Amonsen, David F Smith, Richard D Cummings, Gillian M Air |
Journal | Journal of virology
(J Virol)
Vol. 81
Issue 15
Pg. 8341-5
(Aug 2007)
ISSN: 0022-538X [Print] United States |
PMID | 17522226
(Publication Type: Journal Article, Research Support, N.I.H., Extramural)
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Chemical References |
- Hemagglutinin Glycoproteins, Influenza Virus
- Oligosaccharides
- Polysaccharides
- Receptors, Virus
- hemagglutinin, avian influenza A virus
- N-Acetylneuraminic Acid
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Topics |
- Animals
- Carbohydrate Conformation
- Carbohydrate Sequence
- Hemagglutinin Glycoproteins, Influenza Virus
(metabolism)
- Humans
- Influenza A Virus, H5N1 Subtype
(metabolism)
- Microarray Analysis
- Molecular Sequence Data
- N-Acetylneuraminic Acid
(chemistry, metabolism)
- Oligosaccharides
(chemistry, metabolism)
- Parainfluenza Virus 1, Human
(metabolism)
- Parainfluenza Virus 3, Human
(metabolism)
- Polysaccharides
(chemistry, metabolism)
- Receptors, Virus
(metabolism)
- Respirovirus Infections
- Virus Attachment
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