Relative accessibility of N-acetylglucosamine in trimers of the adenovirus types 2 and 5 fiber proteins
| Autor: | Richard B. Marchase, Gerald W. Hart, Robert S. Haltiwanger, Jeffrey A. Engler, Karen Gheesling Mullis |
|---|---|
| Rok vydání: | 1990 |
| Předmět: |
Cytoplasm
Glycosylation Macromolecular Substances Nuclear Envelope viruses Blotting Western Immunology In Vitro Techniques Microbiology Chromatography Affinity Acetylglucosamine Sepharose chemistry.chemical_compound Capsid Affinity chromatography Lectins Virology N-Acetylglucosamine Transferase Fiber biology Adenoviruses Human Galactose Lectin biochemical phenomena metabolism and nutrition Galactosyltransferases Wheat germ agglutinin Molecular Weight carbohydrates (lipids) Biochemistry chemistry Insect Science biology.protein Capsid Proteins Protein Processing Post-Translational HeLa Cells Research Article |
| Zdroj: | Journal of Virology. 64:5317-5323 |
| ISSN: | 1098-5514 0022-538X |
| DOI: | 10.1128/jvi.64.11.5317-5323.1990 |
| Popis: | Fiber is an adenovirus capsid protein responsible for virus attachment to the cell surface and contains O-linked N-acetylglucosamine (GlcNAc). Results of both amino acid analysis and Dionex chromatography indicated that 3 to 4 and 1.7 to 2.5 mol of GlcNAc are attached per mol of affinity-purified adenovirus type 2 (Ad2) and Ad5 fibers, respectively. Fiber shares an epitope with nuclear pore proteins containing O-linked GlcNAc, as shown by reactivity to monoclonal antibody RL2 directed against these pore proteins. GlcNAc on fiber was found to serve as an acceptor for the transfer of galactose from UDP-galactose by 4 beta-galactosyl-transferase in Ad2 and Ad5 but not in Ad7; quantitation by labeling with UDP-[U-14C]galactose in this reaction gave a 100-fold-lower estimate of the GlcNAc content of fiber, suggesting that these monosaccharides are buried within fiber trimers and are not accessible to the transferase. Affinity chromatography on lectin-bound Sepharose beads showed that Ad2 and Ad5 fibers bound weakly to wheat germ agglutinin and did not bind to ricin or concanavalin A; weak binding to wheat germ agglutinin suggests either that GlcNAc is not easily accessible or that there are not sufficient GlcNAcs for efficient binding. These data suggest that O-linked GlcNAc might be important for Ad2 and Ad5 fiber assembly or stabilization. |
| Databáze: | OpenAIRE |
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