Hantaan virus replication: effects of monensin, tunicamycin and endoglycosidases on the structural glycoproteins
| Autor: | Joel M. Dalrymple, Lynn Rasmussen, Sherman E. Hasty, Connie S. Schmaljohn |
|---|---|
| Rok vydání: | 1986 |
| Předmět: |
Orthohantavirus
Glycosylation Glycoside Hydrolases viruses Bunyaviridae Biology Virus Replication Virus chemistry.chemical_compound Viral Proteins Viral envelope Virology Acetylglucosaminidase RNA Viruses Monensin Furans Antigens Viral Hantaan virus Glycoproteins chemistry.chemical_classification Viral Structural Proteins Glucosamine Tunicamycin Molecular biology carbohydrates (lipids) Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase Viral replication chemistry Glycoprotein |
| Zdroj: | The Journal of general virology. 67 |
| ISSN: | 0022-1317 |
| Popis: | The monovalent ionophore monensin, which interferes with cellular transport pathways, and the antibiotic tunicamycin, which prevents glycosylation of newly synthesized proteins, were used to examine Hantaan virus particle formation and polypeptide synthesis. Viral replication in the presence of either drug resulted in reduced antigen production as well as reduced yields of both intracellular and extracellular infectious virus. Analysis of viral polypeptides synthesized in the presence of the drugs suggested differential effects of monensin and tunicamycin on Hantaan virus. Although reduced levels of the three major structural proteins were detected with increasing concentrations of monensin, the electrophoretic migrations of the polypeptides synthesized were unaltered. In contrast, after tunicamycin treatment, G1 was no longer detectable and G2 displayed both a quantitative reduction and an apparent molecular weight reduction of approximately 3000. Both G1 and G2 were sensitive to endoglycosidases H and F with resultant electrophoretic mobility shifts corresponding to molecular weights of approximately 7000 for G1 and 3000 for G2. Oligosaccharides appeared to be mostly, but not entirely, of the high-mannose type. |
| Databáze: | OpenAIRE |
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