Characterization of bovine rotavirus VP6 and VP7 as glycoproteins using monoclonal antibodies
| Autor: | E. Cornaglia, Youssef Elazhary, Brian G. Talbot |
|---|---|
| Rok vydání: | 1991 |
| Předmět: |
chemistry.chemical_classification
Glycan Linear epitope medicine.drug_class viruses Proteolytic enzymes virus diseases Tunicamycin Biology Monoclonal antibody Microbiology Molecular biology Epitope carbohydrates (lipids) chemistry.chemical_compound Endoglycosidase H Biochemistry chemistry Genetics medicine biology.protein Glycoprotein Molecular Biology |
| Zdroj: | FEMS Microbiology Letters. 79:147-152 |
| ISSN: | 1574-6968 0378-1097 |
| DOI: | 10.1111/j.1574-6968.1991.tb04520.x |
| Popis: | Bovine rotavirus proteins were analysed by a panel of monoclonal antibodies. Glycosylated epitopes were identified on both inner and outer capsid proteins (VP6 and VP7 respectively). VP7 possessed a periodate insensitive epitope which was, however, sensitive to endoglycosidase H, mixed glycosidases and to protease treatment. This epitope was not detected on viruses grown in the presence of 2-deoxy-D-glucose or tunicamycin. An epitope was detected on VP6 which was sensitive to periodate oxidation. The blotted protein reacted with a glycan assay kit; yet the epitope was not affected by endoglycosidase H and was found on viruses grown in the presence of 2-deoxy-D-glucose or tunicamycin. These results suggest that VP7 and VP6 epitopes are carbohydrate dependent. The VP7 epitope contains an N-linked carbohydrate moiety in contrast to the VP6 epitope which appears to contain O-linked glycosyl units. |
| Databáze: | OpenAIRE |
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