The glycoprotein of measles virus. External radioactive labelling of its carbohydrate and partial characterization of the glycopeptide
Anttonen, O.; Jokinen, M.; Salmi, A.; Vainionpää, R.; Gahmberg, C.G.
Biochemical Journal 185(1): 189-194
1980
ISSN/ISBN: 0264-6021 PMID: 7378046 DOI: 10.1042/bj1850189
Accession: 006684532
Measles virus was propagated in [African green monkey kidney] Vero cells and purified from the culture supernatants by 2 successive tartrate-density-gradient centrifugations. Surface carbohydrates were labeled both in vitro and in vivo with 3H after treatment with galactose oxidase/NaB3H4 or with [3H]glucosamine. The major labeled glycoprotein in measles virions had a MW of 79,000. After labeling with periodate/ NaB3H4, which would result in specific labeling of sialic acid residues, the 79,000-MW glycoprotein was very weakly labeled. This suggests that there is little or no sialic acid in the virions. Further analysis of the glycoprotein showed that galactose is the terminal carbohydrate unit in the oligosaccharide, and the MW of the glycopeptide obtained after Pronase digestion is about 3000. The oligosaccharide is attached to the polypeptide through an alkali-stable bond, indicating a N-glycosidic asparagine linkage.