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Analysis of viral glycoproteins by glycosidic digestion inside a polyacrylamide gel

We adapted the method described by Cleveland et al. (1977); (Peptide mapping by limited proteolysis in sodium dodecyl sulphate and analysis by gel electrophoresis. J. Biol. Chem. 252, 1102–1106) to study the glycosidic residues linked to the viral glycoproteins of two enveloped viruses: Junin virus...

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Bibliographic Details
Published in:Journal of virological methods 1999-07, Vol.80 (2), p.217-221
Main Authors: Grutadauria, Sergio, Castilla, Viviana, Zapata, Marta, Mersich, Susana
Format: Article
Language:English
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Summary:We adapted the method described by Cleveland et al. (1977); (Peptide mapping by limited proteolysis in sodium dodecyl sulphate and analysis by gel electrophoresis. J. Biol. Chem. 252, 1102–1106) to study the glycosidic residues linked to the viral glycoproteins of two enveloped viruses: Junin virus (JV) and rubella virus (RV). Radioiodinated glycoproteins were obtained from purified virions, isolated from SDS–polyacrylamide gels and then hydrolysed by specific glycosidases inside a second gel. N-linked oligosaccharides, mannose and galactose were found as terminal residues in the JV-G1 glycoprotein. Mannose and N-glycans of complex hybrid type were present on RV glycoproteins.
ISSN:0166-0934
1879-0984
DOI:10.1016/S0166-0934(99)00005-1