The equine-virulent Venezuelan encephalitis virus, Trinidad donkey (TRD), was compared to its vaccine derivative, TC-83 virus, by examining the glycosylation of the two structural envelope glycoproteins (E and E). The number of size classes of glycopeptides on the glycoproteins was determined by P-6 column chromatography following Pronase digestion. The E glycoprotein had three glycopeptide size species and the E glycoprotein contained four size species ranging in mol. wt. from 1900 to 2700. Both viruses contained similar glycopeptide size species, although the relative amounts on the E glycoproteins appeared to be somewhat different. All of the glycopeptide species appeared to be complex, since all were labelled with glucosamine, mannose, galactose and fucose. No mannose-rich species could be detected. The different glycopeptide species appeared to be sialylation isomers of a smaller core glycopeptide with an apparent mol. wt. of 1800 which was the sole product following desialylation of the larger glycopeptides. The number of oligosaccharide attachment sites present on both E and E of each virus was determined using reverse-phase high pressure liquid chromatography. This analysis indicated that the E glycoprotein of both viruses had six or seven similar sugar-labelled peptide fragments following trypsin digestion. However, the E glycoprotein of TRD virus contained three oligosaccharide attachment sites, whereas TC-83 E glycoprotein had only two.


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