Antigenic variants of CVS XXXX with altered glycosylation sites.

@entity3208 @entity535 @entity1735 @entity2734 @entity17839 @entity2975 @entity214
The virion-associated glycoprotein of the CVS-11 strain of @entity17839 exists in two forms, GI and GII, which differ in their @entity1735 content. The structural relationship between GI and GII is investigated in order to account for the difference in glycosylation. Partial sequence analysis and mapping of tryptic glycopeptides isolated from the parent CVS-11 GI and GII glycoprotein forms revealed that two of the three predicted glycosylation sites (at @entity2734 -204 and @entity2734 -319) were utilized in the GI form whereas only one of these two sites (at @entity2734 -319) was utilized in the GII form. One predicted glycosylation site (at @entity2734 -37) was not utilized in either species. In the variant virus, RV231-22, a single glycoprotein species was detected which corresponded in electrophoretic mobility to the GI form of the parent virus. Nucleotide sequence analysis of the variant glycoprotein gene revealed a base mutation which specifies an @entity535 change six residues upstream from the predicted glycosylation site at @entity2734 -204. This single @entity535 substitution apparently results in utilization of the signal at @entity2734 -204 in the GII form of RV231-22 virus. The @entity535 substitution is discussed in relation to altered conformation. In the variant virus RV194-2 (F3), both GI and GII glycoprotein forms were present, but each revealed slower electrophoretic mobilities compared with the corresponding parent glycoprotein forms in @entity3208 - @entity2975 gel electrophoresis ( @entity214 -PAGE). An extra glycosylation site was identified in both glycoprotein forms of this variant virus.
