辛德毕斯病毒分离株E2蛋白中一条额外的高甘露糖型寡糖链。
One extra oligosaccharide chain of the high-mannose class in the E2 protein of a Sindbis virus isolate.
作者信息
Cancedda R, Bonatti S, Leone A
出版信息
J Virol. 1981 Apr;38(1):8-14. doi: 10.1128/JVI.38.1.8-14.1981.
Abstract
The number and nature of oligosaccharide chains in the E2 envelope protein (and its precursor PE2) from two strains of Sindbis virus, originally derived from the same HR strain, were investigated. The E2 glycoproteins (and the PE2 proteins) of the two strains had different electrophoretic mobilities on a sodium dodecyl sulfate-polyacrylamide gel. We observed that the glycopeptides from the E2 protein of one of the two strains included an extra oligosaccharide chain of the mannose-rich type. The altered pattern of glycosylation does not interfere with the intracellular migration of the protein and the envelopment and budding of the virus.
摘要
对最初源自同一HR株的两株辛德毕斯病毒E2包膜蛋白（及其前体PE2）中寡糖链的数量和性质进行了研究。这两株病毒的E2糖蛋白（和PE2蛋白）在十二烷基硫酸钠-聚丙烯酰胺凝胶上具有不同的电泳迁移率。我们观察到，两株病毒中一株的E2蛋白糖肽包含一条额外的富含甘露糖型寡糖链。糖基化模式的改变并不影响该蛋白在细胞内的迁移以及病毒的包膜和出芽过程。
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