Both G W, Siegman L J, Bellamy A R, Atkinson P H
J Virol. 1983 Nov;48(2):335-9. doi: 10.1128/JVI.48.2.335-339.1983.
A cloned DNA copy of simian rotavirus SA11 genomic segment 10 was used to confirm the assignment of the nonstructural glycoprotein NCVP5 to this gene. Determination of the nucleotide sequence for gene 10 indicated that NCVP5 is 175 amino acids in length and has an N-terminal hydrophobic region with the characteristics of a signal sequence for membrane translocation. Unexpectedly, this region was also the location for the only two potential glycosylation sites within the molecule, asparagine residues 8 and 18. The carbohydrates carried by NCVP5 were of the high-mannose type, Man9GlcNAc and Man8GlcNAc, with the mannose 9 species predominating; no complex oligosaccharides were present. If these asparagine residues are the sites for carbohydrate attachment, this implies that cleavage of the putative signal peptide does not occur during the maturation of this nonstructural glycoprotein.
使用猿猴轮状病毒SA11基因组片段10的克隆DNA拷贝来确认非结构糖蛋白NCVP5与该基因的对应关系。对基因10的核苷酸序列测定表明,NCVP5长度为175个氨基酸,其N端有一个疏水区域,具有膜转运信号序列的特征。出乎意料的是,该区域也是分子内仅有的两个潜在糖基化位点的位置,即天冬酰胺残基8和18。NCVP5携带的碳水化合物为高甘露糖型,即Man9GlcNAc和Man8GlcNAc,其中甘露糖9型占主导;不存在复合寡糖。如果这些天冬酰胺残基是碳水化合物附着的位点,这意味着在这种非结构糖蛋白的成熟过程中,假定的信号肽不会被切割。