Kotwal G J, Capone J, Irving R A, Rhee S H, Bilan P, Toneguzzo F, Hofmann T, Ghosh H P
Virology. 1983 Aug;129(1):1-11. doi: 10.1016/0042-6822(83)90390-2.
The NH2-terminal amino acid sequences of the envelope glycoproteins and the in vitro synthesized, nonglycosylated precursors of the glycoproteins of three serotypes, namely Indiana (Toronto), Cocal, and New Jersey (Concan) of vesicular stomatitis virus were determined. A comparison of the sequences showed little homology in the signal peptides present in the nonglycosylated precursors except for their high hydrophobic amino acid content. In contrast, the NH2-terminal amino acid sequences of the mature envelope glycoproteins revealed extensive homology suggesting that this region is conserved and may be involved in essential biological function(s) of the rhabdovirus.
测定了水疱性口炎病毒三种血清型(即印第安纳型(多伦多株)、科卡尔型和新泽西型(康坎株))包膜糖蛋白的氨基末端氨基酸序列以及这些糖蛋白的体外合成非糖基化前体的序列。序列比较显示,非糖基化前体中存在的信号肽之间几乎没有同源性,只是它们的疏水氨基酸含量较高。相比之下,成熟包膜糖蛋白的氨基末端氨基酸序列显示出广泛的同源性,这表明该区域是保守的,可能参与弹状病毒的基本生物学功能。