甲病毒多肽的氨基末端序列分析。
Amino-terminal sequence analysis of alphavirus polypeptides.
作者信息
Welch W J, Sefton B M, Esch F S
出版信息
J Virol. 1981 Jun;38(3):968-72. doi: 10.1128/JVI.38.3.968-972.1981.
Abstract
The single late 26S mRNA of Semliki Forest virus (SFV) directs the synthesis of the four viral structural proteins, C, E3, E2, and E1, and the recently described nonstructural protein, 6K. We report here partial NH2-terminal amino acid sequences of the SFV polypeptides E3 and 6K and of p62, the precursor to E3 and E2. In addition, were have determined a partial NH2-terminal sequence of the Sindbis virus homolog of 6K, the 4.2K protein. p62 and E3 of SFV have identical NH2-terminal amino acid sequences. Comparison of the partial NH2-terminal sequences of 6K of SFV and 4.2K of Sindbis virus with the deduced amino acid sequence encoded by the 26S mRNA of each virus reveals that the genes for these peptides are located in each case between those for E2 and E1. The order of the genes on the 26S mRNA of the alphaviruses is therefore 5'-C-E3-E2-6K-E1-3'. We discuss two mechanisms by which the nascent viral glycoproteins may be inserted into the membrane of the endoplasmic reticulum.
摘要
辛德毕斯病毒（SFV）的单一晚期26S信使核糖核酸指导合成四种病毒结构蛋白，即衣壳蛋白（C）、E3、E2和E1，以及最近描述的非结构蛋白6K。我们在此报告SFV多肽E3和6K以及E3和E2的前体p62的部分氨基末端氨基酸序列。此外，我们还确定了6K的辛德毕斯病毒同源物4.2K蛋白的部分氨基末端序列。SFV的p62和E3具有相同的氨基末端氨基酸序列。将SFV的6K和辛德毕斯病毒的4.2K的部分氨基末端序列与每种病毒26S信使核糖核酸编码的推导氨基酸序列进行比较，结果表明，这些肽的基因在每种情况下都位于E2和E1的基因之间。因此，甲病毒26S信使核糖核酸上的基因顺序为5'-衣壳蛋白（C）-E3-E2-6K-E1-3'。我们讨论了新生病毒糖蛋白可能插入内质网膜的两种机制。
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本文引用的文献
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The capsid protein of Semliki Forest virus has clusters of basic amino acids and prolines in its amino-terminal region.Semliki森林病毒的衣壳蛋白在其氨基末端区域有碱性氨基酸簇和脯氨酸簇。
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