PRIMARY STRUCTURES OF THE CORE PROTEINS OF THE ALPHAVIRUSES SEMLIKI FOREST VIRUS AND SINDBIS VIRUS
PRIMARY STRUCTURES OF THE CORE PROTEINS OF THE ALPHAVIRUSES SEMLIKI FOREST VIRUS AND SINDBIS VIRUS
复制标题
DOI：
10.1016/0042-6822(81)90156-2
复制
发表时间：
1981-01-01
期刊：
影响因子：
3.7
通讯作者：
WITTMANNLIEBOLD, B
中科院分区：
文献类型：
--
作者：
BOEGE, U;WENGLER, G;WITTMANNLIEBOLD, B
分析了甲病毒属辛德毕斯病毒和塞姆利基森林病毒的核心蛋白的氨基酸序列。这两种蛋白质的完整的一级结构。在N-末端序列区域的几个点处，使用编码蛋白质的mRNA的核苷酸序列来比对肽。蛋白质的N-末端部分富含碱性氨基酸和脯氨酸;分子的C-末端区域不显示特定类型氨基酸的优势。2个区域之间的转换发生在氨基酸残基110周围的区域。尽管两种分子的C-末端部分存在广泛的序列同源性（163个氨基酸残基中的113个存在于相同的序列中），但N-末端部分存在的序列同源性不太明显。在蛋白质的N-末端部分，物理化学性质而不是确切的氨基酸序列显然是保守的。这两种蛋白质在分子的C-末端高度保守区域中含有真核丝氨酸蛋白酶特征性的氨基酸序列Gly-Asp-Ser-Gly。甲病毒特异性的核心蛋白的两个部分在组装的病毒和病毒结构蛋白的合成中的可能的功能进行了讨论。
The amino acid sequences of the core proteins of the alphaviruses Sindbis virus and Semliki Forest virus were analyzed. The complete primary structures of both proteins are presented. At a few points in the N-terminal sequence regions the nucleotide sequences of the mRNA coding for the proteins were used to align peptides. The N-terminal part of the proteins is rich in basic amino acids and proline; the C-terminal region of the molecules does not show a preponderance of a specific type of amino acid. The transition between the 2 regions occurs in the region around amino acid residue 110. Whereas extensive sequence homology exists in the C-terminal part of both molecules (113 of 163 amino acid residues ware present in identical sequences), the sequence homology present in the N-terminal part is less pronounced. The physicochemical properties rather than the exact amino acid sequence apparently are conserved in the N-terminal parts of the proteins. Both proteins contain the amino acid sequence Gly-Asp-Ser-Gly characteristic of eukaryotic serine proteases in the C-terminal highly conserved region of the molecule. Possible functions of both parts of the alphavirus-specific core proteins in the assembly of the virus and in the synthesis of viral structural proteins are discussed.