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首页> 外文期刊>Journal of Virology >Amino-terminal sequence analysis of alphavirus polypeptides.
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Amino-terminal sequence analysis of alphavirus polypeptides.

机译：alphavirus多肽的氨基末端序列分析。

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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.
机译：Semliki林病毒（SFV）的单身后期MRNA指示四种病毒结构蛋白，C，E3，E2和E1的合成，最近描述的非结构蛋白6K。我们在此报告SFV多肽E3和6K和P62的部分NH 2 - 末端氨基酸序列，E3和E2的前体。此外，已确定6K，4.2K蛋白的SINDBIS病毒同源物的部分NH2末端序列。 SFV的P62和E3具有相同的NH2 - 末端氨基酸序列。对每个病毒26s mRNA编码的推导氨基酸序列的SFV和4.2K的部分NH 2末端序列的比较显示，这些肽的基因位于E2和E1之间的每种情况下。因此，alphavirouses的26s mRNA上的基因的顺序是5'-C-E3-E2-6K-E1-3'。我们讨论两种机制可以将新生病毒糖蛋白可以插入内质网的膜中。

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