Cleavage sites in the polypeptide precursors of poliovirus protein P2-X.
Cleavage sites in the polypeptide precursors of poliovirus protein P2-X.
复制标题
脊髓灰质炎病毒蛋白 P2-X 的多肽前体中的切割位点。
DOI：
10.1016/0042-6822(81)90242-7
复制
发表时间：
1981
期刊：
影响因子：
3.7
通讯作者：
Wimmer,E
中科院分区：
文献类型：
--
作者：
Semler,BL;Hanecak,R;Anderson,CW;Wimmer,E
对脊髓灰质炎病毒多蛋白中心区 (P2) 的三种主要多肽产物 (P2-3b、P2-5b 和 P2-X) 进行了部分氨基末端序列分析，该分析相对于脊髓灰质炎病毒 RNA 基因组的核苷酸序列精确定位了这些产物的氨基末端。与复制酶区域 (P3) 的大多数产物一样，P2-5b 和 P2-X 的氨基末端是通过谷氨酰胺和甘氨酸残基之间的裂解产生的。因此，P2-5b 和 P2-X 可能都是由单一（病毒编码的？）蛋白酶的作用产生的。另一方面，P2-3b 的氨基末端是由 VP1 的羧基末端酪氨酸和核苷酸 3381-3383 编码的甘氨酸之间的裂解产生的。这一结果可能表明脊髓灰质炎病毒多蛋白的完整加工需要不止一种蛋白水解活性。
Partial amino-terminal sequence analysis has been performed on the three major polypeptide products (P2-3b, P2-5b, and P2-X) from the central region (P2) of the poliovirus polyprotein, and this analysis precisely locates the amino termini of these products with respect to the nucleotide sequence of the poliovirus RNA genome. Like most of the products of the replicase region (P3), the amino termini of P2-5b and P2-X are generated by cleavage between glutamine and glycine residues. Thus, P2-5b and P2-X are probably both produced by the action of a single (virus-encoded?) proteinase. The amino terminus of P2-3b, on the other hand, is produced by a cleavage between the carboxy-terminal tyrosine of VP1 and the glycine encoded by nucleotides 3381–3383. This result may suggest that more than one proteolytic activity is required for the complete processing of the poliovirus polyprotein.