Expression and maturation of human foamy virus Gag precursor polypeptides
Expression and maturation of human foamy virus Gag precursor polypeptides
复制标题
DOI：
10.1128/jvi.71.2.1635-1639.1997
复制
发表时间：
1997-02-01
影响因子：
5.4
通讯作者：
EmanoilRavier, R
中科院分区：
文献类型：
--
作者：
Giron, ML;Colas, S;EmanoilRavier, R
在本报告中，我们讨论了先前报道的非典型的人类泡沫病毒 Gag 多肽的加工过程。在受感染细胞的细胞质或细胞核以及游离病毒颗粒中，鉴定出两种大约 72 和 68 kDa 的 Gag 前体多肽，p72 通过成熟过程产生 p68。仅在两种情况下观察到 Gag 前体的有效成熟：(i) 在病毒吸附的早期步骤期间和 (ii) 在实验条件下，包括用 DNase I 处理，已知该酶可解离与高离子强度和离子去污剂相关的肌动蛋白聚合物。 Gag 前体与细胞骨架网络的关联可能不是病毒蛋白酶功能缺陷，而是通过抑制蛋白酶的裂解而导致 Gag 蛋白成熟率低。
In this report, we address the processing of the Gag polypeptides of human foamy virus previously reported to be atypical. In the cytoplasm or the nucleus of infected cells as well as in free virus particles, two Gag precursor polypeptides were identified at approximately 72 and 68 kDa, p72 giving rise to p68 by a maturation process. Efficient maturation of Gag precursors was observed only in two situations: (i) during the early steps of virus adsorption and (ii) under experimental conditions, including treatment with DNase I, known to dissociate actin polymers associated with high ionic strength and ionic detergents. Rather than being a defective viral protease function, an association of Gag precursors with a cytoskeleton network might be responsible for the low rate of Gag protein maturation through inhibition of their cleavage by the protease.