期刊
INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES
卷 23, 期 13, 页码 -出版社
MDPI
DOI: 10.3390/ijms23136946
关键词
Hsp90; heat shock protein 90; rabies virus; large protein; phosphoprotein
资金
- Polish National Science Centre [2016/23/B/NZ6/02536]
- ESF [POWR.03.02.00-00-1028/17-00]
- Mossakowski Medical Research Institute, Warsaw, Poland
The replication of Mononegavirales viruses relies on the chaperone activity of Hsp90, with a specific interaction between L and P proteins being necessary for functional viral polymerase. Interestingly, rabies and vesicular stomatitis virus L proteins can be expressed independently of P protein presence and in the presence of Hsp90 inhibitor.
Mononegavirales is an order of viruses with a genome in the form of a non-segmented negative-strand RNA that encodes several proteins. The functional polymerase complex of these viruses is composed of two proteins: a large protein (L) and a phosphoprotein (P). The replication of viruses from this order depends on Hsp90 chaperone activity. Previous studies have demonstrated that Hsp90 inhibition results in the degradation of mononegaviruses L protein, with exception of the rabies virus, for which the degradation of P protein was observed. Here, we demonstrated that Hsp90 inhibition does not affect the expression of rabies L and P proteins, but it inhibits binding of the P protein and L protein into functional viral polymerase. Rabies and the vesicular stomatitis virus, but not the measles virus, L proteins can be expressed independently of the presence of a P protein and in the presence of an Hsp90 inhibitor. Our results suggest that the interaction of L proteins with P proteins and Hsp90 in the process of polymerase maturation may be a process specific to particular viruses.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据