Regulation of viral transcription by the matrix protein of vesicular stomatitis virus probed by monoclonal antibodies and temperature-sensitive mutants.
Regulation of viral transcription by the matrix protein of vesicular stomatitis virus probed by monoclonal antibodies and temperature-sensitive mutants.
复制标题
通过单克隆抗体和温度敏感突变体探测水疱性口炎病毒基质蛋白对病毒转录的调节。
DOI：
10.1128/jvi.56.2.386-394.1985
复制
发表时间：
1985
影响因子：
5.4
通讯作者：
Wagner,RR
中科院分区：
文献类型：
--
作者：
Pal,R;Grinnell,BW;Snyder,RM;Wagner,RR
The ability of the matrix (M) protein of wild-type vesicular stomatitis virus (VSV) to regulate viral transcription was studied with monoclonal antibodies and temperature-sensitive (ts) mutants in complementation group III, the M proteins of which are restricted in transcription inhibition. The marked inhibition of transcription by VSV ribonucleoprotein (RNP) cores complexed with M protein (RNP/M) was reversed by antibody to epitope 1. Antibodies to epitopes 2 and 3 not only failed to reverse the transcription-inhibitory activity of isolated M protein but actually increased M-protein inhibition of transcription in a reconstituted system. Monoclonal antibodies to epitopes 2 and 3 strongly bound to M proteins from all wild-type and ts-mutant virions, but monoclonal antibody to epitope 1 completely failed to bind to the M protein of ts023(III) even though it reacted strongly with M proteins of mutants tsG31(III) and tsG33(III). The M protein of a tsO23 revertant (R11) completely recovered its capacity to inhibit transcription and to bind monoclonal antibody to epitope 1, whereas the M proteins of three other revertants remained restricted in their capacity to inhibit transcription and to bind monoclonal antibody to epitope 1. These studies indicate that exposure of epitope 1 on the surface of M protein is essential for inhibiting transcription by VSV RNP cores.
