Structural and functional characterization of the RNA-positive complementation groups, C and D, of the New Jersey serotype of vesicular stomatitis virus: assignment of the M gene to the C complementation group.
Structural and functional characterization of the RNA-positive complementation groups, C and D, of the New Jersey serotype of vesicular stomatitis virus: assignment of the M gene to the C complementation group.
复制标题
新泽西水泡性口炎病毒血清型的 RNA 阳性互补组 C 和 D 的结构和功能特征：将 M 基因分配给 C 互补组。
DOI：
10.1016/0042-6822(84)90089-8
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发表时间：
1984
期刊：
影响因子：
3.7
通讯作者：
Lesnaw,JA
中科院分区：
文献类型：
--
作者：
Kennedy-Morrow,J;Lesnaw,JA
The structural and functional lesions in the RNA-positive complementation groups, C and D, of the New Jersey serotype (Hazelhurst subtype) of vesicular stomatitis virus have been characterized. The M protein of the temperature-sensitive mutant C1, the prototype of the C complementation group, was degraded at the restrictive temperaturein vivo, and was resolved from the wild-type M protein by SDS-polyacrylamide gel electrophoresis and nonequilibrium pH gradient electrophoresis. Coreversion of these properties and the temperature-sensitive phenotype was observed in a spontaneous revertant. On the basis of these results, the M gene was assigned to the C complementation group. Intracellular nucleocapsids could not be isolated from New Jersey serotype infections by procedures developed for Indiana serotype infections. Therefore, in order to assess the ability of New Jerseytsmutants to accumulate nucleocapsids at the restrictive temperature, a procedure for their isolation was developed. Hypertranscription was observed in C1-infected cells incubated at the restrictive temperature, but was not accompanied by proportionate increases in intracellular viral nucleocapsids or protein synthesis. The G and N proteins of the temperature-sensitive mutant D1, the sole representative of the D complementation group, were electrophoresic variants. The relative yield of intracellular D1 N protein was lower at the restrictive than at the permissive temperature, and the D1 L protein was thermolabile. No intracellular viral nucleocapsids were detected in D1 infected cells incubated at the restrictive temperature; however, more 40 S and less message-sized RNA were synthesized at the restrictive than at the permissive temperature. These results suggested functional defects in both the N protein and polymerase of D1.
