PROCESSING OF PESTIVIRUS POLYPROTEIN - CLEAVAGE SITE BETWEEN AUTOPROTEASE AND NUCLEOCAPSID PROTEIN OF CLASSICAL SWINE FEVER VIRUS

被引:146
作者
STARK, R
MEYERS, G
RUMENAPF, T
THIEL, HJ
机构
[1] FED RES CTR VIRUS DIS ANIM, POB 1149, D-72001 TUBINGEN, GERMANY
[2] CALTECH, DIV BIOL, PASADENA, CA 91125 USA
关键词
D O I
10.1128/JVI.67.12.7088-7095.1993
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
The polyprotein of classical swine fever virus starts with the nonstructural protein p23, which is followed by the nucleocapsid protein p14. Proteolytic cleavage between p23 and p14 was demonstrated in a cell-free transcription-translation system. Successive truncation of the cDNA used for the transcription indicated that the proteolytic activity responsible for the cleavage between p23 and p14 resides within p23. In order to determine the cleavage site between these two proteins, the respective genomic regions were expressed in two different expression systems. N-terminal sequencing of the resulting p14-related proteins revealed that cleavage occurs between Cys-168 and Ser-169. Comparison of the sequence around the cleavage site with sequences of other pestiviruses suggests a conserved processing site between similar proteins.
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页码:7088 / 7095
页数:8
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