Abstract
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.
MeSH Terms
Amino Acid Sequence
Animals
Base Sequence
Capsid/biosynthesis,isolation & purification
Capsid Proteins
Cell-Free System
Classical Swine Fever Virus/metabolism
DNA Mutational Analysis
DNA, Complementary/genetics
Molecular Sequence Data
Pestivirus/metabolism
Protein Precursors/metabolism
Protein Processing, Post-Translational
Recombinant Proteins/biosynthesis
Sequence Analysis
Sequence Homology, Amino Acid
Swine
Tumor Cells, Cultured
Viral Core Proteins/biosynthesis,isolation & purification
Viral Nonstructural Proteins/biosynthesis
Viral Proteins/biosynthesis
Chemicals
Capsid Proteins
DNA, Complementary
Protein Precursors
Recombinant Proteins
Viral Core Proteins
Viral Nonstructural Proteins
Viral Proteins
p23 protein, classical swine fever virus
protein p14, classical swine fever virus
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Stark R
Federal Research Centre for Virus Diseases of Animals, Tübingen, Federal Republic of Germany.
Meyers G
Rümenapf T
Thiel H J
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