A second protease of foot-and-mouth disease virus.
AUTOR(ES)
Strebel, K
RESUMO
Foot-and-mouth disease virus (FMDV) genes are expressed as a polyprotein which is rapidly processed into the four primary cleavage products L, P1, P2, and P3. In secondary cleavage reactions, these are further processed into the mature proteins. The FMDV L protein is located at the N terminus of the polyprotein and is the first gene product released from the nascent polyprotein. For analysis of its biological function, the L gene was mutated by site-directed mutagenesis of cloned cDNA. In vitro translation of in vitro transcripts of these DNAs and expression studies in Escherichia coli showed that the L mutants affect the processing of the viral polyprotein. The mutants isolated were partially or totally defective in processing the polyprotein at the L/P1 junction. These mutants could, however, be processed in the presence of the wild-type L protein. Furthermore, an antiserum directed against the L protein inhibited processing at the L/P1 cleavage site, so that the release of the L protein from the polyprotein was blocked. These data reveal that the L gene product represents a viral protease which catalyzes its own release from the nascent polyprotein.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=252997Documentos Relacionados
- Antiviral effects of a thiol protease inhibitor on foot-and-mouth disease virus.
- In vitro morphogenesis of foot-and-mouth disease virus.
- Analysis of neutralizing epitopes on foot-and-mouth disease virus.
- Nucleotide sequence and genome organization of foot-and-mouth disease virus.
- Biochemical map of polypeptides specified by foot-and-mouth disease virus.