Multiple proteases in foot-and-mouth disease virus replication.
Translation of foot-and-mouth disease virus RNA in a rabbit reticulocyte lysate for short time intervals resulted in the production of the peptides P20a , P16, and P88 (Lab, Lb, and P1) (R. R. Rueckert , Recommendations of the 3rd European Study Group on Molecular Biology of Picornavirus, Urbino , Italy, 1983). If further translation was prevented, the structural protein precursor P88 was not cleaved, even after prolonged incubation. This result indicates that the mechanism of the cleavage between P20a -P16 and P88 and of that between P88 and P52 (P2) differs from the mechanism of the secondary cleavages which produce the structural proteins. Furthermore, treatment of foot-and-mouth disease virus-infected cells with the protease inhibitor D-valyl phenylalanyl lysyl chloromethyl ketone prevented the in vivo cleavage between P20a -P16 and P88 but had no effect on any of the other cleavage events. These results suggest that the cleavage of the foot-and-mouth disease virus polyprotein utilizes two different host proteases.
D000818:Animals; D005537:Aphthovirus / Q000201:enzymology / Q000235:genetics*; D002460:Cell Line; D006224:Cricetinae; D004261:DNA Replication; D007668:Kidney; D007700:Kinetics; D010447:Peptide Hydrolases / Q000235:genetics*; D014176:Protein Biosynthesis; D011817:Rabbits; D012156:Reticulocytes / Q000378:metabolism; D014764:Viral Proteins / Q000235:genetics; D014779:Virus Replication
D014764:Viral Proteins; D010447:Peptide Hydrolases