PROCESSING OF RABBIT HEMORRHAGIC-DISEASE VIRUS POLYPROTEIN

Expression of rabbit hemorrhagic disease virus (RHDV) cDNAs in vitro w ith rabbit reticulocyte lysates and in Escherichia coli have been used to study the proteolytic processing of RHDV polyprotein encoded by OR F1. An epitope tag was used for monitoring the gene products by a spec ific antibody. We have identified four gene products with molecular ma sses of 80, 43, 73, and 60 kDa, from the amino to the carboxy terminus of the polyprotein. The amino-terminal sequences of the 43- and 73-kD a products were determined and indicated that RHDV 3C proteinase cleav ed Glu-Gly peptide bonds.