Translation of a mixture of the two grapevine fanleaf virus (GFLV) RNAS in reticulocyte lysates in the presence of the amino acid analogs canavanine, S-aminoethyl-cysteine, and p-fluorophenylalanine gave two products of molecular weights (Mr) 220,000 (from RNA-1) and 125,000 (from RNA-2). In the absence of these analogs a protease apparently induced by RNA-1 catalyzed cleavage of the RNA-2 product (Mr 125,000) into two proteins of Mr 68,000 and 58,000. The 58,000 Mr protein was shown to be the likely virus coat protein by peptide mapping after partial proteolysis. Cleavage of the RNA-2 product of GFLV was not catalyzed by the translation products of another nepovirus, tobacco ringspot virus.