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J. Virol., Feb 1996, 1261-1265, Vol 70, No. 2
Copyright © 1996, American Society for Microbiology

Processing of rabbit hemorrhagic disease virus polyprotein

JM Martin Alonso, R Casais, JA Boga and F Parra
Departamento de Bioquimica y Biologia Molecular, Universidad de Oviedo, Spain.

Expression of rabbit hemorrhagic disease virus (RHDV) cDNAs in vitro with rabbit reticulocyte lysates and in Escherichia coli have been used to study the proteolytic processing of RHDV polyprotein encoded by ORF1. An epitope tag was used for monitoring the gene products by a specific antibody. We have identified four gene products with molecular masses 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-kDa products were determined and indicated that RHDV 3C proteinase cleaved Glu-Gly peptide bonds.

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