Processing of rabbit hemorrhagic disease virus polyprotein.
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.
Martín Alonso
J M
JM
Departamento de Bioquímica y Biología Molecular, Universidad de Oviedo, Spain.
Casais
R
R
Boga
J A
JA
Parra
F
F
D000818:Animals; D003546:Cysteine Endopeptidases / Q000378:metabolism; D017929:Hemorrhagic Disease Virus, Rabbit / Q000378:metabolism*; D011499:Protein Processing, Post-Translational; D011506:Proteins / Q000378:metabolism; D011817:Rabbits; D017361:Viral Nonstructural Proteins / Q000378:metabolism; D014764:Viral Proteins / Q000378:metabolism*; D015678:Viral Structural Proteins / Q000378:metabolism
D011506:Proteins; D017361:Viral Nonstructural Proteins; D014764:Viral Proteins; D015678:Viral Structural Proteins; C081149:viral protein 60, rabbit hemorrhagic disease virus; C089391:3C-like protease, rabbit hemorrhagic disease virus; D003546:Cysteine Endopeptidases