1887

Abstract

are a family of insect RNA viruses that diverged profoundly from other families of the . Mesonivirus replicative proteins are produced from large polyprotein (pp) precursors (pp1a and pp1ab) through proteolytic cleavage by the viral 3C-like protease (3CL) and, possibly, other proteases. Using recombinant forms of the Cavally virus 3CL and pp1a/pp1ab-derived substrates, we characterized 3CL cleavage sites in mesonivirus polyproteins. Our data lead us to suggest that 3CL cleaves the central and C-proximal regions of mesonivirus pp1a/pp1ab at 12 conserved sites. Compared to other nidovirus homologues, the mesonivirus 3CL features a distinct substrate specificity, with asparagine at P2 being a major specificity determinant. Furthermore, we provide evidence that expression of the ORF1b-encoded part of pp1ab involves a −1 ribosomal frameshift at a conserved GGAUUUU heptanucleotide sequence in the ORF1a/1b overlap region. Taken together, the study identifies critical steps in the expression and maturation of mesonivirus replicative proteins.

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2016-06-01
2024-04-19
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