In:
Journal of General Virology, Microbiology Society, Vol. 89, No. 2 ( 2008-02-01), p. 494-499
Abstract:
The two N-terminal cleavage products, nsp1 α and nsp1 β , of the replicase polyproteins of porcine reproductive and respiratory syndrome virus (PRRSV) each contain a papain-like autoproteinase domain, which have been named PCP α and PCP β , respectively. To assess their role in the PRRSV life cycle, substitutions and deletions of the presumed catalytic cysteine and histidine residues of PCP α and PCP β were introduced into a PRRSV infectious cDNA clone. Mutations that inactivated PCP α activity completely blocked subgenomic mRNA synthesis, but did not affect genome replication. In contrast, mutants in which PCP β activity was blocked proved to be non-viable and no sign of viral RNA synthesis could be detected, indicating that the correct processing of the nsp1 β /nsp2 cleavage site is essential for PRRSV genome replication. In conclusion, the data presented here show that a productive PRRSV life cycle depends on the correct processing of both the nsp1 α /nsp1 β and nsp1 β /nsp2 junctions.
Type of Medium:
Online Resource
ISSN:
0022-1317
,
1465-2099
DOI:
10.1099/vir.0.83253-0
Language:
English
Publisher:
Microbiology Society
Publication Date:
2008
detail.hit.zdb_id:
2007065-2
SSG:
12
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