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The nsp1 and nsp1β papain-like autoproteinases are essential for porcine reproductive and respiratory syndrome virus RNA synthesis

Judy N. A. Bos-de Ruijter^1,

Ben P. H. Peeters^1,

Janneke J. M. Meulenberg^1,

¹ Wageningen UR, Animal Sciences Group, Division of Infectious Diseases, PO Box 65, 8200 AB Lelystad, The Netherlands
² Molecular Virology Laboratory, Department of Medical Microbiology, Center of Infectious Diseases, Leiden University Medical Center, Leiden, The Netherlands

Correspondence
Lisette A. H. M. Cornelissen
lisette.cornelissen{at}wur.nl

The two N-terminal cleavage products, nsp1 and nsp1β, of the replicase polyproteins of porcine reproductive and respiratory syndrome virus (PRRSV) each contain a papain-like autoproteinase domain, which have been named PCP and PCPβ, respectively. To assess their role in the PRRSV life cycle, substitutions and deletions of the presumed catalytic cysteine and histidine residues of PCP and PCPβ were introduced into a PRRSV infectious cDNA clone. Mutations that inactivated PCP activity completely blocked subgenomic mRNA synthesis, but did not affect genome replication. In contrast, mutants in which PCPβ 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 nsp1β/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/nsp1β and nsp1β/nsp2 junctions.

Present address: Genmab, PO Box 85199, 3508 AD Utrecht, The Netherlands.

Present address: Wageningen UR, Central Institute for Animal Disease Control Lelystad, CIDC-Lelystad, PO Box 2004, 8203 AA Lelystad, The Netherlands.

Present address: Amsterdam Molecular Therapeutics, PO Box 22506, 1100 DA Amsterdam, The Netherlands.