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Journal of Virology, March 2007, p. 2923-2929, Vol. 81, No. 6
0022-538X/07/$08.00+0     doi:10.1128/JVI.02077-06
Copyright © 2007, American Society for Microbiology. All Rights Reserved.

The MyD116 African Swine Fever Virus Homologue Interacts with the Catalytic Subunit of Protein Phosphatase 1 and Activates Its Phosphatase Activity{triangledown}

José Rivera ,1,{dagger},{ddagger} Charles Abrams,2,{dagger} Bruno Hernáez,1 Alberto Alcázar,3 José M. Escribano,1 Linda Dixon,2 and Covadonga Alonso1*

Departamento de Biotecnología, INIA, Ctra. La Coruña km 7.5, 28040 Madrid, Spain,1 Institute for Animal Health, Pirbright GU24 ONF, United Kingdom,2 Servicio de Bioquímica-Investigación, Hospital Ramon y Cajal, 28034 Madrid, Spain3

Received 22 September 2006/ Accepted 3 January 2007

The DP71L protein of African swine fever virus (ASFV) shares sequence similarity with the herpes simplex virus ICP34.5 protein over a C-terminal domain. We showed that the catalytic subunit of protein phosphatase 1 (PP1) interacts specifically with the ASFV DP71L protein in a yeast two-hybrid screen. The chimeric full-length DP71L protein, from ASFV strain Badajoz 71 (BA71V), fused to glutathione S-transferase (DP71L-GST) was expressed in Escherichia coli and shown to bind specifically to the PP1-{alpha} catalytic subunit expressed as a histidine fusion protein (6xHis-PP1{alpha}) in E. coli. The functional effects of this interaction were investigated by measuring the levels of PP1 and PP2A in ASFV-infected Vero cells. This showed that infection with wild-type ASFV strain BA71V activated PP1 between two- and threefold over that of mock-infected cells. This activation did not occur in cells infected with the BA71V isolate in which the DP71L gene had been deleted, suggesting that expression of DP71L leads to PP1 activation. In contrast, no effect was observed on the activity of PP2A following ASFV infection. We showed that infection of cells with wild-type BA71V virus resulted in decreased phosphorylation of the {alpha} subunit of eukaryotic initiation factor 2 (eIF-2{alpha}). ICP34.5 recruits PP1 to dephosphorylate the {alpha} subunit of eukaryotic translational initiation factor 2 (also known as eIF-2{alpha}); possibly the ASFV DP71L protein has a similar function.

* Corresponding author. Mailing address: Departamento de Biotecnología, INIA, Ctra. La Coruña km 7.5, 28040 Madrid, Spain. Phone: 34 91 3476896. Fax: 34 91 3573107. E-mail: calonso{at}inia.es.

{triangledown} Published ahead of print on 10 January 2007.

{dagger} J. Rivera and C. Abrams contributed equally to this work.

{ddagger} Present address: Centro Nacional de Investigaciones Oncológicas (CNIO), Melchor Fernández Almagro, 3, 28029 Madrid, Spain.

Journal of Virology, March 2007, p. 2923-2929, Vol. 81, No. 6
0022-538X/07/$08.00+0     doi:10.1128/JVI.02077-06
Copyright © 2007, American Society for Microbiology. All Rights Reserved.



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