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The p59 oligoadenylate synthetase-like protein possesses antiviral activity that requires the C-terminal ubiquitin-like domain

Joao Marques^1,

¹ Department of Cancer Biology, The Cleveland Foundation, 9500 Euclid Avenue, Cleveland, OH 44195, USA
² Centre for Structural Biology, Department of Molecular Biology, University of Aarhus, Gustav Wieds vej 10 C, 8000 Aarhus C, Denmark
³ Institute of Medical Microbiology and Immunology, University of Aarhus, Aarhus, Denmark
⁴ Department of Molecular Genetic, The Cleveland Foundation, 9500 Euclid Avenue, Cleveland, OH 44195, USA
⁵ Monash Institute of Medical Research, 246 Clayton Road, Clayton, VIC 3168, Australia

Correspondence
Rune Hartmann
rh{at}mb.au.dk

Viral infection of mammalian cells prompts the innate immune system to initiate an antiviral response. The recognition of the virus triggers several antiviral signalling pathways, which among others include the family of 2'-5' oligoadenylate synthetase (OAS) proteins. The p59 protein encoded by the OAS-like (OASL) gene is an atypical member of the OAS family in the sense that it lacks the characteristic 2'-5' oligoadenylate synthetase activity. We decided to investigate the putative antiviral activity of p59 by ectopically expressing this protein in Vero cells and then infecting these cells with virus. We demonstrate that OASL has an antiviral effect against the single-stranded RNA virus picornavirus, encephalomyocarditis virus, but not against a large DNA virus, herpes simplex virus 1. Importantly, this antiviral activity was lost in a truncated version of p59 lacking the ubiquitin-like C-terminal domain of p59. Taken together our results indicate that p59 is indeed an antiviral protein that works through a novel mechanism distinct from other OAS proteins.

Present address: Department of Biochemistry, Molecular Biology and Cell Biology, Northwestern University, 2205 Tech Drive, Evanston, IL 60208, USA.

A figure showing the lack of 2-5A synthetase activity of p59 is available with the online version of this paper.