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

Joao Marques; Jangawar Anwar; Signe Eskildsen-Larsen; Dominique Rebouillat; Søren Riis Paludan; Ganes Sen; Bryan R G Williams; Rune Hartmann

doi:10.1099/vir.0.2008/003558-0

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

Joao Marques, Jangawar Anwar, Signe Eskildsen-Larsen, Dominique Rebouillat, Søren Riis Paludan, Ganes Sen, Bryan R G Williams, Rune Hartmann

Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaper › Journal article › Research › peer-review

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Abstract

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.

Original language	English
Journal	Journal of General Virology
Volume	89
Issue	Pt 11
Pages (from-to)	2767-72
Number of pages	5
ISSN	0022-1317
DOIs	https://doi.org/10.1099/vir.0.2008/003558-0
Publication status	Published - 2008

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

abstract = "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.",

author = "Joao Marques and Jangawar Anwar and Signe Eskildsen-Larsen and Dominique Rebouillat and Paludan, {S{\o}ren Riis} and Ganes Sen and Williams, {Bryan R G} and Rune Hartmann",

year = "2008",

doi = "10.1099/vir.0.2008/003558-0",

language = "English",

volume = "89",

pages = "2767--72",

journal = "Journal of General Virology",

issn = "0022-1317",

publisher = "Microbiology Society",

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The p59 oligoadenylate synthetase-like protein possesses antiviral activity that requires the C-terminal ubiquitin-like domain. / Marques, Joao; Anwar, Jangawar; Eskildsen-Larsen, Signe et al.
In: Journal of General Virology, Vol. 89, No. Pt 11, 2008, p. 2767-72.

Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaper › Journal article › Research › peer-review

TY - JOUR

T1 - The p59 oligoadenylate synthetase-like protein possesses antiviral activity that requires the C-terminal ubiquitin-like domain

AU - Marques, Joao

AU - Anwar, Jangawar

AU - Eskildsen-Larsen, Signe

AU - Rebouillat, Dominique

AU - Paludan, Søren Riis

AU - Sen, Ganes

AU - Williams, Bryan R G

AU - Hartmann, Rune

PY - 2008

Y1 - 2008

N2 - 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.

AB - 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.

U2 - 10.1099/vir.0.2008/003558-0

DO - 10.1099/vir.0.2008/003558-0

M3 - Journal article

C2 - 18931074

SN - 0022-1317

VL - 89

SP - 2767

EP - 2772

JO - Journal of General Virology

JF - Journal of General Virology

IS - Pt 11

ER -

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

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