The oligoadenylate synthetase family: an ancient protein family with multiple antiviral activities

Helle Kristiansen; Hans Henrik Gad; Signe Eskildsen Larsen; Philippe Despres; Rune Hartmann

doi:10.1089/jir.2010.0107

The oligoadenylate synthetase family: an ancient protein family with multiple antiviral activities

Helle Kristiansen, Hans Henrik Gad, Signe Eskildsen Larsen, Philippe Despres, Rune Hartmann

Department of Molecular Biology and Genetics

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

247 Citations (Scopus)

Abstract

The 2'-5' oligoadenylate synthetases (OAS) are interferon-induced antiviral enzymes that recognize virally produced dsRNA and initiate RNA destabilization through activation of RNase L within infected cells. However, recent evidence points toward several RNase L-independent pathways, through which members of the OAS family can exert antiviral activity. The crystal structure of OAS led to a novel insight into the catalytic mechanism, and revealed a remarkable similarity between OAS, Polyadenosine polymerase, and the class I CCA-adding enzyme from Archeoglobus fulgidus. This, combined with a variety of bioinformatic data, leads to the definition of a superfamily of template independent polymerases and proved that the OAS family are ancient proteins, which probably arose as early as the beginning of metazoan evolution.

Original language	English
Journal	Journal of Interferon & Cytokine Research
Volume	31
Issue	1
Pages (from-to)	41-47
Number of pages	7
ISSN	1079-9907
DOIs	https://doi.org/10.1089/jir.2010.0107
Publication status	Published - 12 Jan 2011

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title = "The oligoadenylate synthetase family: an ancient protein family with multiple antiviral activities",

abstract = "The 2'-5' oligoadenylate synthetases (OAS) are interferon-induced antiviral enzymes that recognize virally produced dsRNA and initiate RNA destabilization through activation of RNase L within infected cells. However, recent evidence points toward several RNase L-independent pathways, through which members of the OAS family can exert antiviral activity. The crystal structure of OAS led to a novel insight into the catalytic mechanism, and revealed a remarkable similarity between OAS, Polyadenosine polymerase, and the class I CCA-adding enzyme from Archeoglobus fulgidus. This, combined with a variety of bioinformatic data, leads to the definition of a superfamily of template independent polymerases and proved that the OAS family are ancient proteins, which probably arose as early as the beginning of metazoan evolution.",

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The oligoadenylate synthetase family: an ancient protein family with multiple antiviral activities. / Kristiansen, Helle; Gad, Hans Henrik; Larsen, Signe Eskildsen et al.
In: Journal of Interferon & Cytokine Research, Vol. 31, No. 1, 12.01.2011, p. 41-47.

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

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T1 - The oligoadenylate synthetase family: an ancient protein family with multiple antiviral activities

AU - Kristiansen, Helle

AU - Gad, Hans Henrik

AU - Larsen, Signe Eskildsen

AU - Despres, Philippe

AU - Hartmann, Rune

PY - 2011/1/12

Y1 - 2011/1/12

N2 - The 2'-5' oligoadenylate synthetases (OAS) are interferon-induced antiviral enzymes that recognize virally produced dsRNA and initiate RNA destabilization through activation of RNase L within infected cells. However, recent evidence points toward several RNase L-independent pathways, through which members of the OAS family can exert antiviral activity. The crystal structure of OAS led to a novel insight into the catalytic mechanism, and revealed a remarkable similarity between OAS, Polyadenosine polymerase, and the class I CCA-adding enzyme from Archeoglobus fulgidus. This, combined with a variety of bioinformatic data, leads to the definition of a superfamily of template independent polymerases and proved that the OAS family are ancient proteins, which probably arose as early as the beginning of metazoan evolution.

AB - The 2'-5' oligoadenylate synthetases (OAS) are interferon-induced antiviral enzymes that recognize virally produced dsRNA and initiate RNA destabilization through activation of RNase L within infected cells. However, recent evidence points toward several RNase L-independent pathways, through which members of the OAS family can exert antiviral activity. The crystal structure of OAS led to a novel insight into the catalytic mechanism, and revealed a remarkable similarity between OAS, Polyadenosine polymerase, and the class I CCA-adding enzyme from Archeoglobus fulgidus. This, combined with a variety of bioinformatic data, leads to the definition of a superfamily of template independent polymerases and proved that the OAS family are ancient proteins, which probably arose as early as the beginning of metazoan evolution.

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DO - 10.1089/jir.2010.0107

M3 - Journal article

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SN - 1079-9907

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JO - Journal of Interferon & Cytokine Research

JF - Journal of Interferon & Cytokine Research

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The oligoadenylate synthetase family: an ancient protein family with multiple antiviral activities

Abstract

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