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J Interferon Cytokine Res. 2011 Jan;31(1):41-7. doi: 10.1089/jir.2010.0107. Epub 2010 Dec 12.

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

Author information

1
Centre for Structural Biology, Department of Molecular Biology, Aarhus University, Aarhus, Denmark.

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.

PMID:
21142819
DOI:
10.1089/jir.2010.0107
[Indexed for MEDLINE]

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