Key result
Oligoadenylate synthetases (OAS) are interferon-stimulated genes with both canonical antiviral functions via RNase L activation and noncanonical functions beyond viral infection.
Why the study?
Recent evidence suggests alternative antiviral mechanisms and wider functions beyond viral infection for several 2'-5' oligoadenylate synthetase family proteins.
This review highlights the diverse canonical and noncanonical functions of OAS proteins in innate immunity and beyond.
2'-5' Oligoadenylate synthetases (OAS) are interferon-stimulated genes that are most well-known to protect hosts from viral infections. They are evolutionarily related to an ancient family of Nucleotidyltransferases, which are primarily involved in pathogen-sensing and innate immune response. Classical function of OAS proteins involves double-stranded RNA-stimulated polymerization of adenosine triphosphate in 2'-5' oligoadenylates (2-5A), which can activate the latent RNase (RNase L) to degrade RNA. However, accumulated evidence over the years have suggested alternative mode of antiviral function of several OAS family proteins. Furthermore, recent studies have connected some OAS proteins with wider function beyond viral infection. Here, we review some of the canonical and noncanonical functions of OAS proteins and their mechanisms.
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Sarkar et al. (2023) conducted a review in Viral infections. Oligoadenylate synthetases (OAS) was evaluated. Oligoadenylate synthetases (OAS) are interferon-stimulated genes with both canonical antiviral functions via RNase L activation and noncanonical functions beyond viral infection.
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