2'-5'-Oligoadenylate synthetase 2 (OAS2)

2'-5'-Oligoadenylate synthetase 2 (OAS2) is an interferon-induced enzyme and a member of the 2-5A synthetase family, playing a critical role in the innate immune response to viral infection[2]. OAS2 is activated upon binding to double-stranded RNA, which is often generated during viral replication. Upon activation, OAS2 catalyzes the conversion of ATP into 2'-5'-linked oligoadenylates, which subsequently activate latent RNase L. Activated RNase L degrades both viral and cellular RNA, thereby inhibiting protein synthesis and terminating viral replication[2][1]. OAS2 exists as a dimer, with one catalytically active and one inactive domain, enabling discrimination of RNA length to prevent autoreactivity to short RNAs[1]. Mutations in OAS2 have been linked to autoimmune diseases, and the protein may also modulate cellular processes such as apoptosis, cell growth, and differentiation[2]. There are no current specific drugs known to directly target OAS2, but its pathway is essential in the interferon-mediated antiviral response.

Other names

2'-5'-oligoadenylate synthase 2(2-5')oligo(A) synthase 22-5A synthase 2p69OASp71OASp69 OASp71 OAS(2'-5')oligo(A) synthetase 22'-5'-oligoadenylate synthetase 269/71kDaOAS2 protein, human

Activation of RNase L via synthesis of 2'-5'-oligoadenylates from ATP upon double-stranded RNA detection, leading to viral and cellular RNA degradation and inhibition of viral replication