Cancer Virology Program, UPMC Hillman Cancer Center, University of Pittsburgh School of Medicine, Pittsburgh, Pennsylvania, USA.
Department of Microbiology and Molecular Genetics, University of Pittsburgh School of Medicine, Pittsburgh, Pennsylvania, USA.
J Interferon Cytokine Res. 2023 Nov;43(11):487-494. doi: 10.1089/jir.2023.0098. Epub 2023 Sep 25.
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.
2'-5'寡聚腺苷酸合成酶(OAS)是干扰素刺激的基因,它们最著名的功能是保护宿主免受病毒感染。它们与古老的核苷酸转移酶家族在进化上相关,该家族主要参与病原体感应和先天免疫反应。OAS 蛋白的经典功能涉及双链 RNA 刺激的三磷酸腺苷在 2'-5'寡腺苷酸(2-5A)中的聚合,这可以激活潜伏的核糖核酸酶(RNase L)来降解 RNA。然而,多年来积累的证据表明,几种 OAS 家族蛋白具有抗病毒作用的替代模式。此外,最近的研究将一些 OAS 蛋白与病毒感染以外的更广泛功能联系起来。在这里,我们回顾了 OAS 蛋白的一些典型和非典型功能及其机制。