OASL

Official Full Name

2'-5'-oligoadenylate synthetase like

Organism

Homo sapiens

GeneID

8638

Background

Enables DNA binding activity and double-stranded RNA binding activity. Involved in several processes, including interleukin-27-mediated signaling pathway; negative regulation of viral genome replication; and positive regulation of RIG-I signaling pathway. Located in cytosol; nucleolus; and nucleoplasm. [provided by Alliance of Genome Resources, Feb 2025]

Synonyms

OASL1; OASLd; TRIP14; TRIP-14; p59OASL; p59 OASL; p59-OASL;

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Detailed Information

To counter virus infection, the immune system produces antiviral cytokines. Interferon (IFN) is the most powerful antiviral cytokine. It induces IFN-stimulated genes which mediate antiviral effector functions. Among the proteins induced by IFN, oligoadenylate synthase (OAS) proteins have been identified as enzymes which sense exogenous nucleic acid and initiate antiviral pathways. The OAS family proteins contain OAS1, OAS2, OAS3 and OAS-like protein (OASL). OASL consists of one OAS domain, two ubiquitin-like repeats and a CCY motif instead of CFK in the OAS unit that is required for oligomerization. Thus the human OASL (hOASL) lacks the 2’-5’- linked OAS activity that is one of the hallmarks of OAS. And the expression of OASL is also regulated differently from OAS.

OASL and antiviral innate immunity

The role of OASL was identified later than that of OAS. However, the recently identified functions seem to be critical to the antiviral innate and adaptive immune responses. These make further studies of OASL valuable. Because of its inactive nucleotidyltransferase domain and OAS-like qualities (activation by IFN and binding to dsRNA), OASL has been assumed to interfere with the 2-5A and RNase L pathway by competing with OAS. An SNP study of the response to IFN therapy for chronic hepatitis C suggested that OASL could negatively regulate the antiviral function of OAS. An SNP that cause lower levels of OASL was observed to be associated with a sustained virological response after treatment. Nevertheless, it has been demonstrated that hOASL possesses antiviral activity through the C-terminal ubiquitin-like domain. In Vero cells, hOASL expression increases the resistance against single-stranded RNA viruses, including encephalomyocarditis and picornavirus, but not against a DNA virus, herpes simplex virus 1. Studies have shown that human OASL promotes antiviral activity by enhancing the sensitivity of RIG-I activation. From a number of biochemical and structural studies, a model for RIG-I activation has been proposed where RIG-I adopts a stable auto-inhibited conformation in the absence of RNA (Figure 1).

Figure 1. A schematic model of OASL-mediated enhancement of RIG-I signaling. (Choi U Y, et al., 2015)

SNPs in OASL-associated diseases

Several SNPs in the OAS family genes have been identified and associated with many diseases. Consistent with the main role of OAS proteins, SNPs in OAS genes affect the susceptibility to viral infection. Genetic factors, environmental conditions and age may have important roles in disease progression. Sequencing the OAS family exons in 33 patients with West Nile Virus (WNV) infection showed that a SNP (rs3213545) of the OASL gene is associated with WNV infection. Although the rs3213545 SNP is synonymous in OASL exon2, it contains a splice enhancer site that is a minor allele ‘T’, which generates a dominant-negative mutant form of OASL. The rs3213545 SNP is significantly associated with a sustained virological response, an efficacy measure of hepatitis C virus treatment after IFN therapy; that is, diminished OASL activity confers an advantage for IFN treatment.

The role of OASL in diseases other than immune-related diseases is demonstrated by genome-wide association studies. The locus of the OASL gene on chromosome 12 was shown to affect multiple cardiovascular-related traits, especially ‘high or low’ gamma glutamyltransferase, C-reactive protein and low-density lipoprotein. The study identified the rs3213545 SNP as a possible candidate associated with liver function and lipid constitution.

References:

Choi U Y, et al. Oligoadenylate synthase-like (OASL) proteins: dual functions and associations with diseases. Experimental & Molecular Medicine, 2015, 47(3):e144.
Zhu J, et al. OASL-a new player in controlling antiviral innate immunity. Current Opinion in Virology, 2015, 12:15.
Middelberg R P, et al. Genetic variants in LPL, OASL and TOMM40/APOE-C1-C2-C4 genes are associated with multiple cardiovascular-related traits. BMC Medical Genetics, 2011, 12(1):123.
O'Neill L A, Bowie A G. The powerstroke and camshaft of the RIG-I antiviral RNA detection machine. Cell, 2011, 147(2):259-261.

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