Disease relevance of OAS2

• Biochemical analyses using recombinant proteins produced in Escherichia coli showed that all the novel mouse 2-5OAS molecules have double-stranded RNA (dsRNA) binding ability, but they do not have 2-5OAS activity except for the OAS2 and OAS3 mouse homologs [1].

High impact information on OAS2

• Only one gene, OAS2, was differentially expressed by these cell lines, and this was confirmed by quantitative PCR [2].
• OAS1 is the small form and OAS2 is the medium form of the human interferon-induced 2'-5' oligoadenylate synthetases [3].
• DON also impaired induction of two type 1 IFN-dependent antiviral genes, double-stranded RNA activated protein kinase R (PKR) and oligoadenylate synthase 2 (OAS2) [4].
• We characterize the anti-viral responses of synthetic siRNA and in vitro-transcribed siRNA by measuring the mRNA levels of IFN-beta and OAS2 in HeLa cells [5].
• In mice, however, OAS genes corresponding to human OAS2 and OAS3 have not been identified [1].

Biological context of OAS2

• By in situ hybridization, we assign the human OAS-40/46, OAS-69/71, and OAS-100 genes (referred to as OAS1, OAS2, and OAS3, respectively) to a unique cytogenetic location on chromosomal region 12q24 [6].
• BACKGROUND: The 2',5'-oligoadenylate synthetase genes (OAS1, OAS2, and OAS3) map to human chromosome 12q24 and encode a family of enzymes pivotal to innate antiviral defence [7].

References