BETA ZEN
OASL
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| Aliases | OASL, OASLd, TRIP-14, TRIP14, p59 p59-p592'-5'-oligoadenylate synthetase like, OASL1 | |||||||||||||||||||||||||||||||||||||||||||||||||||||
| External IDs | OMIM: 603281; MGI: 2180849; GeneCards: OASL | |||||||||||||||||||||||||||||||||||||||||||||||||||||
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59 kDa 2'-5'-oligoadenylate synthetase-like protein is an enzyme that in humans is encoded by the OASL gene.[5][6] It enhances antiviral innate immunity by acting as a RIG-I signaling amplifier.
2'-5'-oligoadenylate synthase is a protein family of structurally similar proteins, including OAS1, OAS2, and OAS3. However, mutations in the OAS domain mean it lacks the motif to allow oligomerization, preventing the synthesis of oligoadenylates. OASL, like the proteins of 2'-5'-oligoadenylate synthase family, is induced by interferons.
Function
RNA virus infection
In RNA virus infection, viral genetic material binds to the RNA sensor RIG-I, triggering a reaction cascade that culminates in the secretion of type I interferons.[7] OASL acts as a sensitiser of RIG-I, binding to the caspase activation and recruitment domain and enhancing interferon production.[8]
DNA virus infection
While OASL has an anti-viral role in RNA viral infection, it has also demonstrated a pro-viral role in DNA viral infection.[9] OASL can bind to the viral DNA sensor cGAS, inhibiting its catalytic activity and preventing the secretion of interferons.[10]
Intracellular bacterial infection
OASL is shown to be upregulated during a wide variety of vacuolar and cytosolic bacterial infections.[11] It possesses an ability to inhibit autophagic mechanisms and antimicrobial peptide secretion within the host cell through unclear mechanisms, preventing clearance of the pathogen and creating a favourable intracellular environment.[12]
See also
References
- 1 2 3 GRCh38: Ensembl release 89: ENSG00000135114 – Ensembl, May 2017
- 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000041827 – Ensembl, May 2017
- ↑ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- ↑ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- ↑ Hovnanian A, Rebouillat D, Levy ER, Mattei MG, Hovanessian AG (May 1999). "The human 2',5'-oligoadenylate synthetase-like gene (OASL) encoding the interferon-induced 56-kDa protein maps to chromosome 12q24.2 in the proximity of the 2',5'-OAS locus". Genomics. 56 (3): 362–363. doi:10.1006/geno.1998.5737. PMID 10087211.
- ↑ "Entrez Gene: OASL 2'-5'-oligoadenylate synthetase-like".
- ↑ Kell AM, Gale M (May 2015). "RIG-I in RNA virus recognition". Virology. 479–480: 110–121. doi:10.1016/j.virol.2015.02.017. PMC 4424084. PMID 25749629.
- ↑ Zhu J, Zhang Y, Ghosh A, Cuevas RA, Forero A, Dhar J, et al. (June 2014). "Antiviral activity of human OASL protein is mediated by enhancing signaling of the RIG-I RNA sensor". Immunity. 40 (6): 936–948. doi:10.1016/j.immuni.2014.05.007. PMC 4101812. PMID 24931123.
- ↑ Choi UY, Kang JS, Hwang YS, Kim YJ (March 2015). "Oligoadenylate synthase-like (OASL) proteins: dual functions and associations with diseases". Experimental & Molecular Medicine. 47 (3): e144. doi:10.1038/emm.2014.110. PMC 4351405. PMID 25744296.
- ↑ Rex V, Stempel M, Halle S, Brinkmann MM (June 2023). "The two faces of oligoadenylate synthetase-like: effective antiviral protein and negative regulator of innate immunity". Current Opinion in Virology. 60 101329. doi:10.1016/j.coviro.2023.101329. PMID 37079941.
- ↑ Leisching G, Wiid I, Baker B (2017). "The Association of OASL and Type I Interferons in the Pathogenesis and Survival of Intracellular Replicating Bacterial Species". Frontiers in Cellular and Infection Microbiology. 7 196. doi:10.3389/fcimb.2017.00196. PMC 5437694. PMID 28580319.
- ↑ de Toledo-Pinto TG, Ferreira AB, Ribeiro-Alves M, Rodrigues LS, Batista-Silva LR, Silva BJ, et al. (July 2016). "STING-Dependent 2'-5' Oligoadenylate Synthetase-Like Production Is Required for Intracellular Mycobacterium leprae Survival". The Journal of Infectious Diseases. 214 (2): 311–320. doi:10.1093/infdis/jiw144. PMID 27190175.[dead link]
Further reading
- Mackay V, Linn S (1976). "Selective inhibition of the dnase activity of the recBC enzyme by the DNA binding protein from Escherichia coli". The Journal of Biological Chemistry. 251 (12): 3716–3719. doi:10.1016/S0021-9258(17)33402-6. PMID 776974.
- Lee JW, Choi HS, Gyuris J, Brent R, Moore DD (February 1995). "Two classes of proteins dependent on either the presence or absence of thyroid hormone for interaction with the thyroid hormone receptor". Molecular Endocrinology. 9 (2). Baltimore, Md.: 243–254. doi:10.1210/mend.9.2.7776974. PMID 7776974.
- Hartmann R, Olsen HS, Widder S, Jorgensen R, Justesen J (September 1998). "p59OASL, a 2'-5' oligoadenylate synthetase like protein: a novel human gene related to the 2'-5' oligoadenylate synthetase family". Nucleic Acids Research. 26 (18): 4121–4128. doi:10.1093/nar/26.18.4121. PMC 147837. PMID 9722630.
- Rebouillat D, Marié I, Hovanessian AG (1998). "Molecular cloning and characterization of two related and interferon-induced 56-kDa and 30-kDa proteins highly similar to 2'-5' oligoadenylate synthetase". European Journal of Biochemistry. 257 (2): 319–330. doi:10.1046/j.1432-1327.1998.2570319.x. PMID 9826176.
- Andersen JB, Strandbygård DJ, Hartmann R, Justesen J (2004). "Interaction between the 2'-5' oligoadenylate synthetase-like protein p59 OASL and the transcriptional repressor methyl CpG-binding protein 1". European Journal of Biochemistry. 271 (3): 628–636. doi:10.1046/j.1432-1033.2003.03966.x. PMID 14728690.
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