OASL

OASL
Identifiers
AliasesOASL, OASLd, TRIP-14, TRIP14, p59 p59-p592'-5'-oligoadenylate synthetase like, OASL1
External IDsOMIM: 603281; MGI: 2180849; GeneCards: OASL
Available structures
PDBOrtholog search: PDBe RCSB
Orthologs
DatabasesNCBI: entry; OMA: entry
SpeciesHumanMouse
Entrez

8638

231655

Ensembl

ENSG00000135114

ENSMUSG00000041827

UniProt

Q15646

Q8VI94

RefSeq (mRNA)

NM_198213
NM_001261825
NM_003733
NM_001395418
NM_001395419

NM_145209
NM_001359945
NM_001359946

RefSeq (protein)

NP_001248754
NP_003724
NP_937856

NP_660210
NP_001346874
NP_001346875

Location (UCSC)Chr 12: 121.02 – 121.04 MbChr 5: 115.06 – 115.08 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

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. ^ a b c GRCh38: Ensembl release 89: ENSG00000135114 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000041827 – Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ 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.
  6. ^ "Entrez Gene: OASL 2'-5'-oligoadenylate synthetase-like".
  7. ^ 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.
  8. ^ 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.
  9. ^ 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.
  10. ^ 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.
  11. ^ 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.
  12. ^ 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

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