The Association of OASL and Type I Interferons in the Pathogenesis and Survival of Intracellular Replicating Bacterial Species

Frontiers in Cellular and Infection Microbiology

Volumn 7, Issue MAY, 2017, Pages

  Leisching, Gina ^a   Wiid, Ian ^a   Baker, Bienyameen ^a  

^a UNIVERSITY OF STELLENBOSCH   (South Africa)

Author keywords

CGAS; Mycobacteria; OAS; OASL; Pathogenesis; STING; Type I IFN

Indexed keywords

2',5' OLIGOADENYLATE SYNTHETASE; CASPASE RECRUITMENT DOMAIN PROTEIN 15; CATHEPSIN E; CYCLIC AMP; CYCLIC GMP; EXTRACHROMOSOMAL DNA; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; INTERFERON; INTERFERON INDUCED HELICASE C DOMAIN CONTAINING PROTEIN 1; INTERFERON REGULATORY FACTOR 3; LIPOPOLYSACCHARIDE; LIPOPROTEIN; NUCLEOTIDE BINDING OLIGOMERIZATION DOMAIN LIKE RECEPTOR; PATTERN RECOGNITION RECEPTOR; POLYPEPTIDE ANTIBIOTIC AGENT; RETINOIC ACID INDUCIBLE PROTEIN I; RIBONUCLEASE L; MB21D1 PROTEIN, HUMAN; NUCLEOTIDYLTRANSFERASE; OASL PROTEIN, HUMAN;

ANTIVIRAL ACTIVITY; BACTERIAL GENE; BACTERIAL INFECTION; BACTERIAL SURVIVAL; BRUCELLA ABORTUS; CHLAMYDIA PNEUMONIAE; CHLAMYDIA TRACHOMATIS; DNA VIRUS; INTRACELLULAR BACTERIUM; LACTOBACILLUS ACIDOPHILUS; LISTERIA MONOCYTOGENES; MEMBRANE FUSION; MYCOBACTERIUM LEPRAE; MYCOBACTERIUM TUBERCULOSIS; NONHUMAN; PATHOGENESIS; PROTEIN EXPRESSION; RNA VIRUS; SHORT SURVEY; SIGNAL TRANSDUCTION; VACCINIA VIRUS; VIRUS INFECTION; AUTOPHAGY; BACTERIUM; CELL VACUOLE; CLASSIFICATION; CYTOPLASM; CYTOSOL; GENE EXPRESSION REGULATION; GENETICS; GROWTH, DEVELOPMENT AND AGING; HOST PATHOGEN INTERACTION; HUMAN; IMMUNOLOGY; INNATE IMMUNITY; MICROBIOLOGY; MYCOBACTERIUM; PATHOGENICITY; PHYSIOLOGY;

2',5'-OLIGOADENYLATE SYNTHETASE; AUTOPHAGY; BACTERIA; CYTOPLASM; CYTOSOL; GENE EXPRESSION REGULATION; HOST-PATHOGEN INTERACTIONS; HUMANS; IMMUNITY, INNATE; INTERFERON TYPE I; MYCOBACTERIUM; NUCLEOTIDYLTRANSFERASES; SIGNAL TRANSDUCTION; VACUOLES; VIRUS DISEASES;

EID: 85027461440     PISSN: None     EISSN: 22352988     Source Type: Journal    
DOI: 10.3389/fcimb.2017.00196     Document Type: Short Survey

References (39)

1. Akira, S., Uematsu, S., and Takeuchi, O. (2006). Pathogen recognition and innate immunity. Cell 124, 783–801. doi: 10.1016/j.cell.2006.02.015
2. Chen, Q., Sun, L., and Chen, Z. J. (2016). Regulation and function of the cGAS-STING pathway of cytosolic DNA sensing. Nat. Immunol. 17, 1142–1149. doi: 10.1038/ni.3558
3. Chiu, Y.-H., MacMillan, J. B., and Chen, Z. J. (2009). RNA polymerase III detects cytosolic DNA and induces type I interferons through the RIG-I pathway. Cell 138, 576–591. doi: 10.1016/j.cell.2009.06.015
4. Choi, U. Y., Kang, J.-S., Hwang, Y. S., and Kim, Y.-J. (2015). Oligoadenylate synthase-like (OASL) proteins: dual functions and associations with diseases. Exp. Mol. Med. 47, e144. doi: 10.1038/emm.2014.110
5. ′ oligoadenylate synthetase-like production is required for intracellular mycobacterium leprae survival. J. Infect. Dis. 214, 311–320. doi: 10.1093/infdis/jiw144
6. ′ -oligoadenylate synthetase type 2 and enhances RNase-L function in THP-1 cells. Mol. Immunol. 47, 560–566. doi: 10.1016/j.molimm.2009.09.025
7. Eickhoff, M., Thalmann, J., Hess, S., Martin, M., Laue, T., Kruppa, J., et al. (2007). Host cell responses to Chlamydia pneumoniae in gamma interferoninduced persistence overlap those of productive infection and are linked to genes involved in apoptosis, cell cycle, and metabolism. Infect. Immun. 75, 2853–2863. doi: 10.1128/IAI.01045-06
8. Eskildsen, S., Justesen, J., Schierup, M. H., and Hartmann, R. (2003). Characterization of the 2′ –5′ -oligoadenylate synthetase ubiquitin-like family. Nucleic Acids Res. 31, 3166–3173. doi: 10.1093/nar/gkg427
9. ′ Oligoadenylate Synthetase -like (OASL) proteins during DNA virus infection. J. Immunol. 196(Suppl. 1), 61.6.
10. Girardin, S. E., Boneca, I. G., Viala, J., Chamaillard, M., Labigne, A., and Sansonetti, P. J. (2003). Nod2 is a general sensor of peptidoglycan through muramyl dipeptide (MDP) detection. J. Biol. Chem. 278, 8869–8872. doi: 10.1074/jbc.C200651200
11. Gordon, S. (2002). Pattern recognition receptors: doubling up for the innate immune response. Cell 111, 927–930. doi: 10.1016/S0092-8674(02) 01201-1
12. Hasegawa, M., Yang, K., Hashimoto, M., Park, J.-H., Kim, Y.-G., Fujimoto, Y., et al. (2006). Differential release and distribution of Nod1 and Nod2 immunostimulatory molecules among bacterial species and environments. J. Biol. Chem. 281, 29054–29063. doi: 10.1074/jbc.M6026 38200
13. Henry, T., and Monack, D.M. (2007). Activation of the inflammasome upon Francisella tularensis infection: interplay of innate immune pathways and virulence factors. Cell. Microbiol. 9, 2543–2551. doi: 10.1111/j.1462-5822.2007.01022.x
14. Holm, C. K., Jensen, S. B., Jakobsen, M. R., Cheshenko, N., Horan, K. A., and Yarovinsky, T.O. (2012). Virus-cell fusion as a trigger of innate immunity dependent on the adaptor STING. Nat. Immunol. 13, 737–743. doi: 10.1038/ni.2350
15. Ishikawa, H., Ma, Z., and Barber, G. N. (2009). STING regulates intracellular DNAmediated, type I interferon-dependent innate immunity. Nature 461, 788–792. doi: 10.1038/nature08476
16. Jo, E.-K. (2008). Mycobacterial interaction with innate receptors: TLRs, C-type lectins, and NLRs. Curr. Opin. Infect. Dis. 21, 279–286. doi: 10.1097/QCO.0b013e3282f88b5d
17. Kawai, T., and Akira, S. (2010). The role of pattern-recognition receptors in innate immunity: update on Toll-like receptors. Nat. Immunol. 11, 373–384. doi: 10.1038/ni.1863
18. Kutsch, S., Degrandi, D., and Pfeffer, K. (2008). Immediate lymphotoxin β receptor-mediated transcriptional response in host defense against L. monocytogenes. Immunobiology 213, 353–366. doi: 10.1016/j.imbio.2007. 10.011
19. Lad, S. P., Fukuda, E. Y., Li, J., Luis, M., and Li, E. (2005). Up-regulation of the JAK/STAT1 signal pathway during Chlamydia trachomatis infection. J. Immunol. 174, 7186–7193. doi: 10.4049/jimmunol.174. 11.7186
20. Leisching, G., Pietersen, R.-D., van Heerden, C., van Helden, P., Wiid, I., and Baker, B. (2016). RNAseq reveals hypervirulence-specific host responses to M. tuberculosis infection. Virulence. doi: 10.1080/21505594.2016.1250994. [Epub ahead of print].
21. Li, Y., Banerjee, S., Wang, Y., Goldstein, S. A., Dong, B., and Weiss, S. R. (2016). Activation of RNase L is dependent on OAS3 expression during infection with diverse human viruses. Proc. Natl. Acad. Sci. U.S.A. 113, 2241–2246. doi: 10.1073/pnas.1519657113
22. Manzanillo, P. S., Shiloh, M. U., Portnoy, D. A., and Cox, J. S. (2012). Mycobacterium tuberculosis activates the DNA-dependent cytosolic surveillance pathway within macrophages. Cell Host Microbe 11, 469–480. doi: 10.1016/j.chom.2012.03.007
23. Melchjorsen, J., Kristiansen, H., Christiansen, R., Rintahaka, J., Matikainen, S., Paludan, S., et al. (2009). Differential regulation of the OASL and OAS1 genes in response to viral infections. J. Interferon Cytokine Res. 29, 199–208. doi: 10.1089/jir.2008.0050
24. Meylan, E., Tschopp, J., and Karin, M. (2006). Intracellular pattern recognition receptors in the host response. Nature 442, 39–44. doi: 10.1038/nature 04946
25. Patrick, K. L., Bell, S. L., and Watson, R. O. (2016). For better or worse: cytosolic DNA sensing during intracellular bacterial infection induces potent innate immune responses. J. Mol. Biol. 428, 3372–3386 doi: 10.1016/j.jmb.2016. 04.030
26. Roux, C. M., Rolán, H. G., Santos, R. L., Beremand, P. D., Thomas, T. L., and Tsolis, R. M. (2007). Brucella requires a functional Type IV secretion system to elicit innate immune responses in mice. Cell. Microbiol. 9, 1851–1869. doi: 10.1111/j.1462-5822.2007.00922.x
27. Shaw, M. H., Reimer, T., Kim, Y.-G., and Nuñez, G. (2008). NOD-like receptors (NLRs): bona fide intracellular microbial sensors. Curr. Opin. Immunol. 20, 377–382. doi: 10.1016/j.coi.2008.06.001
28. ′ -oligoadenylate synthetase and RNase L during the interferon antiviral response. J. Virol. 81, 12720–12729. doi: 10.1128/JVI.01471-07
29. Stanley, S. A., Johndrow, J. E., Manzanillo, P., and Cox, J. S. (2007). The type I IFN response to infection with Mycobacterium tuberculosis requires ESX-1-mediated secretion and contributes to pathogenesis. J. Immunol. 178, 3143–3152. doi: 10.4049/jimmunol.178.5.3143
30. Sun, L., Wu, J., Du, F., Chen, X., and Chen, Z. J. (2013). Cyclic GMP-AMP synthase is a cytosolic DNA sensor that activates the type I interferon pathway. Science 339, 786–791. doi: 10.1126/science.1232458
31. ′ -linked oligoadenylates by human ribonuclease L. EMBO J. 23, 3929–3938. doi: 10.1038/sj.emboj. 7600420
32. Tsukuba, T., Yanagawa, M., Kadowaki, T., Takii, R., Okamoto, Y., Sakai, E., et al. (2013). Cathepsin E deficiency impairs autophagic proteolysis in macrophages. PLoS ONE 8:e82415. doi: 10.1371/journal.pone.0082415
33. Uematsu, S., and Akira, S. (2006). Toll-like receptors and innate immunity. J. Mol. Med. 84, 712–725. doi: 10.1007/s00109-00 6-0084-y
34. Vance, R. E., Isberg, R. R., and Portnoy, D. A. (2009). Patterns of pathogenesis: discrimination of pathogenic and nonpathogenic microbes by the innate immune system. Cell Host Microbe 6, 10–21. doi: 10.1016/j.chom.2009. 06.007
35. Weiss, G., Rasmussen, S., Zeuthen, L. H., Nielsen, B. N., Jarmer, H., and FrøkiÃęr, H. (2010). Lactobacillus acidophilus induces virus immune defence genes in murine dendritic cells by a Toll-like receptor-2-dependent mechanism. Immunology 131, 268–281. doi: 10.1111/j.1365-2567.2010. 03301.x
36. Yoneyama, M., Kikuchi, M., Natsukawa, T., Shinobu, N., Imaizumi, T., Miyagishi, M., et al. (2004). The RNA helicase RIG-I has an essential function in doublestranded RNA-induced innate antiviral responses. Nat. Immunol. 5, 730–737. doi: 10.1038/ni1087
37. ′ -oligoadenylate-dependent RNase L. EMBO J. 16, 6355–6363. doi: 10.1093/emboj/16.21.6355
38. Zhu, J., Ghosh, A., and Sarkar, S. N. (2015). OASL—a new player in controlling antiviral innate immunity. Curr. Opin. Virol. 12, 15–19. doi: 10.1016/j.coviro.2015.01.010
39. Zhu, J., Zhang, Y., Ghosh, A., Cuevas, R. A., Forero, A., and Ganapathiraju, M. K. (2014). Antiviral activity of human OASL protein is mediated by enhancing signaling of the RIG-I RNA sensor. Immunity 40, 936–948. doi: 10.1016/j.immuni.2014.05.007