Innate recognition of intracellular bacteria

Current Opinion in Immunology

Volumn 19, Issue 1, 2007, Pages 10-16

  Delbridge, Laura M ^a   O'Riordan, Mary XD ^a  

^a UNIVERSITY OF MICHIGAN MEDICAL SCHOOL   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL RNA; BACTERIAL TOXIN; CASPASE 9; CASPASE RECRUITMENT DOMAIN PROTEIN 15; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; INTERLEUKIN 1BETA CONVERTING ENZYME; LIGAND; NEURONAL APOPTOSIS INHIBITORY PROTEIN; NEURONAL APOPTOSIS INHIBITORY PROTEIN 5; PEPTIDOGLYCAN; TOLL LIKE RECEPTOR; UNCLASSIFIED DRUG;

BACTERIAL FLAGELLUM; BACTERIAL IMMUNITY; BACTERIAL INFECTION; BACTERIAL VIRULENCE; BACTERIUM; CELL SURFACE; CULTURE MEDIUM; CYTOSOL; ENDOSOME; ENZYME ACTIVATION; IMMUNOREGULATION; IMMUNOSENSOR; INFLAMMATION; INNATE IMMUNITY; LIGAND BINDING; MOLECULAR RECOGNITION; NONHUMAN; REVIEW; SIGNAL TRANSDUCTION;

ANIMALS; BACTERIA; HUMANS; IMMUNITY, NATURAL; INTRACELLULAR FLUID; LEGIONELLA PNEUMOPHILA; MYCOBACTERIUM TUBERCULOSIS; SALMONELLA TYPHIMURIUM;

EID: 33846136089     PISSN: 09527915     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.coi.2006.11.005     Document Type: Review

References (51)

1. Medzhitov R., and Janeway Jr. C.A. An ancient system of host defense. Curr Opin Immunol 10 (1998) 12-15
2. Kawai T., and Akira S. TLR signaling. Cell Death Differ 13 (2006) 816-825
3. O'Riordan M., and Portnoy D.A. The host cytosol: front-line or home front?. Trends Microbiol 10 (2002) 361-364
4. Pamer E.G. Immune responses to Listeria monocytogenes. Nat Rev Immunol 4 (2004) 812-823
5. Martinon F., and Tschopp J. NLRs join TLRs as innate sensors of pathogens. Trends Immunol 26 (2005) 447-454
6. Inohara, Chamaillard, McDonald C., and Nunez G. NOD-LRR proteins: role in host-microbial interactions and inflammatory disease. Annu Rev Biochem 74 (2005) 355-383
7. Inohara N., Ogura Y., Chen F.F., Muto A., and Nunez G. Human Nod1 confers responsiveness to bacterial lipopolysaccharides. J Biol Chem 276 (2001) 2551-2554
8. Kato H., Takeuchi O., Sato S., Yoneyama M., Yamamoto M., Matsui K., Uematsu S., Jung A., Kawai T., Ishii K.J., et al. Differential roles of MDA5 and RIG-I helicases in the recognition of RNA viruses. Nature 441 (2006) 101-105
9. Meylan E., Tschopp J., and Karin M. Intracellular pattern recognition receptors in the host response. Nature 442 (2006) 39-44
10. Akira S., Uematsu S., and Takeuchi O. Pathogen recognition and innate immunity. Cell 124 (2006) 783-801
11. Bonizzi G., and Karin M. The two NF-κB activation pathways and their role in innate and adaptive immunity. Trends Immunol 25 (2004) 280-288
12. Martinon F., Burns K., and Tschopp J. The inflammasome: a molecular platform triggering activation of inflammatory caspases and processing of proIL-β. Mol Cell 10 (2002) 417-426
13. •] demonstrated that IPAF is involved in sensing bacterial flagellin using Salmonella enterica as a model pathogen. Activation of IPAF triggered caspase-1 processing and IL1-β cleavage and secretion.
14. Matzinger P. The danger model: a renewed sense of self. Science 296 (2002) 301-305
15. Ogura Y., Inohara N., Benito A., Chen F.F., Yamaoka S., and Nunez G. Nod2, a Nod1/Apaf-1 family member that is restricted to monocytes and activates NF-κB. J Biol Chem 276 (2001) 4812-4818
16. Girardin S.E., Boneca I.G., Carneiro L.A., Antignac A., Jehanno M., Viala J., Tedin K., Taha M.K., Labigne A., Zahringer U., et al. Nod1 detects a unique muropeptide from Gram-negative bacterial peptidoglycan. Science 300 (2003) 1584-1587
17. Magalhaes J.G., Philpott D.J., Nahori M.A., Jehanno M., Fritz J., Bourhis L.L., Viala J., Hugot J.P., Giovannini M., Bertin J., et al. Murine Nod1 but not its human orthologue mediates innate immune detection of tracheal cytotoxin. EMBO Rep 6 (2005) 1201-1207. This study demonstrates that murine NOD1 is the sensor for tracheal cytotoxin - a peptidoglycan fragment derived from Bordetella pertussis. Murine NOD1 mediated innate immune responses to a DAP-containing tetrapeptide whereas human NOD1 sensed a DAP containing tripeptide, indicating host specificity in immune surveillance for bacterial peptidoglycan.
18. Girardin S.E., Boneca I.G., Viala J., Chamaillard M., Labigne A., Thomas G., Philpott D.J., and Sansonetti P.J. Nod2 is a general sensor of peptidoglycan through muramyl dipeptide (MDP) detection. J Biol Chem 278 (2003) 8869-8872
19. Girardin S.E., Jehanno M., Mengin-Lecreulx D., Sansonetti P.J., Alzari P.M., and Philpott D.J. Identification of the critical residues involved in peptidoglycan detection by Nod1. J Biol Chem 280 (2005) 38648-38656
20. Tanabe T., Chamaillard M., Ogura Y., Zhu L., Qiu S., Masumoto J., Ghosh P., Moran A., Predergast M.M., Tromp G., et al. Regulatory regions and critical residues of NOD2 involved in muramyl dipeptide recognition. EMBO J 23 (2004) 1587-1597
21. Hugot J.P., Chamaillard M., Zouali H., Lesage S., Cezard J.P., Belaiche J., Almer S., Tysk C., O'Morain C.A., Gassull M., et al. Association of NOD2 leucine-rich repeat variants with susceptibility to Crohn's disease. Nature 411 (2001) 599-603
22. Ogura Y., Bonen D.K., Inohara N., Nicolae D.L., Chen F.F., Ramos R., Britton H., Moran T., Karaliuskas R., Duerr R.H., et al. A frameshift mutation in NOD2 associated with susceptibility to Crohn's disease. Nature 411 (2001) 603-606
23. McGovern D.P., Hysi P., Ahmad T., van Heel D.A., Moffatt M.F., Carey A., Cookson W.O., and Jewell D.P. Association between a complex insertion/deletion polymorphism in NOD1 (CARD4) and susceptibility to inflammatory bowel disease. Hum Mol Genet 14 (2005) 1245-1250
24. Maeda S., Hsu L.C., Liu H., Bankston L.A., Iimura M., Kagnoff M.F., Eckmann L., and Karin M. Nod2 mutation in Crohn's disease potentiates NF-κB activity and IL-1β processing. Science 307 (2005) 734-738. Since the identification of mutations in NOD2 as a predisposing factor for Crohn's disease and inflammatory bowel disease, the role of NOD2 in the inflammatory process has been widely debated. This report describes the creation of a knock-in mouse carrying a Nod2 allele containing a mutation analogous to those found in some Crohn's disease patients. Using a chemically induced model of inflammatory bowel disease, these data show association of a gain-of-function NOD2 mutation with increased intestinal inflammation in an animal model.
25. Kobayashi K.S., Chamaillard M., Ogura Y., Henegariu O., Inohara N., Nunez G., and Flavell R.A. Nod2-dependent regulation of innate and adaptive immunity in the intestinal tract. Science 307 (2005) 731-734
26. Eckmann L., and Karin M. NOD2 and Crohn's disease: loss or gain of function?. Immunity 22 (2005) 661-667
27. Boyden E.D., and Dietrich W.F. Nalp1b controls mouse macrophage susceptibility to anthrax lethal toxin. Nat Genet 38 (2006) 240-244
28. Scobie H.M., and Young J.A. Interactions between anthrax toxin receptors and protective antigen. Curr Opin Microbiol 8 (2005) 106-112
29. Martinon F., Agostini L., Meylan E., and Tschopp J. Identification of bacterial muramyl dipeptide as activator of the NALP3/cryopyrin inflammasome. Curr Biol 14 (2004) 1929-1934
30. Kanneganti T.D., Ozoren N., Body-Malapel M., Am A., Park J.H., Franchi L., Whitfield J., Barchet W., Colonna M., Vandenabeele P., et al. Bacterial RNA and small antiviral compounds activate caspase-1 through cryopyrin/Nalp3. Nature 440 (2006) 233-236. This article provided evidence that the cytosolic sensor NALP3 distinguishes host RNA from microbial RNA. In addition, synergy between NALP3 and TLR4 in stimulating secretion of IL1-β and IL-18 was demonstrated, suggesting that extracellular and cytosolic innate immune sensors might act to amplify the production of common target genes or proteins.
31. Mariathasan S., Weiss D.S., Newton K., McBride J., O'Rourke K., Roose-Girma M., Lee W.P., Weinrauch Y., Monack D.M., and Dixit V.M. Cryopyrin activates the inflammasome in response to toxins and ATP. Nature 440 (2006) 228-232
32. Martinon F., Petrilli V., Mayor A., Tardivel A., and Tschopp J. Gout-associated uric acid crystals activate the NALP3 inflammasome. Nature 440 (2006) 237-241
33. Sutterwala F.S., Ogura Y., Szczepanik M., Lara-Tejero M., Lichtenberger G.S., Grant E.P., Bertin J., Coyle A.J., Galan J.E., Askenase P.W., et al. Critical role for NALP3/CIAS1/Cryopyrin in innate and adaptive immunity through its regulation of caspase-1. Immunity 24 (2006) 317-327
34. •] showed that Legionella pneumophila flagellin contaminating the host cytosol activated caspase-1 in a NAIP5-dependent manner. Flagellin-deficient Legionella were able to evade macrophage killing.
35. Wright E.K., Goodart S.A., Growney J.D., Hadinoto V., Endrizzi M.G., Long E.M., Sadigh K., Abney A.L., Bernstein-Hanley I., and Dietrich W.F. Naip5 affects host susceptibility to the intracellular pathogen Legionella pneumophila. Curr Biol 13 (2003) 27-36
36. Diez E., Lee S.H., Gauthier S., Yaraghi Z., Tremblay M., Vidal S., and Gros P. Birc1e is the gene within the Lgn1 locus associated with resistance to Legionella pneumophila. Nat Genet 33 (2003) 55-60
37. •].
38. •].
39. •].
40. Sato S., and Nieminen J. Seeing strangers or announcing "danger": galectin-3 in two models of innate immunity. Glycoconj J 19 (2004) 583-591
41. Brown G.D., and Gordon S. Immune recognition. A new receptor for beta-glucans. Nature 413 (2001) 36-37
42. O'Riordan M., Yi C.H., Gonzales R., Lee K.D., and Portnoy D.A. Innate recognition of bacteria by a macrophage cytosolic surveillance pathway. Proc Natl Acad Sci USA 99 (2002) 13861-13866
43. Stetson D.B., and Medzhitov R. Recognition of cytosolic DNA activates an IRF3-dependent innate immune response. Immunity 24 (2006) 93-103. This study identifies bacterial DNA as a microbial ligand recognized in the host cytosol. Bacterial DNA delivered to the inside of host cells triggered expression of Type I interferons, whereas mammalian DNA delivered similarly did not.
44. Mariathasan S., Weiss D.S., Dixit V.M., and Monack D.M. Innate immunity against Francisella tularensis is dependent on the ASC/caspase-1 axis. J Exp Med 202 (2005) 1043-1049
45. Perrin A.J., Jiang X., Birmingham C.L., So N.S., and Brumell J.H. Recognition of bacteria in the cytosol of Mammalian cells by the ubiquitin system. Curr Biol 14 (2004) 806-811
46. Deretic V. Autophagy in innate and adaptive immunity. Trends Immunol 26 (2005) 523-528
47. Nakagawa I., Amano A., Mizushima N., Yamamoto A., Yamaguchi H., Kamimoto T., Nara A., Funao J., Nakata M., Tsuda K., et al. Autophagy defends cells against invading group A Streptococcus. Science 306 (2004) 1037-1040
48. Singh S.B., Davis A.S., Taylor G.A., and Deretic V. Human IRGM induces autophagy to eliminate intracellular mycobacteria. Science 313 (2006) 1438-1441
49. Birmingham C.L., Smith A.C., Bakowski M.A., Yoshimori T., and Brumell J.H. Autophagy controls Salmonella infection in response to damage to the Salmonella-containing vacuole. J Biol Chem 281 (2006) 11374-11383
50. Deretic V., Singh S., Master S., Harris J., Roberts E., Kyei G., Davis A., de Haro S., Naylor J., Lee H.H., et al. Mycobacterium tuberculosis inhibition of phagolysosome biogenesis and autophagy as a host defence mechanism. Cell Microbiol 8 (2006) 719-727
51. Lara-Tejero M., Sutterwala F.S., Ogura Y., Grant E.P., Bertin J., Coyle A.J., Flavell R.A., and Galan J.E. Role of the caspase-1 inflammasome in Salmonella typhimurium pathogenesis. J Exp Med 203 (2006) 1407-1412. Although many studies have focused on the molecular events triggered by the presence of bacterial products in the cytosol, the physiological roles of many cytosolic sensing proteins in antibacterial immunity remains unknown. This study tests the requirement for IPAF and other components of the inflammasome in a murine model of Salmonella infection. Although other studies had identified IPAF as a cytosolic sensor for Salmonella flagellin, these data show that IPAF is not necessary for an effective immune response against Salmonella in vivo.