Detection of peptidoglycans by NOD proteins

Trends in Cell Biology

Volumn 13, Issue 12, 2003, Pages 610-614

  Royet, Julien ^a   Reichhart, Jean Marc ^a  

^a INSTITUT DE BIOLOGIE MOLÉCULAIRE ET CELLULAIRE   (France)

Author keywords

[No Author keywords available]

Indexed keywords

DIAMINOPIMELIC ACID; NEUROPEPTIDE; NUCLEOTIDE BINDING OLIGOMERIZATION DOMAIN 1; NUCLEOTIDE BINDING PROTEIN; PEPTIDOGLYCAN; UNCLASSIFIED DRUG;

BACTERIAL CELL; GRAM NEGATIVE BACTERIUM; IMMUNITY; INVERTEBRATE; MOLECULAR RECOGNITION; NONHUMAN; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN EXPRESSION; PROTEIN MOTIF; RECEPTOR BINDING; REVIEW; SIGNAL TRANSDUCTION;

BACTERIA (MICROORGANISMS); INVERTEBRATA; NEGIBACTERIA;

EID: 0242643726     PISSN: 09628924     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.tcb.2003.10.003     Document Type: Short Survey

References (24)

1. Hoffmann J.A., et al. Phylogenetic perspectives in innate immunity. Science. 284:1999;1313-1318.
2. Takeda K., et al. Toll-like receptors. Annu. Rev. Immunol. 21:2003;335-376.
3. Inohara N., Nunez G. NODs: intracellular proteins involved in inflammation and apoptosis. Nat. Rev. Immunol. 3:2003;371-382.
4. Aballay A., Ausubel F.M. Programmed cell death mediated by ced-3 and ced-4 protects Caenorhabditis elegans from Salmonella typhimurium-mediated killing. Proc. Natl. Acad. Sci. U. S. A. 98:2001;2735-2739.
5. Bertin J., et al. Human CARD4 protein is a novel CED-4/Apaf-1 cell death family member that activates NF-kappaB. J. Biol. Chem. 274:1999;12955-12958.
6. Inohara N., et al. Nod1, an Apaf-1-like activator of caspase-9 and nuclear factor-kappaB. J. Biol. Chem. 274:1999;14560-14567.
7. Chamaillard M., et al. An essential role for NOD1 in host recognition of bacterial peptidoglycan containing diaminopimelic acid. Nat. Immunol. 4:2003;702-707.
8. Girardin S.E., et al. Nod1 detects a unique muropeptide from Gram-negative bacterial peptidoglycan. Science. 300:2003;1584-1587.
9. Inohara N., et al. Human Nod1 confers responsiveness to bacterial lipopolysaccharides. J. Biol. Chem. 276:2001;2551-2554.
10. Girardin S.E., et al. CARD4/Nod1 mediates NF-kappaB and JNK activation by invasive Shigella flexneri. EMBO Rep. 2:2001;736-742.
11. Schleifer K.H., Kandler O. Peptidoglycan types of bacterial cell walls and their taxonomic implications. Bacteriol. Rev. 36:1972;407-477.
12. Girardin S.E., et al. Nod2 is a general sensor of peptidoglycan through muramyl dipeptide (MDP) detection. J. Biol. Chem. 278:2003;8869-8872.
13. Inohara N., et al. Host recognition of bacterial muramyl dipeptide mediated through NOD2. Implications for Crohn's disease. J. Biol. Chem. 278:2003;5509-5512.
14. Leulier, F., et al. The Drosophila immune system detects bacteria through specific peptidoglycan recognition. Nat. Immunol. 4, 478-484.
15. Hoffmann J.A., Reichhart J.M. Drosophila innate immunity: an evolutionary perspective. Nat. Immunol. 3:2002;121-126.
16. Michel T., et al. Drosophila Toll is activated by Gram-positive bacteria through a circulating peptidoglycan recognition protein. Nature. 414:2001;756-759.
17. Gottar M., et al. The Drosophila immune response against Gram-negative bacteria is mediated by a peptidoglycan recognition protein. Nature. 416:2002;640-644.
18. Choe K.M., et al. Requirement for a peptidoglycan recognition protein (PGRP) in Relish activation and antibacterial immune responses in Drosophila. Science. 296:2002;359-362.
19. Ramet M., et al. Functional genomic analysis of phagocytosis and identification of a Drosophila receptor for E. coli. Nature. 416:2002;644-648.
20. Iketani M., et al. Minimum structure of peptidoglycan required for induction of antibacterial protein synthesis in the silkworm, Bombyx mori. Insect Biochem. Mol. Biol. 29:1999;19-24.
21. Liepinsh E., et al. NMR structure of Citrobacter freundii Ampd, comparison with bacteriophage T7 lysozyme and homology with PGRP domains. J. Mol. Biol. 327:2003;833-842.
22. Ogura Y., et al. A frameshift mutation in NOD2 associated with susceptibility to Crohn's disease. Nature. 411:2001;603-606.
23. Dorman C.J., et al. Regulation of virulence gene expression in Shigella flexneri, a facultative intracellular pathogen. Int. J. Med. Microbiol. 291:2001;89-96.
24. Censini S., et al. Cellular responses induced after contact with Helicobacter pylori. Curr. Opin. Microbiol. 4:2001;41-46.