PGRP-SB1: An N-acetylmuramoyl l-alanine amidase with antibacterial activity

Biochemical and Biophysical Research Communications

Volumn 350, Issue 4, 2006, Pages 994-999

  Mellroth, Peter ^a   Steiner, Håkan ^a  

^a STOCKHOLM UNIVERSITY   (Sweden)

Author keywords

Innate immunity; Peptidoglycan; PGRP

Indexed keywords

N ACETYLMURAMOYLALANINE AMIDASE; PEPTIDOGLYCAN; PEPTIDOGLYCAN RECOGNITION PROTEIN SB1; UNCLASSIFIED DRUG;

ANTIBACTERIAL ACTIVITY; ARTICLE; BACILLUS MEGATERIUM; BACTERICIDAL ACTIVITY; CROSS LINKING; DRUG EFFECT; ENZYME ACTIVITY; LETHAL DOSE; MOLECULAR CLONING; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN EXPRESSION;

ANTI-BACTERIAL AGENTS; BACILLUS MEGATERIUM; CARRIER PROTEINS; CELL SURVIVAL; DOSE-RESPONSE RELATIONSHIP, DRUG; DROSOPHILA PROTEINS;

BACILLUS MEGATERIUM; BACTERIA (MICROORGANISMS); HEXAPODA; MAMMALIA; VERTEBRATA;

EID: 33750091050     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2006.09.139     Document Type: Article

References (30)

1. Akira S., and Takeda K. Functions of toll-like receptors: lessons from KO mice. C. R. Biol. 327 (2004) 581-589
2. Philpott D.J., and Girardin S.E. The role of Toll-like receptors and Nod proteins in bacterial infection. Mol. Immunol. 41 (2004) 1099-1108
3. Steiner H. Peptidoglycan recognition proteins: on and off switches for innate immunity. Immunol. Rev. 198 (2004) 83-96
4. Gelius E., Persson C., Karlsson J., and Steiner H. A mammalian peptidoglycan recognition protein with N-acetylmuramoyl-l-alanine amidase activity. Biochem. Biophys. Res. Commun. 306 (2003) 988-994
5. Mellroth P., Karlsson J., and Steiner H. A scavenger function for a Drosophila peptidoglycan recognition protein. J. Biol. Chem. 278 (2003) 7059-7064
6. Wang Z.M., Li X., Cocklin R.R., Wang M., Fukase K., Inamura S., Kusumoto S., Gupta D., and Dziarski R. Human peptidoglycan recognition protein-L is an N-acetylmuramoyl-l-alanine amidase. J. Biol. Chem. 278 (2003) 49044-49052
7. Kim M.S., Byun M., and Oh B.H. Crystal structure of peptidoglycan recognition protein LB from Drosophila melanogaster. Nat. Immunol. 4 (2003) 787-793
8. Zaidman-Remy A., Herve M., Poidevin M., Pili-Floury S., Kim M.S., Blanot D., Oh B.H., Ueda R., Mengin-Lecreulx D., and Lemaitre B. The Drosophila amidase PGRP-LB modulates the immune response to bacterial infection. Immunity 24 (2006) 463-473
9. Bischoff V., Vignal C., Duvic B., Boneca I.G., Hoffmann J.A., and Royet J. Downregulation of the Drosophila immune response by peptidoglycan-recognition proteins SC1 and SC2. PLoS Pathog. 2 (2006) e14
10. Lu X., Wang M., Qi J., Wang H., Li X., Gupta D., and Dziarski R. Peptidoglycan recognition proteins are a new class of human bactericidal proteins. J. Biol. Chem. 281 (2006) 5895-5907
11. Cho J.H., Fraser I.P., Fukase K., Kusumoto S., Fujimoto Y., Stahl G.L., and Ezekowitz R.A. Human peptidoglycan recognition protein S is an effector of neutrophil-mediated innate immunity. Blood 106 (2005) 2551-2558
12. Liu C., Gelius E., Liu G., Steiner H., and Dziarski R. Mammalian peptidoglycan recognition protein binds peptidoglycan with high affinity, is expressed in neutrophils, and inhibits bacterial growth. J. Biol. Chem. 275 (2000) 24490-24499
13. Tydell C.C., Yuan J., Tran P., and Selsted M.E. Bovine peptidoglycan recognition protein-S: antimicrobial activity, localization, secretion, and binding properties. J. Immunol. 176 (2006) 1154-1162
14. Tydell C.C., Yount N., Tran D., Yuan J., and Selsted M.E. Isolation, characterization, and antimicrobial properties of bovine oligosaccharide-binding protein. A microbicidal granule protein of eosinophils and neutrophils. J. Biol. Chem. 277 (2002) 19658-19664
15. Hultmark D., Engstrom A., Andersson K., Steiner H., Bennich H., and Boman H.G. Insect immunity. Attacins, a family of antibacterial proteins from Hyalophora cecropia. EMBO J. 2 (1983) 571-576
16. Boman H.G., Nilsson-Faye I., Paul K., and Rasmuson Jr. T. Insect immunity. I. Characteristics of an inducible cell-free antibacterial reaction in hemolymph of Samia cynthia pupae. Infect. Immun. 10 (1974) 136-145
17. Edlund T., Siden I., and Boman H.G. Evidence for two immune inhibitors from Bacillus thuringiensis interfering with the humoral defense system of saturniid pupae. Infect. Immun. 14 (1976) 934-941
18. Boman H.G., Wade D., Boman I.A., Wahlin B., and Merrifield R.B. Antibacterial and antimalarial properties of peptides that are cecropin-melittin hybrids. FEBS Lett. 259 (1989) 103-106
19. Andreu D., Merrifield R.B., Steiner H., and Boman H.G. N-terminal analogues of cecropin A: synthesis, antibacterial activity, and conformational properties. Biochemistry 24 (1985) 1683-1688
20. Andersson M., Gunne H., Agerberth B., Boman A., Bergman T., Sillard R., Jornvall H., Mutt V., Olsson B., Wigzell H., et al. NK-lysin, a novel effector peptide of cytotoxic T and NK cells. Structure and cDNA cloning of the porcine form, induction by interleukin 2, antibacterial and antitumour activity. EMBO J. 14 (1995) 1615-1625
21. Simelyte E., Rimpilainen M., Zhang X., and Toivanen P. Role of peptidoglycan subtypes in the pathogenesis of bacterial cell wall arthritis. Ann. Rheum. Dis. 62 (2003) 976-982
22. Mellroth P., Karlsson J., Hakansson J., Schultz N., Goldman W.E., and Steiner H. Ligand-induced dimerization of Drosophila peptidoglycan recognition proteins in vitro. Proc. Natl. Acad. Sci. USA 102 (2005) 6455-6460
23. Kaneko T., Yano T., Aggarwal K., Lim J.H., Ueda K., Oshima Y., Peach C., Erturk-Hasdemir D., Goldman W.E., Oh B.H., Kurata S., and Silverman N. PGRP-LC and PGRP-LE have essential yet distinct functions in the Drosophila immune response to monomeric DAP-type peptidoglycan. Nat. Immunol. 7 (2006) 715-723
24. Kaneko T., Goldman W.E., Mellroth P., Steiner H., Fukase K., Kusumoto S., Harley W., Fox A., Golenbock D., and Silverman N. Monomeric and polymeric gram-negative peptidoglycan but not purified LPS stimulate the Drosophila IMD pathway. Immunity 20 (2004) 637-649
25. Lim J.H., Kim M.S., Kim H.E., Yano T., Oshima Y., Aggarwal K., Goldman W.E., Silverman N., Kurata S., and Oh B.H. Structural basis for preferential recognition of diaminopimelic acid-type peptidoglycan by a subset of peptidoglycan recognition proteins. J. Biol. Chem. 281 (2006) 8286-8295
26. Chang C.I., Chelliah Y., Borek D., Mengin-Lecreulx D., and Deisenhofer J. Structure of tracheal cytotoxin in complex with a heterodimeric pattern-recognition receptor. Science 311 (2006) 1761-1764
27. Folkesson A., Eriksson S., Andersson M., Park J.T., and Normark S. Components of the peptidoglycan-recycling pathway modulate invasion and intracellular survival of Salmonella enterica serovar Typhimurium. Cell. Microbiol. 7 (2005) 147-155
28. Werner T., Liu G., Kang D., Ekengren S., Steiner H., and Hultmark D. A family of peptidoglycan recognition proteins in the fruit fly Drosophila melanogaster. Proc. Natl. Acad. Sci. USA 97 (2000) 13772-13777
29. Chahboune A., Decaffmeyer M., Brasseur R., and Joris B. Membrane topology of the Escherichia coli AmpG permease required for recycling of cell wall anhydromuropeptides and AmpC beta-lactamase induction. Antimicrob. Agents Chemother. 49 (2005) 1145-1149
30. Cheng Q., and Park J.T. Substrate specificity of the AmpG permease required for recycling of cell wall anhydro-muropeptides. J. Bacteriol. 184 (2002) 6434-6436