메뉴 건너뛰기




Volumn 1, Issue 5, 2009, Pages 494-506

ClpX contributes to innate defense peptide resistance and virulence phenotypes of Bacillus anthracis

Author keywords

Antimicrobial peptides; Bacillus anthracis; Bacterial infection; Cathelicidins; Hemolysis; Innate immunity; Protease; Transposon mutagenesis; Virulence factor

Indexed keywords

ADENOSINE TRIPHOSPHATASE; AGAR; ALPHA DEFENSIN; CASEIN; CATHELICIDIN; ENDOPEPTIDASE CLPX; LYSOZYME; POLYPEPTIDE ANTIBIOTIC AGENT; VIRULENCE FACTOR;

EID: 77953395311     PISSN: 1662811X     EISSN: 16628128     Source Type: Journal    
DOI: 10.1159/000225955     Document Type: Article
Times cited : (42)

References (40)
  • 3
    • 0000079777 scopus 로고    scopus 로고
    • The capsule of Bacillus anthracis, a review
    • Ezzell JW, Welkos SL: The capsule of Bacillus anthracis , a review. J Appl Microbiol 1999;87:250.
    • (1999) J Appl Microbiol , vol.87 , pp. 250
    • Ezzell, J.W.1    Welkos, S.L.2
  • 5
    • 33846942977 scopus 로고    scopus 로고
    • Clp ATPases and ClpP proteolytic complexes regulate vital biological processes in low GC, Gram-positive bacteria
    • Frees D, Savijoki K, Varmanen P, Ingmer H: Clp ATPases and ClpP proteolytic complexes regulate vital biological processes in low GC, Gram-positive bacteria. Mol Microbiol 2007;63:1285-1295.
    • (2007) Mol Microbiol , vol.63 , pp. 1285-1295
    • Frees, D.1    Savijoki, K.2    Varmanen, P.3    Ingmer, H.4
  • 6
    • 0029126356 scopus 로고
    • Homology in structural organization between E. coli ClpAP protease and the eukaryotic 26 S proteasome
    • Kessel M, Maurizi MR, Kim B, Kocsis E, Trus BL, Singh SK, Steven AC: Homology in structural organization between E. coli ClpAP protease and the eukaryotic 26 S proteasome. J Mol Biol 1995;250:587-594.
    • (1995) J Mol Biol , vol.250 , pp. 587-594
    • Kessel, M.1    Maurizi, M.R.2    Kim, B.3    Kocsis, E.4    Trus, B.L.5    Singh, S.K.6    Steven, A.C.7
  • 7
    • 0024552829 scopus 로고
    • Protease Ti from Escherichia coli requires ATP hydrolysis for protein breakdown but not for hydrolysis of small peptides
    • Woo KM, Chung WJ, Ha DB, Goldberg AL, Chung CH: Protease Ti from Escherichia coli requires ATP hydrolysis for protein breakdown but not for hydrolysis of small peptides. J Biol Chem 1989;264:2088-2091.
    • (1989) J Biol Chem , vol.264 , pp. 2088-2091
    • Woo, K.M.1    Chung, W.J.2    Ha, D.B.3    Goldberg, A.L.4    Chung, C.H.5
  • 8
    • 0029000134 scopus 로고
    • The ClpX heat-shock protein of Escherichia coli, the ATP-dependent substrate specificity component of the ClpPClpX protease, is a novel molecular chaperone
    • Wawrzynow A, Wojtkowiak D, Marszalek J, Banecki B, Jonsen M, Graves B, Georgopoulos C, Zylicz M: The ClpX heat-shock protein of Escherichia coli , the ATP-dependent substrate specificity component of the ClpPClpX protease, is a novel molecular chaperone. EMBO J 1995;14:1867-1877.
    • (1995) EMBO J , vol.14 , pp. 1867-1877
    • Wawrzynow, A.1    Wojtkowiak, D.2    Marszalek, J.3    Banecki, B.4    Jonsen, M.5    Graves, B.6    Georgopoulos, C.7    Zylicz, M.8
  • 9
    • 0037351068 scopus 로고    scopus 로고
    • Proteomic discovery of cellular substrates of the ClpXP protease reveals five classes of ClpX-recognition signals
    • Flynn JM, Neher SB, Kim YI, Sauer RT, Baker TA: Proteomic discovery of cellular substrates of the ClpXP protease reveals five classes of ClpX-recognition signals. Mol Cell 2003;11:671-683.
    • (2003) Mol Cell , vol.11 , pp. 671-683
    • Flynn, J.M.1    Neher, S.B.2    Kim, Y.I.3    Sauer, R.T.4    Baker, T.A.5
  • 10
    • 0033042119 scopus 로고    scopus 로고
    • Role of Lon and ClpX in the post-translational regulation of a sigma subunit of RNA polymerase required for cellular differentiation in Bacillus subtilis
    • DOI 10.1046/j.1365-2958.1999.01489.x
    • Liu J, Cosby WM, Zuber P: Role of Lon and ClpX in the post-translational regulation of a sigma subunit of RNA polymerase required for cellular differentiation in Bacillus subtilis . Mol Microbiol 1999;33:415-428. (Pubitemid 29322527)
    • (1999) Molecular Microbiology , vol.33 , Issue.2 , pp. 415-428
    • Liu, J.1    Cosby, W.M.2    Zuber, P.3
  • 11
    • 9644300997 scopus 로고    scopus 로고
    • Beta-lactamase gene expression in a penicillin-resistant Bacillus anthracis strain
    • Chen Y, Tenover FC, Koehler TM: Beta-lactamase gene expression in a penicillin-resistant Bacillus anthracis strain. Antimicrob Agents Chemother 2004;48:4873-4877.
    • (2004) Antimicrob Agents Chemother , vol.48 , pp. 4873-4877
    • Chen, Y.1    Tenover, F.C.2    Koehler, T.M.3
  • 13
    • 0033590591 scopus 로고    scopus 로고
    • A vector for promoter trapping in Bacillus cereus
    • Dunn AK, Handelsman J: A vector for promoter trapping in Bacillus cereus . Gene 1999;226:297-305.
    • (1999) Gene , vol.226 , pp. 297-305
    • Dunn, A.K.1    Handelsman, J.2
  • 14
    • 0028157366 scopus 로고
    • Regulation of the Bacillus anthracis protective antigen gene: CO2 and a trans -acting element activate transcription from one of two promoters
    • Koehler TM, Dai Z, Kaufman-Yarbray M: Regulation of the Bacillus anthracis protective antigen gene: CO2 and a trans -acting element activate transcription from one of two promoters. J Bacteriol 1994;176:586-595.
    • (1994) J Bacteriol , vol.176 , pp. 586-595
    • Koehler, T.M.1    Dai, Z.2    Kaufman-Yarbray, M.3
  • 15
    • 0037767296 scopus 로고    scopus 로고
    • Characterization of anthrolysin O, the Bacillus anthracis cholesterol-dependent cytolysin
    • Shannon JG, Ross CL, Koehler TM, Rest RF: Characterization of anthrolysin O, the Bacillus anthracis cholesterol-dependent cytolysin. Infect Immun 2003;71:3183-3189.
    • (2003) Infect Immun , vol.71 , pp. 3183-3189
    • Shannon, J.G.1    Ross, C.L.2    Koehler, T.M.3    Rest, R.F.4
  • 17
    • 0001864545 scopus 로고
    • Sporulation, germination and outgrowth
    • Harwood CR, Cutting SM (eds): Chichester, John Wiley & Sons
    • Nicholson WL, Setow P: Sporulation, germination and outgrowth; in Harwood CR, Cutting SM (eds): Molecular biological methods for Bacillus. Chichester, John Wiley & Sons, 1990, pp 391-450.
    • (1990) Molecular Biological Methods for Bacillus , pp. 391-450
    • Nicholson, W.L.1    Setow, P.2
  • 20
    • 0031833703 scopus 로고    scopus 로고
    • Factors affecting transposition of the Himar1 mariner transposon in vitro
    • Lampe DJ, Grant TE, Robertson HM: Factors affecting transposition of the Himar1 mariner transposon in vitro. Genetics 1998;149:179-187. (Pubitemid 28246796)
    • (1998) Genetics , vol.149 , Issue.1 , pp. 179-187
    • Lampe, D.J.1    Grant, T.E.2    Robertson, H.M.3
  • 21
    • 33646507877 scopus 로고    scopus 로고
    • Transposon mutagenesis of Bacillus anthracis strain Sterne using Bursa aurealis
    • Tam C, Glass EM, Anderson DM, Missiakas D: Transposon mutagenesis of Bacillus anthracis strain Sterne using Bursa aurealis . Plasmid 2006;56:74-77.
    • (2006) Plasmid , vol.56 , pp. 74-77
    • Tam, C.1    Glass, E.M.2    Anderson, D.M.3    Missiakas, D.4
  • 22
    • 36349012535 scopus 로고    scopus 로고
    • New transposon delivery plasmids for insertional mutagenesis in Bacillus anthracis
    • Wilson AC, Perego M, Hoch JA: New transposon delivery plasmids for insertional mutagenesis in Bacillus anthracis . J Microbiol Methods 2007;71:332-335.
    • (2007) J Microbiol Methods , vol.71 , pp. 332-335
    • Wilson, A.C.1    Perego, M.2    Hoch, J.A.3
  • 23
    • 33947432067 scopus 로고    scopus 로고
    • The alternative sigma factor SigmaH is required for toxin gene expression by Bacillus anthracis
    • Hadjifrangiskou M, Chen Y, Koehler TM: The alternative sigma factor SigmaH is required for toxin gene expression by Bacillus anthracis . J Bacteriol 2007;189:1874-1883.
    • (2007) J Bacteriol , vol.189 , pp. 1874-1883
    • Hadjifrangiskou, M.1    Chen, Y.2    Koehler, T.M.3
  • 24
    • 0036532403 scopus 로고    scopus 로고
    • How do bacteria resist human antimicrobial peptides?
    • Peschel A: How do bacteria resist human antimicrobial peptides? Trends Microbiol 2002;10:179-186.
    • (2002) Trends Microbiol , vol.10 , pp. 179-186
    • Peschel, A.1
  • 25
    • 33745606225 scopus 로고    scopus 로고
    • Proteolytic degradation of human antimicrobial peptide LL-37 by Bacillus anthracis may contribute to virulence
    • Thwaite JE, Hibbs S, Titball RW, Atkins TP: Proteolytic degradation of human antimicrobial peptide LL-37 by Bacillus anthracis may contribute to virulence. Antimicrob Agents Chemother 2006;50:2316-2322.
    • (2006) Antimicrob Agents Chemother , vol.50 , pp. 2316-2322
    • Thwaite, J.E.1    Hibbs, S.2    Titball, R.W.3    Atkins, T.P.4
  • 27
    • 33745698864 scopus 로고    scopus 로고
    • Defensins in innate antiviral immunity
    • Klotman ME, Chang TL: Defensins in innate antiviral immunity. Nat Rev Immunol 2006;6:447-456.
    • (2006) Nat Rev Immunol , vol.6 , pp. 447-456
    • Klotman, M.E.1    Chang, T.L.2
  • 28
    • 18644363054 scopus 로고    scopus 로고
    • Mouse cathelin-related antimicrobial peptide chemoattracts leukocytes using formyl peptide receptor-like 1/mouse formyl peptide receptor-like 2 as the receptor and acts as an immune adjuvant
    • Kurosaka K, Chen Q, Yarovinsky F, Oppenheim JJ, Yang D: Mouse cathelin-related antimicrobial peptide chemoattracts leukocytes using formyl peptide receptor-like 1/mouse formyl peptide receptor-like 2 as the receptor and acts as an immune adjuvant. J Immunol 2005;174:6257-6265. (Pubitemid 40663818)
    • (2005) Journal of Immunology , vol.174 , Issue.10 , pp. 6257-6265
    • Kurosaka, K.1    Chen, Q.2    Yarovinsky, F.3    Oppenheim, J.J.4    Yang, D.5
  • 29
    • 0027237329 scopus 로고
    • Plasma defensin concentrations are elevated in patients with septicemia or bacterial meningitis
    • Panyutich AV, Panyutich EA, Krapivin VA, Baturevich EA, Ganz T: Plasma defensin concentrations are elevated in patients with septicemia or bacterial meningitis. J Lab Clin Med 1993;122:202-207.
    • (1993) J Lab Clin Med , vol.122 , pp. 202-207
    • Panyutich, A.V.1    Panyutich, E.A.2    Krapivin, V.A.3    Baturevich, E.A.4    Ganz, T.5
  • 32
    • 33748987913 scopus 로고    scopus 로고
    • Transcriptional profiling of the Bacillus anthracis life cycle in vitro and an implied model for regulation of spore formation
    • Bergman NH, Anderson EC, Swenson EE, Niemeyer MM, Miyoshi AD, Hanna PC: Transcriptional profiling of the Bacillus anthracis life cycle in vitro and an implied model for regulation of spore formation. J Bacteriol 2006;188:6092-6100.
    • (2006) J Bacteriol , vol.188 , pp. 6092-6100
    • Bergman, N.H.1    Anderson, E.C.2    Swenson, E.E.3    Niemeyer, M.M.4    Miyoshi, A.D.5    Hanna, P.C.6
  • 33
    • 32444449199 scopus 로고    scopus 로고
    • The dlt ABCD operon of Bacillus anthracis Sterne is required for virulence and resistance to peptide, enzymatic, and cellular mediators of innate immunity
    • Fisher N, Shetron-Rama L, Herring-Palmer A, Heffernan B, Bergman N, Hanna P: The dlt ABCD operon of Bacillus anthracis Sterne is required for virulence and resistance to peptide, enzymatic, and cellular mediators of innate immunity. J Bacteriol 2006;188:1301-1309.
    • (2006) J Bacteriol , vol.188 , pp. 1301-1309
    • Fisher, N.1    Shetron-Rama, L.2    Herring-Palmer, A.3    Heffernan, B.4    Bergman, N.5    Hanna, P.6
  • 34
    • 0038236437 scopus 로고    scopus 로고
    • Alternative roles of ClpX and ClpP in Staphylococcus aureus stress tolerance and virulence
    • Frees D, Qazi SN, Hill PJ, Ingmer H: Alternative roles of ClpX and ClpP in Staphylococcus aureus stress tolerance and virulence. Mol Microbiol 2003;48:1565-1578.
    • (2003) Mol Microbiol , vol.48 , pp. 1565-1578
    • Frees, D.1    Qazi, S.N.2    Hill, P.J.3    Ingmer, H.4
  • 35
    • 28444470162 scopus 로고    scopus 로고
    • Global virulence regulation in Staphylococcus aureus: Pinpointing the roles of ClpP and ClpX in the sar/agr regulatory network
    • Frees D, Sorensen K, Ingmer H: Global virulence regulation in Staphylococcus aureus : Pinpointing the roles of ClpP and ClpX in the sar/agr regulatory network. Infect Immun 2005;73:8100-8108.
    • (2005) Infect Immun , vol.73 , pp. 8100-8108
    • Frees, D.1    Sorensen, K.2    Ingmer, H.3
  • 36
    • 35748985576 scopus 로고    scopus 로고
    • Cathelicidin-deficient (CnlP-/-) mice show increased susceptibility to Pseudomonas aeruginos a keratitis
    • Huang LC, Reins RY, Gallo RL, McDermott AM: Cathelicidin-deficient (CnlP-/-) mice show increased susceptibility to Pseudomonas aeruginos a keratitis. Invest Ophthalmol Vis Sci 2007;48:4498-4508.
    • (2007) Invest Ophthalmol Vis Sci , vol.48 , pp. 4498-4508
    • Huang, L.C.1    Reins, R.Y.2    Gallo, R.L.3    McDermott, A.M.4
  • 37
    • 17044404692 scopus 로고    scopus 로고
    • Cathelicidin mediates innate intestinal defense against colonization with epithelial adherent bacterial pathogens
    • Iimura M, Gallo RL, Hase K, Miyamoto Y, Eckmann L, Kagnoff MF: Cathelicidin mediates innate intestinal defense against colonization with epithelial adherent bacterial pathogens. J Immunol 2005;174:4901-4907. (Pubitemid 40504574)
    • (2005) Journal of Immunology , vol.174 , Issue.8 , pp. 4901-4907
    • Iimura, M.1    Gallo, R.L.2    Hase, K.3    Miyamoto, Y.4    Eckmann, L.5    Kagnoff, M.F.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.