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Volumn 32, Issue 12, 2004, Pages 2485-2490

The antimicrobial peptide BMAP-28 reduces lethality in mouse models of staphylococcal sepsis

Author keywords

Antimicrobial peptide; BMAP 28; Cathelicidins; Septic shock; Staphylococcal sepsis

Indexed keywords

ANTIMICROBIAL PEPTIDE BMAP 28; CLARITHROMYCIN; CLINDAMYCIN; IMIPENEM; INTERLEUKIN 6; ISOTONIC SOLUTION; NITRIC OXIDE; POLYPEPTIDE ANTIBIOTIC AGENT; SODIUM CHLORIDE; TUMOR NECROSIS FACTOR ALPHA; UNCLASSIFIED DRUG; VANCOMYCIN;

EID: 10644276256     PISSN: 00903493     EISSN: None     Source Type: Journal    
DOI: 10.1097/01.CCM.0000148221.09704.22     Document Type: Article
Times cited : (41)

References (46)
  • 1
    • 0033590515 scopus 로고    scopus 로고
    • Treating patients with severe sepsis
    • Wheeler AP, Bernard GR: Treating patients with severe sepsis. N Engl J Med 1999; 340:207-214
    • (1999) N Engl J Med , vol.340 , pp. 207-214
    • Wheeler, A.P.1    Bernard, G.R.2
  • 2
    • 0032839548 scopus 로고    scopus 로고
    • A 25-year study of nosocomial bacteremia in an adult intensive care unit
    • Edgeworth JD, Treacher DF, Eykyn SJ: A 25-year study of nosocomial bacteremia in an adult intensive care unit. Crit Care Med 1999; 27:1421-1428
    • (1999) Crit Care Med , vol.27 , pp. 1421-1428
    • Edgeworth, J.D.1    Treacher, D.F.2    Eykyn, S.J.3
  • 4
    • 0034958947 scopus 로고    scopus 로고
    • Epidemiology of severe sepsis in the United States: Analysis of incidence, outcome, and associated cost of care
    • Angus DC, Linde-Zwirble WT, Lidicker J, et al: Epidemiology of severe sepsis in the United States: Analysis of incidence, outcome, and associated cost of care. Crit Care Med 2001; 29:1303-1310
    • (2001) Crit Care Med , vol.29 , pp. 1303-1310
    • Angus, D.C.1    Linde-Zwirble, W.T.2    Lidicker, J.3
  • 5
    • 0028040319 scopus 로고
    • Gram-positive organisms and sepsis
    • Bone RC: Gram-positive organisms and sepsis. Arch Intern Med 1994; 154:26-34
    • (1994) Arch Intern Med , vol.154 , pp. 26-34
    • Bone, R.C.1
  • 6
    • 0037226528 scopus 로고    scopus 로고
    • In vivo antibacterial activity of RWJ-54428, a new cephalosporin with activity against Gram-positive bacteria
    • Griffith DC, Harford L, Williams R, et al: In vivo antibacterial activity of RWJ-54428, a new cephalosporin with activity against Gram-positive bacteria. Antimicrob Agents Chemother 2003; 47:43-47
    • (2003) Antimicrob Agents Chemother , vol.47 , pp. 43-47
    • Griffith, D.C.1    Harford, L.2    Williams, R.3
  • 7
    • 0037451929 scopus 로고    scopus 로고
    • The epidemiology of sepsis in the United States from 1979 through 2000
    • Martin GS, Mannino DM, Eaton S, et al: The epidemiology of sepsis in the United States from 1979 through 2000. N Engl J Med 2003; 348:1546-1554
    • (2003) N Engl J Med , vol.348 , pp. 1546-1554
    • Martin, G.S.1    Mannino, D.M.2    Eaton, S.3
  • 8
    • 0033389160 scopus 로고    scopus 로고
    • Implications of vancomycin resistant Staphylococcus aureus
    • Tenover FC: Implications of vancomycin resistant Staphylococcus aureus. J Hosp Infect 1999; 43(Suppl):S3-S7
    • (1999) J Hosp Infect , vol.43 , Issue.SUPPL.
    • Tenover, F.C.1
  • 9
    • 0031926087 scopus 로고    scopus 로고
    • Staphylococcus epidermidis emerging resistance and need for alternative agents
    • Raad I, Alrahwan A, Rolston K: Staphylococcus epidermidis emerging resistance and need for alternative agents. Clin Infect Dis 1998; 26:1182-1187
    • (1998) Clin Infect Dis , vol.26 , pp. 1182-1187
    • Raad, I.1    Alrahwan, A.2    Rolston, K.3
  • 10
    • 0028824813 scopus 로고
    • The cell wall components peptidoglycan and lipoteichoic acid from Staphylococcus aureus act in synergy to cause shock and multiple organ failure
    • De Kimpe SJ, Kengatharan M, Thiemermann C, et al: The cell wall components peptidoglycan and lipoteichoic acid from Staphylococcus aureus act in synergy to cause shock and multiple organ failure. Proc Natl Acad Sci U S A 1995; 92:10359-10363
    • (1995) Proc Natl Acad Sci U S A , vol.92 , pp. 10359-10363
    • De Kimpe, S.J.1    Kengatharan, M.2    Thiemermann, C.3
  • 11
    • 0026334206 scopus 로고
    • Hemodynamic responses to Gram-positive versus Gram-negative sepsis in critically ill patients with or without circulatory shock
    • Ahmed A, Kruse J, Haupt M, et al: Hemodynamic responses to Gram-positive versus Gram-negative sepsis in critically ill patients with or without circulatory shock. Crit Care Med 1991; 19:1520-1525
    • (1991) Crit Care Med , vol.19 , pp. 1520-1525
    • Ahmed, A.1    Kruse, J.2    Haupt, M.3
  • 12
    • 0028285885 scopus 로고
    • Gram-positive cell walls stimulate synthesis of tumor necrosis factor alpha and interleukin-6 by human monocytes
    • Heumann D, Barras C, Severin A, et al: Gram-positive cell walls stimulate synthesis of tumor necrosis factor alpha and interleukin-6 by human monocytes. Infect Immun 1994; 62:2715-2721
    • (1994) Infect Immun , vol.62 , pp. 2715-2721
    • Heumann, D.1    Barras, C.2    Severin, A.3
  • 13
    • 0027373390 scopus 로고
    • Induction of release of tumor necrosis factor from human monocytes by staphylococci and staphylococcal peptidoglycans
    • Timmerman CP, Mattsson E, Martinez-Martinez L, et al: Induction of release of tumor necrosis factor from human monocytes by staphylococci and staphylococcal peptidoglycans. Infect Immun 1993; 61:4167-4172
    • (1993) Infect Immun , vol.61 , pp. 4167-4172
    • Timmerman, C.P.1    Mattsson, E.2    Martinez-Martinez, L.3
  • 14
    • 0031821974 scopus 로고    scopus 로고
    • Mechanism of Gram-positive shock: Identification of peptidoglycan and lipoteichoic acid mioeties essential in the induction of nitric oxide synthase, shock, and multiple organ failure
    • Kengatharan M, De Kimpe SJ, Robson C, et al: Mechanism of Gram-positive shock: Identification of peptidoglycan and lipoteichoic acid mioeties essential in the induction of nitric oxide synthase, shock, and multiple organ failure. J Exp Med 1998; 188:305-315
    • (1998) J Exp Med , vol.188 , pp. 305-315
    • Kengatharan, M.1    De Kimpe, S.J.2    Robson, C.3
  • 15
    • 0035142620 scopus 로고    scopus 로고
    • Inhibition of bacterial superantigens by peptides and antibodies
    • Visvanathan K, Charles A, Bannan J, et al: Inhibition of bacterial superantigens by peptides and antibodies. Infect Immun 2001; 69:875-884
    • (2001) Infect Immun , vol.69 , pp. 875-884
    • Visvanathan, K.1    Charles, A.2    Bannan, J.3
  • 16
    • 0033997295 scopus 로고    scopus 로고
    • Defining a novel domain of staphylococcal toxic shock syndrome toxin-1 critical for major histocompatibility complex class II binding, superantigenic activity, and lethality
    • Kum WW, Laupland KB, Chow AW: Defining a novel domain of staphylococcal toxic shock syndrome toxin-1 critical for major histocompatibility complex class II binding, superantigenic activity, and lethality. Can J Microbiol 2000; 46:171-179
    • (2000) Can J Microbiol , vol.46 , pp. 171-179
    • Kum, W.W.1    Laupland, K.B.2    Chow, A.W.3
  • 17
    • 0036234708 scopus 로고    scopus 로고
    • Superantigens: Microbial agents that corrupt immunity
    • Llewelyn M, Cohen J: Superantigens: Microbial agents that corrupt immunity. Lancet Infect Dis 2002; 2:56-162
    • (2002) Lancet Infect Dis , vol.2 , pp. 56-162
    • Llewelyn, M.1    Cohen, J.2
  • 18
    • 0030044284 scopus 로고    scopus 로고
    • Interleukins 6 and 11 protect mice from mortality in a staphylococcal enterotoxin-induced toxic shock model
    • Barton BE, Shortall J, Jackson JV: Interleukins 6 and 11 protect mice from mortality in a staphylococcal enterotoxin-induced toxic shock model. Infect Immun 1996; 64:714-718
    • (1996) Infect Immun , vol.64 , pp. 714-718
    • Barton, B.E.1    Shortall, J.2    Jackson, J.V.3
  • 19
    • 0032752132 scopus 로고    scopus 로고
    • Interaction of cationic peptides with lipoteichoic acid and gram-positive bacteria
    • Scott MG, Gold MR, Hancock REW: Interaction of cationic peptides with lipoteichoic acid and gram-positive bacteria. Infect Immun 1999; 67:6445-6453
    • (1999) Infect Immun , vol.67 , pp. 6445-6453
    • Scott, M.G.1    Gold, M.R.2    Hancock, R.E.W.3
  • 20
    • 0033605557 scopus 로고    scopus 로고
    • Inactivation of the dit operon in Staphylococcus aureus confers sensitivity to defensins, protegrins, and other antimicrobial peptides
    • Peschel A, Otto M, Jack RW, et al: Inactivation of the dit operon in Staphylococcus aureus confers sensitivity to defensins, protegrins, and other antimicrobial peptides. J Biol Chem 1999; 274:8405-8410
    • (1999) J Biol Chem , vol.274 , pp. 8405-8410
    • Peschel, A.1    Otto, M.2    Jack, R.W.3
  • 21
    • 0029797592 scopus 로고    scopus 로고
    • Supernatants from Staphylococcus epidermidis grown in the presence of different antibiotics induce differential release of tumor necrosis factors alpha from human monocytes
    • Mattsson E, Van Dijk H, Verhoef J, et al: Supernatants from Staphylococcus epidermidis grown in the presence of different antibiotics induce differential release of tumor necrosis factors alpha from human monocytes. Infect Immun 1996; 64:4351-4355
    • (1996) Infect Immun , vol.64 , pp. 4351-4355
    • Mattsson, E.1    Van Dijk, H.2    Verhoef, J.3
  • 22
    • 0038447123 scopus 로고    scopus 로고
    • Receptors, mediators, and mechanisms involved in bacterial sepsis and septic shock
    • Van Amersfoort ES, Van Berkel TJC, Kuiper J: Receptors, mediators, and mechanisms involved in bacterial sepsis and septic shock. Clin Microb Rev 2003; 16:379-414
    • (2003) Clin Microb Rev , vol.16 , pp. 379-414
    • Van Amersfoort, E.S.1    Van Berkel, T.J.C.2    Kuiper, J.3
  • 23
    • 0038578608 scopus 로고    scopus 로고
    • Novel strategies for the treatment of sepsis
    • Riedemann NC, Guo RF, Ward PA: Novel strategies for the treatment of sepsis. Nature Med 2003; 9:517-524
    • (2003) Nature Med , vol.9 , pp. 517-524
    • Riedemann, N.C.1    Guo, R.F.2    Ward, P.A.3
  • 24
    • 0034255255 scopus 로고    scopus 로고
    • The role of antimicrobial peptides in animal defenses
    • Hancock REW, Scott MG: The role of antimicrobial peptides in animal defenses. Proc Natl Acad Sci U S A 2000; 97:856-861
    • (2000) Proc Natl Acad Sci U S A , vol.97 , pp. 856-861
    • Hancock, R.E.W.1    Scott, M.G.2
  • 25
    • 0038184127 scopus 로고    scopus 로고
    • Administration of protegrin peptide IB-367 to prevent endotoxin-induced mortality in bile duct-ligated rats
    • Giacometti A, Cirioni O, Ghiselli R, et al: Administration of protegrin peptide IB-367 to prevent endotoxin-induced mortality in bile duct-ligated rats. Gut 2003; 52:874-878
    • (2003) Gut , vol.52 , pp. 874-878
    • Giacometti, A.1    Cirioni, O.2    Ghiselli, R.3
  • 26
    • 0029824838 scopus 로고    scopus 로고
    • Antiendotoxin activity of cationic peptide antimicrobial agents
    • Gough M, Hancock REW, Kelly NM: Antiendotoxin activity of cationic peptide antimicrobial agents. Infect Immun 1996; 64:4922-4927
    • (1996) Infect Immun , vol.64 , pp. 4922-4927
    • Gough, M.1    Hancock, R.E.W.2    Kelly, N.M.3
  • 27
    • 0036257411 scopus 로고    scopus 로고
    • Cathelicidin peptides as candidates for a novel class of antimicrobials
    • Zanetti M, Gennaro R, Skerlavaj B, et al: Cathelicidin peptides as candidates for a novel class of antimicrobials. Curr Pharm Des 2002; 8:779-793
    • (2002) Curr Pharm des , vol.8 , pp. 779-793
    • Zanetti, M.1    Gennaro, R.2    Skerlavaj, B.3
  • 28
    • 0035984978 scopus 로고    scopus 로고
    • Clinical development of cationic peptides: From natural to novel antibiotics
    • Hancock RE, Patrzykat A: Clinical development of cationic peptides: From natural to novel antibiotics. Curr Drug Targets Infect Disord 2002; 2:79-83
    • (2002) Curr Drug Targets Infect Disord , vol.2 , pp. 79-83
    • Hancock, R.E.1    Patrzykat, A.2
  • 29
    • 0842326097 scopus 로고    scopus 로고
    • Cathelicidins, multifunctional peptides of the innate immunity
    • Zanetti M: Cathelicidins, multifunctional peptides of the innate immunity. J Leuk Biol 2004; 75:39-48
    • (2004) J Leuk Biol , vol.75 , pp. 39-48
    • Zanetti, M.1
  • 30
    • 0028844134 scopus 로고
    • Cathelicidins: A novel protein family with common proregion and a variable C-terminal antimicrobial domain
    • Zanetti M, Gennaro R, Romeo D: Cathelicidins: A novel protein family with common proregion and a variable C-terminal antimicrobial domain. FEBS Lett 1995; 374:1-5
    • (1995) FEBS Lett , vol.374 , pp. 1-5
    • Zanetti, M.1    Gennaro, R.2    Romeo, D.3
  • 31
    • 0033863168 scopus 로고    scopus 로고
    • Structural features and biological activities of the cathelicidin-derived antimicrobial peptides
    • Gennaro R, Zanetti M: Structural features and biological activities of the cathelicidin-derived antimicrobial peptides. Biopolymers 2000; 55:31-49
    • (2000) Biopolymers , vol.55 , pp. 31-49
    • Gennaro, R.1    Zanetti, M.2
  • 32
    • 0036135697 scopus 로고    scopus 로고
    • Cathelicidins: A family of endogenous antimicrobial peptides
    • Lehrer RI, Ganz T: Cathelicidins: A family of endogenous antimicrobial peptides. Curr Opin Hematol 2002; 9:18-22
    • (2002) Curr Opin Hematol , vol.9 , pp. 18-22
    • Lehrer, R.I.1    Ganz, T.2
  • 33
    • 0036252092 scopus 로고    scopus 로고
    • Cationic peptides: Distribution and mechanisms of resistance
    • Devine DA, Hancock RE: Cationic peptides: Distribution and mechanisms of resistance. Curr Pharm Des 2002; 8:703-714
    • (2002) Curr Pharm des , vol.8 , pp. 703-714
    • Devine, D.A.1    Hancock, R.E.2
  • 34
    • 0037392693 scopus 로고    scopus 로고
    • In vitro effect on Cryptosporidium parvum of short-term exposure to cathelicidin peptides
    • Giacometti A, Cirioni O, Del Prete MS, et al: In vitro effect on Cryptosporidium parvum of short-term exposure to cathelicidin peptides. J Antimicrob Chemother 2003; 51:843-847
    • (2003) J Antimicrob Chemother , vol.51 , pp. 843-847
    • Giacometti, A.1    Cirioni, O.2    Del Prete, M.S.3
  • 35
    • 0029961492 scopus 로고    scopus 로고
    • Biological characterization of two novel cathelicidin-derived peptides and identification of structural requirements for their antimicrobial and cell lytic activities
    • Skerlavaj B, Gennaro R, Bagella LL, et al: Biological characterization of two novel cathelicidin-derived peptides and identification of structural requirements for their antimicrobial and cell lytic activities. J Biol Chem 1996; 271:28375-28381
    • (1996) J Biol Chem , vol.271 , pp. 28375-28381
    • Skerlavaj, B.1    Gennaro, R.2    Bagella, L.L.3
  • 36
    • 1042278913 scopus 로고    scopus 로고
    • In vitro and in vivo antimicrobial activity of two alpha-helical cathelicidin peptides and of their synthetic analogs
    • Benincasa M, Skerlavaj B, Gennaro R, et al: In vitro and in vivo antimicrobial activity of two alpha-helical cathelicidin peptides and of their synthetic analogs. Peptides 2003; 24:1723-1731
    • (2003) Peptides , vol.24 , pp. 1723-1731
    • Benincasa, M.1    Skerlavaj, B.2    Gennaro, R.3
  • 37
    • 0036929153 scopus 로고    scopus 로고
    • Comparative in vitro activity of five cathelicidin-derived synthetic peptides against Leptospira, Borrelia and Treponema pallidum
    • Sambri V, Marangoni A, Giacani L, et al: Comparative in vitro activity of five cathelicidin-derived synthetic peptides against Leptospira, Borrelia and Treponema pallidum. J Antimicrob Chemother 2002; 50:895-902
    • (2002) J Antimicrob Chemother , vol.50 , pp. 895-902
    • Sambri, V.1    Marangoni, A.2    Giacani, L.3
  • 38
    • 0024418033 scopus 로고
    • Protein estimation by the product of integrated peak area and flow rate
    • Buck MA, Olah TA, Weitzmann CJ, et al: Protein estimation by the product of integrated peak area and flow rate. Anal Biochem 1989; 182:295-299
    • (1989) Anal Biochem , vol.182 , pp. 295-299
    • Buck, M.A.1    Olah, T.A.2    Weitzmann, C.J.3
  • 39
    • 0014109212 scopus 로고
    • Spectroscopic determination of tryptophan and tyrosine in proteins
    • Edelhoch H: Spectroscopic determination of tryptophan and tyrosine in proteins. Biochemistry 1967; 6:1948-1954
    • (1967) Biochemistry , vol.6 , pp. 1948-1954
    • Edelhoch, H.1
  • 41
    • 0036877034 scopus 로고    scopus 로고
    • The role of bacteriolysis in the pathophysiology of inflammation, infection and post-infectious sequelae
    • Ginsburg I: The role of bacteriolysis in the pathophysiology of inflammation, infection and post-infectious sequelae. APMIS 2002; 110:753-770
    • (2002) APMIS , vol.110 , pp. 753-770
    • Ginsburg, I.1
  • 42
    • 0029001686 scopus 로고
    • Release of tumor necrosis factor alpha and interleukin 6 during antibiotic killing of Escherichia coli in whole blood: Influence of antibiotic class, antibiotic concentration, and presence of septic serum
    • Prins JM, Kuijper EJ, Mevissen MLCM, et al: Release of tumor necrosis factor alpha and interleukin 6 during antibiotic killing of Escherichia coli in whole blood: Influence of antibiotic class, antibiotic concentration, and presence of septic serum. Infect Immun 1995; 63:2236-2242
    • (1995) Infect Immun , vol.63 , pp. 2236-2242
    • Prins, J.M.1    Kuijper, E.J.2    Mlcm, M.3
  • 43
    • 0035663083 scopus 로고    scopus 로고
    • Ceftazidime- and imipenem-induced endotoxin release during treatment of Gram-negative infections
    • Byl B, Clevenbergh P, Kentos A, et al: Ceftazidime- and imipenem-induced endotoxin release during treatment of Gram-negative infections. Eur J Clin Microbiol Infect Dis 2001; 20:804-7
    • (2001) Eur J Clin Microbiol Infect Dis , vol.20 , pp. 804-807
    • Byl, B.1    Clevenbergh, P.2    Kentos, A.3
  • 44
    • 0031728726 scopus 로고    scopus 로고
    • Antibiotic-induced release of lipoteichoic acid and peptidoglycan from Staphylococcus aureus: Quantitative measurements and biological reactivities
    • van Langevel P, van Dissel JT, Ravensbergen E, et al: Antibiotic-induced release of lipoteichoic acid and peptidoglycan from Staphylococcus aureus: Quantitative measurements and biological reactivities. Antimicrob Agents Chemother 1998; 42:3073-3078
    • (1998) Antimicrob Agents Chemother , vol.42 , pp. 3073-3078
    • Van Langevel, P.1    Van Dissel, J.T.2    Ravensbergen, E.3
  • 45
    • 0005413121 scopus 로고
    • Mechanism of action of penicillin: Triggering of the pneumococcal autolytic enzyme by inhibitors of cell wall synthesis
    • Tomasz A, Waks S: Mechanism of action of penicillin: Triggering of the pneumococcal autolytic enzyme by inhibitors of cell wall synthesis. Proc Natl Acad Sci U S A 1975; 72:4162-4166
    • (1975) Proc Natl Acad Sci U S A , vol.72 , pp. 4162-4166
    • Tomasz, A.1    Waks, S.2
  • 46
    • 10744231848 scopus 로고    scopus 로고
    • Mechanism of action of the mannopeptimycins, a novel class of glycopeptide antibiotics active against vancomycin-resistant Gram-positive bacteria
    • Ruzin A, Singh G, Severin A, et al: Mechanism of action of the mannopeptimycins, a novel class of glycopeptide antibiotics active against vancomycin-resistant Gram-positive bacteria. Antimicrob Agents Chemother 2004; 48:728-738
    • (2004) Antimicrob Agents Chemother , vol.48 , pp. 728-738
    • Ruzin, A.1    Singh, G.2    Severin, A.3


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