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Volumn 188, Issue 1, 2003, Pages 146-152

Killing of African trypanosomes by antimicrobial peptides

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA DEFENSIN; ANTIINFECTIVE AGENT; BETA DEFENSIN; CATHELICIDIN; NOVISPIRIN; OVISPIRIN; PROINTEGRIN 1; SMAP 29 PROTEIN; UNCLASSIFIED DRUG;

EID: 0037560074     PISSN: 00221899     EISSN: None     Source Type: Journal    
DOI: 10.1086/375747     Document Type: Article
Times cited : (105)

References (42)
  • 1
    • 0029051685 scopus 로고
    • Defensins and other endogenous peptide antibiotics of vertebrates
    • Martin E, Ganz T, Lehrer RI. Defensins and other endogenous peptide antibiotics of vertebrates. J Leukoc Biol 1995; 58:128-36.
    • (1995) J Leukoc Biol , vol.58 , pp. 128-136
    • Martin, E.1    Ganz, T.2    Lehrer, R.I.3
  • 3
    • 0033067196 scopus 로고    scopus 로고
    • Antimicrobial peptides in mammalian and insect host defence
    • Lehrer RI, Ganz T. Antimicrobial peptides in mammalian and insect host defence. Curr Opin Immunol 1999; 11:23-7.
    • (1999) Curr Opin Immunol , vol.11 , pp. 23-27
    • Lehrer, R.I.1    Ganz, T.2
  • 4
    • 0022402545 scopus 로고
    • Defensins: Natural peptide antibiotics of human neutrophils
    • Ganz T, Selsted ME, Szklarek D, et al. Defensins: natural peptide antibiotics of human neutrophils. J Clin Invest 1985; 76:1427-35.
    • (1985) J Clin Invest , vol.76 , pp. 1427-1435
    • Ganz, T.1    Selsted, M.E.2    Szklarek, D.3
  • 5
    • 0035877995 scopus 로고    scopus 로고
    • Human cathelicidin, hCAP-18, is processed to the antimicrobial peptide LL-37 by extracellular cleavage with proteinase 3
    • Sorensen OE, Follin P, Johnsen AH, et al. Human cathelicidin, hCAP-18, is processed to the antimicrobial peptide LL-37 by extracellular cleavage with proteinase 3. Blood 2001; 97:3951-9.
    • (2001) Blood , vol.97 , pp. 3951-3959
    • Sorensen, O.E.1    Follin, P.2    Johnsen, A.H.3
  • 6
    • 0028844134 scopus 로고
    • Cathelicidins: A novel protein family with a common proregion and a variable C-terminal antimicrobial domain
    • Zanetti M, Gennaro R, Romeo D. Cathelicidins: a novel protein family with a 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
  • 8
    • 0024391711 scopus 로고
    • Interaction of human defensins with Escherichia coli: Mechanism of bactericidal activity
    • Lehrer RI, Barton A, Daher KA, Harwig SS, Ganz T, Selsted ME. Interaction of human defensins with Escherichia coli: mechanism of bactericidal activity. J Clin Invest 1989; 84:553-61.
    • (1989) J Clin Invest , vol.84 , pp. 553-561
    • Lehrer, R.I.1    Barton, A.2    Daher, K.A.3    Harwig, S.S.4    Ganz, T.5    Selsted, M.E.6
  • 9
    • 0032457643 scopus 로고    scopus 로고
    • Control and surveillance of African trypanosomiasis: Report of a WHO expert committee
    • World Health Organization (WHO). Control and surveillance of African trypanosomiasis: report of a WHO expert committee. World Health Organ Tech Rep Ser 1998; 881:1-114.
    • (1998) World Health Organ Tech Rep Ser , vol.881 , pp. 1-114
  • 10
    • 0026519361 scopus 로고
    • Molecular biology of African trypanosomes: Development of new strategies to combat an old disease
    • Hajduk S, Adler B, Bertrand K, et al. Molecular biology of African trypanosomes: development of new strategies to combat an old disease. Am J Med Sci 1992; 303:258-70.
    • (1992) Am J Med Sci , vol.303 , pp. 258-270
    • Hajduk, S.1    Adler, B.2    Bertrand, K.3
  • 11
    • 0018096718 scopus 로고
    • Antigenic variation in trypanosomes
    • Vickerman K. Antigenic variation in trypanosomes. Nature 1978; 273:613-7.
    • (1978) Nature , vol.273 , pp. 613-617
    • Vickerman, K.1
  • 13
    • 0035201134 scopus 로고    scopus 로고
    • New drugs for the treatment of human African trypanosomiasis: Research and development
    • Keiser J, Stich A, Burri C. New drugs for the treatment of human African trypanosomiasis: research and development. Trends Parasitol 2001; 17:42-9.
    • (2001) Trends Parasitol , vol.17 , pp. 42-49
    • Keiser, J.1    Stich, A.2    Burri, C.3
  • 14
    • 0018601361 scopus 로고
    • Cultivation and in vitro cloning or procyclic culture forms of Trypanosoma brucei in a semi-defined medium
    • Brun R, Schonenberger. Cultivation and in vitro cloning or procyclic culture forms of Trypanosoma brucei in a semi-defined medium. Acta Trop 1979; 36:289-92.
    • (1979) Acta Trop , vol.36 , pp. 289-292
    • Brun, R.1    Schonenberger2
  • 15
    • 0031083414 scopus 로고    scopus 로고
    • Short communication: Cultivation of bloodstream forms of Trypanosoma brucei and T. evansi in a serum-free medium
    • Hirumi H, Martin S, Hirumi K, et al. Short communication: cultivation of bloodstream forms of Trypanosoma brucei and T. evansi in a serum-free medium. Trop Med Int Health 1997; 2:240-4.
    • (1997) Trop Med Int Health , vol.2 , pp. 240-244
    • Hirumi, H.1    Martin, S.2    Hirumi, K.3
  • 16
    • 0025020371 scopus 로고
    • A modified colorimetric assay of macrophage activation for intracellular cytotoxicity against Leishmania parasites
    • Kiderlen AF, Kaye PM. A modified colorimetric assay of macrophage activation for intracellular cytotoxicity against Leishmania parasites. J Immunol Methods 1990; 127:11-8.
    • (1990) J Immunol Methods , vol.127 , pp. 11-18
    • Kiderlen, A.F.1    Kaye, P.M.2
  • 17
    • 0032721183 scopus 로고    scopus 로고
    • Peptide localization and gene structure of cryptdin 4, a differentially expressed mouse paneth cell alpha-defensin
    • Ouellette AJ, Darmoul D, Tran D, Huttner KM, Yuan J, Selsted ME. Peptide localization and gene structure of cryptdin 4, a differentially expressed mouse paneth cell alpha-defensin. Infect Immun 1999; 67:6643-51.
    • (1999) Infect Immun , vol.67 , pp. 6643-6651
    • Ouellette, A.J.1    Darmoul, D.2    Tran, D.3    Huttner, K.M.4    Yuan, J.5    Selsted, M.E.6
  • 18
    • 0035799314 scopus 로고    scopus 로고
    • The NMR structure of human β-defensin-2 reveals a novel α-helical segment
    • Sawai MV, Jia HP, Liu L, et al. The NMR structure of human β-defensin-2 reveals a novel α-helical segment. Biochemistry 2001; 40:3810-6.
    • (2001) Biochemistry , vol.40 , pp. 3810-3816
    • Sawai, M.V.1    Jia, H.P.2    Liu, L.3
  • 19
    • 0037040913 scopus 로고    scopus 로고
    • The solution structures of the human beta-defensins lead to a better understanding of the potent bactericidal activity of HBD3 against Staphylococcus aureus
    • Schibli DJ, Hunter HN, Aseyev V, et al. The solution structures of the human beta-defensins lead to a better understanding of the potent bactericidal activity of HBD3 against Staphylococcus aureus. J Biol Chem 2002; 277:8279-89.
    • (2002) J Biol Chem , vol.277 , pp. 8279-8289
    • Schibli, D.J.1    Hunter, H.N.2    Aseyev, V.3
  • 20
    • 0036095738 scopus 로고    scopus 로고
    • Activity of novispirin G10 against Pseudomonas aeruginosa in vitro and in infected burns
    • Steinstraesser L, Tack BF, Waring AJ, et al. Activity of novispirin G10 against Pseudomonas aeruginosa in vitro and in infected burns. Antimicrob Agents Chemother 2002; 46:1837-44.
    • (2002) Antimicrob Agents Chemother , vol.46 , pp. 1837-1844
    • Steinstraesser, L.1    Tack, B.F.2    Waring, A.J.3
  • 21
    • 0031690986 scopus 로고    scopus 로고
    • TcDJ1, a putatitve mitochondrial DnaJ protein in Trypanosoma cruzi
    • Carreira MAC, Tibbetts RS, Olson CL, et al. TcDJ1, a putatitve mitochondrial DnaJ protein in Trypanosoma cruzi. FEMS Microbiol Lett 1998; 166:141-6.
    • (1998) FEMS Microbiol Lett , vol.166 , pp. 141-146
    • Carreira, M.A.C.1    Tibbetts, R.S.2    Olson, C.L.3
  • 22
    • 0034721784 scopus 로고    scopus 로고
    • Characterization of luminal paneth cell alpha-defensins in mouse small intestine: Attenuated antimicrobial activities of peptides with truncated amino termini
    • Ouellette AJ, Satchell DP, Hsieh MM, Hagen SJ, Selsted ME. Characterization of luminal paneth cell alpha-defensins in mouse small intestine: attenuated antimicrobial activities of peptides with truncated amino termini. J Biol Chem 2000; 275:33969-73.
    • (2000) J Biol Chem , vol.275 , pp. 33969-33973
    • Ouellette, A.J.1    Satchell, D.P.2    Hsieh, M.M.3    Hagen, S.J.4    Selsted, M.E.5
  • 23
    • 0034721859 scopus 로고    scopus 로고
    • A novel murine beta-defensin expressed in tongue, esophagus, and trachea
    • Jia HP, Wowk SA, Schutte BC, et al. A novel murine beta-defensin expressed in tongue, esophagus, and trachea. J Biol Chem 2000; 275:33314-20.
    • (2000) J Biol Chem , vol.275 , pp. 33314-33320
    • Jia, H.P.1    Wowk, S.A.2    Schutte, B.C.3
  • 24
    • 0034098916 scopus 로고    scopus 로고
    • Bactericidal activity of mammalian cathelicidin-derived peptides
    • Travis SM, Anderson NN, Forsyth WR, et al. Bactericidal activity of mammalian cathelicidin-derived peptides. Infect Immun 2000; 68:2748-55.
    • (2000) Infect Immun , vol.68 , pp. 2748-2755
    • Travis, S.M.1    Anderson, N.N.2    Forsyth, W.R.3
  • 25
    • 0028263457 scopus 로고
    • Identification of a new member of the protegrin family by cDNA cloning
    • Zhao C, Liu L, Lehrer RI. Identification of a new member of the protegrin family by cDNA cloning. FEBS Lett 1994; 346:285-8.
    • (1994) FEBS Lett , vol.346 , pp. 285-288
    • Zhao, C.1    Liu, L.2    Lehrer, R.I.3
  • 26
    • 0030855146 scopus 로고    scopus 로고
    • Protegrin-1: A broad-spectrum, rapidly microbicidal peptide with in vivo activity
    • Steinberg DA, Hurst MA, Fujii CA, et al. Protegrin-1: a broad-spectrum, rapidly microbicidal peptide with in vivo activity. Antimicrob Agents Chemother 1997; 41:1738-42.
    • (1997) Antimicrob Agents Chemother , vol.41 , pp. 1738-1742
    • Steinberg, D.A.1    Hurst, M.A.2    Fujii, C.A.3
  • 27
    • 0031034840 scopus 로고    scopus 로고
    • Differential scanning microcalorimetry indicates that human defensin, HNP-2, interacts specifically with biomembrane mimetic systems
    • Lohner K, Latal A, Lehrer RI, Ganz T. Differential scanning microcalorimetry indicates that human defensin, HNP-2, interacts specifically with biomembrane mimetic systems. Biochemistry 1997; 36:1525-31.
    • (1997) Biochemistry , vol.36 , pp. 1525-1531
    • Lohner, K.1    Latal, A.2    Lehrer, R.I.3    Ganz, T.4
  • 28
    • 0032536098 scopus 로고    scopus 로고
    • Oligomerization of protegrin-1 in the presence of DPC micelles: A proton high-resolution NMR study
    • Roumestand C, Louis V, Aumelas A, Grassy G, Calas B, Chavanieu A. Oligomerization of protegrin-1 in the presence of DPC micelles: a proton high-resolution NMR study. FEBS Lett 1998; 421:263-7.
    • (1998) FEBS Lett , vol.421 , pp. 263-267
    • Roumestand, C.1    Louis, V.2    Aumelas, A.3    Grassy, G.4    Calas, B.5    Chavanieu, A.6
  • 29
    • 0030043634 scopus 로고    scopus 로고
    • In vitro activity, of the antimicrobial peptides human and rabbit defensins and porcine leukocyte protegrin against Mycobacterium tuberculosis
    • Miyakawa Y, Ratnakar P, Rao AG, et al. In vitro activity, of the antimicrobial peptides human and rabbit defensins and porcine leukocyte protegrin against Mycobacterium tuberculosis. Infect Immun 1996; 64:926-32.
    • (1996) Infect Immun , vol.64 , pp. 926-932
    • Miyakawa, Y.1    Ratnakar, P.2    Rao, A.G.3
  • 30
    • 0031686776 scopus 로고    scopus 로고
    • Activities of LL-37, a cathelin-associated antimicrobial peptide of human neutrophils
    • Turner J, Cho Y, Dinh NN, Waring AJ, Lehrer RI. Activities of LL-37, a cathelin-associated antimicrobial peptide of human neutrophils. Antimicrob Agents Chemother 1998; 42:2206-14.
    • (1998) Antimicrob Agents Chemother , vol.42 , pp. 2206-2214
    • Turner, J.1    Cho, Y.2    Dinh, N.N.3    Waring, A.J.4    Lehrer, R.I.5
  • 31
    • 0033798839 scopus 로고    scopus 로고
    • Crystallization of antimicrobial pores in membranes: Magainin and protegrin
    • Yang L, Weiss TM, Lehrer RI, Huang HW. Crystallization of antimicrobial pores in membranes: magainin and protegrin. Biophys J 2000; 79:2002-9.
    • (2000) Biophys J , vol.79 , pp. 2002-2009
    • Yang, L.1    Weiss, T.M.2    Lehrer, R.I.3    Huang, H.W.4
  • 32
    • 0020655657 scopus 로고
    • The membrane form of variant surface glycoproteins of Trypanosoma brucei
    • Cardoso de Almeida ML, Turner MJ. The membrane form of variant surface glycoproteins of Trypanosoma brucei. Nature 1983; 302:349-52.
    • (1983) Nature , vol.302 , pp. 349-352
    • Cardoso De Almeida, M.L.1    Turner, M.J.2
  • 33
    • 0023138615 scopus 로고
    • Decay-accelerating factor (DAF) shares a common carbohydrate determinant with the variant surface glycoprotein (VSG) of the African Trypanosoma brucei
    • Davitz MA, Gurnett AM, Low MG, Turner MJ, Nussenzweig V. Decay-accelerating factor (DAF) shares a common carbohydrate determinant with the variant surface glycoprotein (VSG) of the African Trypanosoma brucei. J Immunol 1987; 138:520-3.
    • (1987) J Immunol , vol.138 , pp. 520-523
    • Davitz, M.A.1    Gurnett, A.M.2    Low, M.G.3    Turner, M.J.4    Nussenzweig, V.5
  • 34
    • 0033569874 scopus 로고    scopus 로고
    • The procyclin repertoire of Trypanosoma brucei: Identification and structural characterization of the Glu-Pro-rich polypeptides
    • Acosta-Serrano A, Cole RN, Mehlert A, Lee MG, Ferguson MA, Englund PT. The procyclin repertoire of Trypanosoma brucei: identification and structural characterization of the Glu-Pro-rich polypeptides. J Biol Chem 1999; 274:29763-71.
    • (1999) J Biol Chem , vol.274 , pp. 29763-29771
    • Acosta-Serrano, A.1    Cole, R.N.2    Mehlert, A.3    Lee, M.G.4    Ferguson, M.A.5    Englund, P.T.6
  • 35
    • 0029924103 scopus 로고    scopus 로고
    • Change in membrane permeability induced by protegrin 1: Implication of disulphide bridges for pore formation
    • Mangoni ME, Aumelas A, Charnet P, et al. Change in membrane permeability induced by protegrin 1: implication of disulphide bridges for pore formation. FEBS Lett 1996; 383:93-8.
    • (1996) FEBS Lett , vol.383 , pp. 93-98
    • Mangoni, M.E.1    Aumelas, A.2    Charnet, P.3
  • 36
    • 0026657783 scopus 로고
    • Developmental variation of glycosylphosphatidylinositol membrane anchors in Trypanosoma brucei: In vitro biosynthesis of intermediates in the construction of the GPI anchor of the major procyclic surface glycoprotein
    • Field MC, Menon AK, Cross GA. Developmental variation of glycosylphosphatidylinositol membrane anchors in Trypanosoma brucei: in vitro biosynthesis of intermediates in the construction of the GPI anchor of the major procyclic surface glycoprotein. J Biol Chem 1992; 267:5324-9.
    • (1992) J Biol Chem , vol.267 , pp. 5324-5329
    • Field, M.C.1    Menon, A.K.2    Cross, G.A.3
  • 37
    • 0024519464 scopus 로고
    • Solution structure of the glycosylphosphatidylinositol membrane anchor glycan of Trypanosoma brucei variant surface glycoprotein
    • Homans SW, Edge CJ, Ferguson MA, Dwek RA, Rademacher TW. Solution structure of the glycosylphosphatidylinositol membrane anchor glycan of Trypanosoma brucei variant surface glycoprotein. Biochemistry 1989; 28:2881-7.
    • (1989) Biochemistry , vol.28 , pp. 2881-2887
    • Homans, S.W.1    Edge, C.J.2    Ferguson, M.A.3    Dwek, R.A.4    Rademacher, T.W.5
  • 38
    • 0030742660 scopus 로고    scopus 로고
    • Expression of a variant surface glycoprotein of Trypanosoma gambiense in procyclic forms of Trypanosoma brucei shows that the cell type dictates the nature of the glycosylphosphatidylinositol membrane anchor attached to the glycoprotein
    • Paturiaux-Hanocq F, Zitzmann N, Hanocq-Quertier J, et al. Expression of a variant surface glycoprotein of Trypanosoma gambiense in procyclic forms of Trypanosoma brucei shows that the cell type dictates the nature of the glycosylphosphatidylinositol membrane anchor attached to the glycoprotein. Biochem J 1997; 324:885-95.
    • (1997) Biochem J , vol.324 , pp. 885-895
    • Paturiaux-Hanocq, F.1    Zitzmann, N.2    Hanocq-Quertier, J.3
  • 39
    • 0034775142 scopus 로고    scopus 로고
    • Susceptibilities of oral bacteria and yeast to mammalian cathelicidins
    • Guthmiller JM, Vargas KG, Srikantha R, et al. Susceptibilities of oral bacteria and yeast to mammalian cathelicidins. Antimicrob Agents Chemother 2001; 45:3216-9.
    • (2001) Antimicrob Agents Chemother , vol.45 , pp. 3216-3219
    • Guthmiller, J.M.1    Vargas, K.G.2    Srikantha, R.3
  • 41
    • 0037308713 scopus 로고    scopus 로고
    • NK-lysin and its shortened analog NK-2 exhibit potent activities against Trypanosoma cruzi
    • Jacobs T, Bruhn H, Gaworski I, Fleischer B, Leippe M. NK-lysin and its shortened analog NK-2 exhibit potent activities against Trypanosoma cruzi. Antimicrob Agents Chemother 2003; 47:607-13.
    • (2003) Antimicrob Agents Chemother , vol.47 , pp. 607-613
    • Jacobs, T.1    Bruhn, H.2    Gaworski, I.3    Fleischer, B.4    Leippe, M.5
  • 42
    • 0037147330 scopus 로고    scopus 로고
    • Dermaseptins from Phyllomedusa oreades and Phyllomedusa distincta: Anti- Trypanosoma cruzi activity without cytotoxicity to mammalian cells
    • Brand GD, Leite JR, Silva LP, et al. Dermaseptins from Phyllomedusa oreades and Phyllomedusa distincta: anti- Trypanosoma cruzi activity without cytotoxicity to mammalian cells. J Biol Chem 2002; 277:49332-40.
    • (2002) J Biol Chem , vol.277 , pp. 49332-49340
    • Brand, G.D.1    Leite, J.R.2    Silva, L.P.3


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