메뉴 건너뛰기




Volumn 94, Issue 6, 2014, Pages 678-689

Cationic amphipathic D-enantiomeric antimicrobial peptides with in vitro and ex vivo activity against drug-resistant Mycobacterium tuberculosis

Author keywords

Antimicrobial peptides; Clinical isolates; Isoniazid; Multi drug resistant; THP 1; Tuberculosis

Indexed keywords

AGAR; D LAK 120; D LAK 120 A; D LAK 120 AP13; D LAK 120 H; D LAK 120 HP13; D LAK 120 P13; DEXTRO AMINO ACID; ISONIAZID; POLYPEPTIDE ANTIBIOTIC AGENT; UNCLASSIFIED DRUG; ANTIMICROBIAL CATIONIC PEPTIDE; TUBERCULOSTATIC AGENT;

EID: 84919460794     PISSN: 14729792     EISSN: 1873281X     Source Type: Journal    
DOI: 10.1016/j.tube.2014.08.001     Document Type: Article
Times cited : (44)

References (42)
  • 3
    • 0030063866 scopus 로고    scopus 로고
    • Immunopathology of tuberculosis: Roles of macrophages and monocytes
    • M.J. Fenton, and M.W. Vermeulen Immunopathology of tuberculosis: roles of macrophages and monocytes Infect Immun 64 1996 683 690
    • (1996) Infect Immun , vol.64 , pp. 683-690
    • Fenton, M.J.1    Vermeulen, M.W.2
  • 4
    • 0033043776 scopus 로고    scopus 로고
    • Survival of Mycobacterium avium and Mycobacterium tuberculosis in acidified vacuoles of murine macrophages
    • M.S. Gomes, S. Paul, A.L. Moreira, R. Appelberg, M. Rabinovitch, and G. Kaplan Survival of Mycobacterium avium and Mycobacterium tuberculosis in acidified vacuoles of murine macrophages Infect Immun 67 1999 3199 3206
    • (1999) Infect Immun , vol.67 , pp. 3199-3206
    • Gomes, M.S.1    Paul, S.2    Moreira, A.L.3    Appelberg, R.4    Rabinovitch, M.5    Kaplan, G.6
  • 5
    • 44649128524 scopus 로고    scopus 로고
    • Mycobacterium tuberculosis and the macrophage: Maintaining a balance
    • J. Pieters Mycobacterium tuberculosis and the macrophage: maintaining a balance Cell Host Microbe 3 2008 399 407
    • (2008) Cell Host Microbe , vol.3 , pp. 399-407
    • Pieters, J.1
  • 6
    • 80052050200 scopus 로고    scopus 로고
    • Importance of phagosomal functionality for growth restriction of Mycobacterium tuberculosis in primary human macrophages
    • A. Welin, J. Raffetseder, D. Eklund, O. Stendahl, and M. Lerm Importance of phagosomal functionality for growth restriction of Mycobacterium tuberculosis in primary human macrophages J Innate Immun 3 2011 508 518
    • (2011) J Innate Immun , vol.3 , pp. 508-518
    • Welin, A.1    Raffetseder, J.2    Eklund, D.3    Stendahl, O.4    Lerm, M.5
  • 7
    • 84867259108 scopus 로고    scopus 로고
    • Conformational flexibility determines selectivity and antibacterial, antiplasmodial, and anticancer potency of cationic alpha-helical peptides
    • L.S. Vermeer, Y. Lan, V. Abbate, E. Ruh, T.T. Bui, and L.J. Wilkinson Conformational flexibility determines selectivity and antibacterial, antiplasmodial, and anticancer potency of cationic alpha-helical peptides J Biol Chem 287 2012 34120 34133
    • (2012) J Biol Chem , vol.287 , pp. 34120-34133
    • Vermeer, L.S.1    Lan, Y.2    Abbate, V.3    Ruh, E.4    Bui, T.T.5    Wilkinson, L.J.6
  • 8
    • 79951634149 scopus 로고    scopus 로고
    • Anti-tuberculosis activity of alpha-helical antimicrobial peptides: De novo designed L- and D-enantiomers versus L- and D-LL-37
    • Z. Jiang, M.P. Higgins, J. Whitehurst, K.O. Kisich, M.I. Voskuil, and R.S. Hodges Anti-tuberculosis activity of alpha-helical antimicrobial peptides: de novo designed L- and D-enantiomers versus L- and D-LL-37 Protein Peptide Lett 18 2011 241 252
    • (2011) Protein Peptide Lett , vol.18 , pp. 241-252
    • Jiang, Z.1    Higgins, M.P.2    Whitehurst, J.3    Kisich, K.O.4    Voskuil, M.I.5    Hodges, R.S.6
  • 9
    • 52049122588 scopus 로고    scopus 로고
    • Role of antimicrobial peptides in host defense against mycobacterial infections
    • P. Mendez-Samperio Role of antimicrobial peptides in host defense against mycobacterial infections Peptides 29 2008 1836 1841
    • (2008) Peptides , vol.29 , pp. 1836-1841
    • Mendez-Samperio, P.1
  • 10
    • 48549100053 scopus 로고    scopus 로고
    • Human macrophage host defense against Mycobacterium tuberculosis
    • P.T. Liu, and R.L. Modlin Human macrophage host defense against Mycobacterium tuberculosis Curr Opin Immunol 20 2008 371 376
    • (2008) Curr Opin Immunol , vol.20 , pp. 371-376
    • Liu, P.T.1    Modlin, R.L.2
  • 11
    • 78449236736 scopus 로고    scopus 로고
    • Antimicrobial peptides: Primeval molecules or future drugs?
    • B.M. Peters, M.E. Shirtliff, and M.A. Jabra-Rizk Antimicrobial peptides: primeval molecules or future drugs? PLoS Pathog 6 2010 e1001067
    • (2010) PLoS Pathog , vol.6 , pp. 1001067
    • Peters, B.M.1    Shirtliff, M.E.2    Jabra-Rizk, M.A.3
  • 12
    • 0037165196 scopus 로고    scopus 로고
    • Antimicrobial peptides of multicellular organisms
    • M. Zasloff Antimicrobial peptides of multicellular organisms Nature 415 2002 389 395
    • (2002) Nature , vol.415 , pp. 389-395
    • Zasloff, M.1
  • 13
    • 14544282377 scopus 로고    scopus 로고
    • Antimicrobial peptides: Pore formers or metabolic inhibitors in bacteria?
    • K.A. Brogden Antimicrobial peptides: pore formers or metabolic inhibitors in bacteria? Nat Rev Microbiol 3 2005 238 250
    • (2005) Nat Rev Microbiol , vol.3 , pp. 238-250
    • Brogden, K.A.1
  • 14
    • 60749118913 scopus 로고    scopus 로고
    • Antimicrobial peptides: Linking partition, activity and high membrane-bound concentrations
    • M.N. Melo, R. Ferre, and M.A. Castanho Antimicrobial peptides: linking partition, activity and high membrane-bound concentrations Nat Rev Microbiol 7 2009 245 250
    • (2009) Nat Rev Microbiol , vol.7 , pp. 245-250
    • Melo, M.N.1    Ferre, R.2    Castanho, M.A.3
  • 15
    • 70350435548 scopus 로고    scopus 로고
    • Multifunctional host defense peptides: Intracellular-targeting antimicrobial peptides
    • P. Nicolas Multifunctional host defense peptides: intracellular-targeting antimicrobial peptides FEBS J 276 2009 6483 6496
    • (2009) FEBS J , vol.276 , pp. 6483-6496
    • Nicolas, P.1
  • 16
    • 0344418718 scopus 로고    scopus 로고
    • Effect of D-amino acid substitution on the stability, the secondary structure, and the activity of membrane-active peptide
    • S.Y. Hong, J.E. Oh, and K.H. Lee Effect of D-amino acid substitution on the stability, the secondary structure, and the activity of membrane-active peptide Biochem Pharmacol 58 1999 1775 1780
    • (1999) Biochem Pharmacol , vol.58 , pp. 1775-1780
    • Hong, S.Y.1    Oh, J.E.2    Lee, K.H.3
  • 17
    • 84870202424 scopus 로고    scopus 로고
    • The effect of d-amino acid substitution on the selectivity of temporin L towards target cells: Identification of a potent anti-Candida peptide
    • P. Grieco, A. Carotenuto, L. Auriemma, M.R. Saviello, P. Campiglia, and I.M. Gomez-Monterrey The effect of d-amino acid substitution on the selectivity of temporin L towards target cells: identification of a potent anti-Candida peptide Biochim Biophys Acta 1828 2013 652 660
    • (2013) Biochim Biophys Acta , vol.1828 , pp. 652-660
    • Grieco, P.1    Carotenuto, A.2    Auriemma, L.3    Saviello, M.R.4    Campiglia, P.5    Gomez-Monterrey, I.M.6
  • 18
    • 0347635410 scopus 로고    scopus 로고
    • Effects of L- or D-Pro incorporation into hydrophobic or hydrophilic helix face of amphipathic alpha-helical model peptide on structure and cell selectivity
    • Y.M. Song, S.T. Yang, S.S. Lim, Y. Kim, K.S. Hahm, and J.I. Kim Effects of L- or D-Pro incorporation into hydrophobic or hydrophilic helix face of amphipathic alpha-helical model peptide on structure and cell selectivity Biochem Biophys Res Commun 314 2004 615 621
    • (2004) Biochem Biophys Res Commun , vol.314 , pp. 615-621
    • Song, Y.M.1    Yang, S.T.2    Lim, S.S.3    Kim, Y.4    Hahm, K.S.5    Kim, J.I.6
  • 19
    • 33747432947 scopus 로고    scopus 로고
    • Contribution of a central proline in model amphipathic alpha-helical peptides to self-association, interaction with phospholipids, and antimicrobial mode of action
    • S.T. Yang, J.Y. Lee, H.J. Kim, Y.J. Eu, S.Y. Shin, and K.S. Hahm Contribution of a central proline in model amphipathic alpha-helical peptides to self-association, interaction with phospholipids, and antimicrobial mode of action FEBS J 273 2006 4040 4054
    • (2006) FEBS J , vol.273 , pp. 4040-4054
    • Yang, S.T.1    Lee, J.Y.2    Kim, H.J.3    Eu, Y.J.4    Shin, S.Y.5    Hahm, K.S.6
  • 20
    • 3042737036 scopus 로고    scopus 로고
    • In vitro activity of protegrin-1 and beta-defensin-1, alone and in combination with isoniazid, against Mycobacterium tuberculosis
    • L. Fattorini, R. Gennaro, M. Zanetti, D. Tan, L. Brunori, and F. Giannoni In vitro activity of protegrin-1 and beta-defensin-1, alone and in combination with isoniazid, against Mycobacterium tuberculosis Peptides 25 2004 1075 1077
    • (2004) Peptides , vol.25 , pp. 1075-1077
    • Fattorini, L.1    Gennaro, R.2    Zanetti, M.3    Tan, D.4    Brunori, L.5    Giannoni, F.6
  • 21
    • 4944264473 scopus 로고    scopus 로고
    • Role of human neutrophil peptide-1 as a possible adjunct to antituberculosis chemotherapy
    • A. Kalita, I. Verma, and G.K. Khuller Role of human neutrophil peptide-1 as a possible adjunct to antituberculosis chemotherapy J Infect Dis 190 2004 1476 1480
    • (2004) J Infect Dis , vol.190 , pp. 1476-1480
    • Kalita, A.1    Verma, I.2    Khuller, G.K.3
  • 22
    • 0035477536 scopus 로고    scopus 로고
    • Mycobacterium smegmatis: An absurd model for tuberculosis?
    • J.M. Reyrat, and D. Kahn Mycobacterium smegmatis: an absurd model for tuberculosis? Trends Microbiol 9 2001 472 474
    • (2001) Trends Microbiol , vol.9 , pp. 472-474
    • Reyrat, J.M.1    Kahn, D.2
  • 23
    • 42149102918 scopus 로고    scopus 로고
    • Insights from the complete genome sequence of Mycobacterium marinum on the evolution of Mycobacterium tuberculosis
    • T.P. Stinear, T. Seemann, P.F. Harrison, G.A. Jenkin, J.K. Davies, and P.D. Johnson Insights from the complete genome sequence of Mycobacterium marinum on the evolution of Mycobacterium tuberculosis Genome Res 18 2008 729 741
    • (2008) Genome Res , vol.18 , pp. 729-741
    • Stinear, T.P.1    Seemann, T.2    Harrison, P.F.3    Jenkin, G.A.4    Davies, J.K.5    Johnson, P.D.6
  • 24
    • 35549008076 scopus 로고    scopus 로고
    • Molecular characterization of clinical isolates of Mycobacterium tuberculosis and their association with phenotypic virulence in human macrophages
    • K.C. Wong, W.M. Leong, H.K. Law, K.F. Ip, J.T. Lam, and K.Y. Yuen Molecular characterization of clinical isolates of Mycobacterium tuberculosis and their association with phenotypic virulence in human macrophages Clin Vacc Immunol CVI 14 2007 1279 1284
    • (2007) Clin Vacc Immunol CVI , vol.14 , pp. 1279-1284
    • Wong, K.C.1    Leong, W.M.2    Law, H.K.3    Ip, K.F.4    Lam, J.T.5    Yuen, K.Y.6
  • 25
    • 0028061607 scopus 로고
    • Mycobacterial cell wall: Structure and role in natural resistance to antibiotics
    • V. Jarlier, and H. Nikaido Mycobacterial cell wall: structure and role in natural resistance to antibiotics FEMS Microbiol Lett 123 1994 11 18
    • (1994) FEMS Microbiol Lett , vol.123 , pp. 11-18
    • Jarlier, V.1    Nikaido, H.2
  • 26
    • 0030070034 scopus 로고    scopus 로고
    • Identification of the surface-exposed lipids on the cell envelopes of Mycobacterium tuberculosis and other mycobacterial species
    • A. Ortalo-Magne, A. Lemassu, M.A. Laneelle, F. Bardou, G. Silve, and P. Gounon Identification of the surface-exposed lipids on the cell envelopes of Mycobacterium tuberculosis and other mycobacterial species J Bacteriol 178 1996 456 461
    • (1996) J Bacteriol , vol.178 , pp. 456-461
    • Ortalo-Magne, A.1    Lemassu, A.2    Laneelle, M.A.3    Bardou, F.4    Silve, G.5    Gounon, P.6
  • 28
    • 73649107809 scopus 로고    scopus 로고
    • Infectiousness, reproductive fitness and evolution of drug-resistant Mycobacterium tuberculosis
    • S. Borrell, and S. Gagneux Infectiousness, reproductive fitness and evolution of drug-resistant Mycobacterium tuberculosis Int J Tuberc Lung Dis Off J Int Union Against Tuberc Lung Dis 13 2009 1456 1466
    • (2009) Int J Tuberc Lung Dis off J Int Union Against Tuberc Lung Dis , vol.13 , pp. 1456-1466
    • Borrell, S.1    Gagneux, S.2
  • 29
    • 0032466234 scopus 로고    scopus 로고
    • Molecular genetic basis of antimicrobial agent resistance in Mycobacterium tuberculosis: 1998 update
    • S. Ramaswamy, and J.M. Musser Molecular genetic basis of antimicrobial agent resistance in Mycobacterium tuberculosis: 1998 update Tuber Lung Dis Off J Int Union Against Tuberc Lung Dis 79 1998 3 29
    • (1998) Tuber Lung Dis off J Int Union Against Tuberc Lung Dis , vol.79 , pp. 3-29
    • Ramaswamy, S.1    Musser, J.M.2
  • 31
    • 33847719510 scopus 로고    scopus 로고
    • From magic bullets back to the magic mountain: The rise of extensively drug-resistant tuberculosis
    • S.E. Dorman, and R.E. Chaisson From magic bullets back to the magic mountain: the rise of extensively drug-resistant tuberculosis Nat Med 13 2007 295 298
    • (2007) Nat Med , vol.13 , pp. 295-298
    • Dorman, S.E.1    Chaisson, R.E.2
  • 32
    • 69249187769 scopus 로고    scopus 로고
    • Chapter 2: Biogenesis of the cell wall and other glycoconjugates of Mycobacterium tuberculosis
    • D. Kaur, M.E. Guerin, H. Skovierova, P.J. Brennan, and M. Jackson Chapter 2: Biogenesis of the cell wall and other glycoconjugates of Mycobacterium tuberculosis Adv Appl Microbiol 69 2009 23 78
    • (2009) Adv Appl Microbiol , vol.69 , pp. 23-78
    • Kaur, D.1    Guerin, M.E.2    Skovierova, H.3    Brennan, P.J.4    Jackson, M.5
  • 33
    • 0037305003 scopus 로고    scopus 로고
    • Human eosinophil peroxidase induces surface alteration, killing, and lysis of Mycobacterium tuberculosis
    • V. Borelli, F. Vita, S. Shankar, M.R. Soranzo, E. Banfi, and G. Scialino Human eosinophil peroxidase induces surface alteration, killing, and lysis of Mycobacterium tuberculosis Infect Immun 71 2003 605 613
    • (2003) Infect Immun , vol.71 , pp. 605-613
    • Borelli, V.1    Vita, F.2    Shankar, S.3    Soranzo, M.R.4    Banfi, E.5    Scialino, G.6
  • 36
    • 67649231146 scopus 로고    scopus 로고
    • Differences in cell wall thickness between resistant and nonresistant strains of Mycobacterium tuberculosis: Using transmission electron microscopy
    • A.A. Velayati, P. Farnia, T.A. Ibrahim, R.Z. Haroun, H.O. Kuan, and J. Ghanavi Differences in cell wall thickness between resistant and nonresistant strains of Mycobacterium tuberculosis: using transmission electron microscopy Chemotherapy 55 2009 303 307
    • (2009) Chemotherapy , vol.55 , pp. 303-307
    • Velayati, A.A.1    Farnia, P.2    Ibrahim, T.A.3    Haroun, R.Z.4    Kuan, H.O.5    Ghanavi, J.6
  • 37
    • 0025010163 scopus 로고
    • Action of 1-isonicotinyl-2-palmitoyl hydrazine against the Mycobacterium avium complex and enhancement of its activity by m-fluorophenylalanine
    • N. Rastogi, and K.S. Goh Action of 1-isonicotinyl-2-palmitoyl hydrazine against the Mycobacterium avium complex and enhancement of its activity by m-fluorophenylalanine Antimicrob Agents Chemother 34 1990 2061 2064
    • (1990) Antimicrob Agents Chemother , vol.34 , pp. 2061-2064
    • Rastogi, N.1    Goh, K.S.2
  • 38
    • 77951216667 scopus 로고    scopus 로고
    • Identification of katG mutations associated with high-level isoniazid resistance in Mycobacterium tuberculosis
    • H. Ando, Y. Kondo, T. Suetake, E. Toyota, S. Kato, and T. Mori Identification of katG mutations associated with high-level isoniazid resistance in Mycobacterium tuberculosis Antimicrob Agents Chemother 54 2010 1793 1799
    • (2010) Antimicrob Agents Chemother , vol.54 , pp. 1793-1799
    • Ando, H.1    Kondo, Y.2    Suetake, T.3    Toyota, E.4    Kato, S.5    Mori, T.6
  • 39
    • 0030042509 scopus 로고    scopus 로고
    • Characterization of the catalase-peroxidase gene (katG) and inhA locus in isoniazid-resistant and -susceptible strains of Mycobacterium tuberculosis by automated DNA sequencing: Restricted array of mutations associated with drug resistance
    • J.M. Musser, V. Kapur, D.L. Williams, B.N. Kreiswirth, D. van Soolingen, and J.D. van Embden Characterization of the catalase-peroxidase gene (katG) and inhA locus in isoniazid-resistant and -susceptible strains of Mycobacterium tuberculosis by automated DNA sequencing: restricted array of mutations associated with drug resistance J Infect Dis 173 1996 196 202
    • (1996) J Infect Dis , vol.173 , pp. 196-202
    • Musser, J.M.1    Kapur, V.2    Williams, D.L.3    Kreiswirth, B.N.4    Van Soolingen, D.5    Van Embden, J.D.6
  • 42
    • 77955872446 scopus 로고    scopus 로고
    • Best drug treatment for multidrug-resistant and extensively drug-resistant tuberculosis
    • J.A. Caminero, G. Sotgiu, A. Zumla, and G.B. Migliori Best drug treatment for multidrug-resistant and extensively drug-resistant tuberculosis Lancet Infect Dis 10 2010 621 629
    • (2010) Lancet Infect Dis , vol.10 , pp. 621-629
    • Caminero, J.A.1    Sotgiu, G.2    Zumla, A.3    Migliori, G.B.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.