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Volumn 56, Issue 6, 2012, Pages 3309-3317

Efficacy of OH-CATH30 and its analogs against drug-resistant bacteria in vitro and in mouse models

Author keywords

[No Author keywords available]

Indexed keywords

AMIKACIN; CATHELICIDIN; CATHELICIDIN ANTIMICROBIAL PEPTIDE LL 37; CEFOPERAZONE; CEFTAZIDIME; CYCLOPHOSPHAMIDE; DEXTRO OH CATH; DEXTRO OH CM6; GENTAMICIN; IMIPENEM; LEVOFLOXACIN; OH CATH30; OH CM6; PEXIGANAN; PIPERACILLIN; POLYMYXIN B; UNCLASSIFIED DRUG; VANCOMYCIN;

EID: 84861165882     PISSN: 00664804     EISSN: 10986596     Source Type: Journal    
DOI: 10.1128/AAC.06304-11     Document Type: Article
Times cited : (68)

References (44)
  • 1
    • 0029163069 scopus 로고
    • Liposomal entrapment of the neutrophil-derived peptide indolicidin endows it with in vivo antifungal activity
    • Ahmad I, Perkins WR, Lupan DM, Selsted ME, Janoff AS. 1995. Liposomal entrapment of the neutrophil-derived peptide indolicidin endows it with in vivo antifungal activity. Biochim. Biophys. Acta 1237:109-114.
    • (1995) Biochim. Biophys. Acta , vol.1237 , pp. 109-114
    • Ahmad, I.1    Perkins, W.R.2    Lupan, D.M.3    Selsted, M.E.4    Janoff, A.S.5
  • 2
    • 0942301292 scopus 로고    scopus 로고
    • Antimicrobial Activity and Bacterial-Membrane Interaction of Ovine-Derived Cathelicidins
    • DOI 10.1128/AAC.48.2.673-676.2004
    • Anderson RC, Hancock RE, Yu PL. 2004. Antimicrobial activity and bacterial-membrane interaction of ovine-derived cathelicidins. Antimicrob. Agents Chemother. 48:673-676. (Pubitemid 38141743)
    • (2004) Antimicrobial Agents and Chemotherapy , vol.48 , Issue.2 , pp. 673-676
    • Anderson, R.C.1    Hancock, R.E.W.2    Yu, P.-L.3
  • 3
    • 0038364156 scopus 로고    scopus 로고
    • Cathelicidins - A family of multifunctional antimicrobial peptides
    • DOI 10.1007/s00018-003-2186-9
    • Bals R, Wilson JM. 2003. Cathelicidins-a family of multifunctional antimicrobial peptides. Cell. Mol. Life Sci. 60:711-720. (Pubitemid 36570762)
    • (2003) Cellular and Molecular Life Sciences , vol.60 , Issue.4 , pp. 711-720
    • Bals, R.1    Wilson, J.M.2
  • 4
    • 33846006520 scopus 로고    scopus 로고
    • Fowlicidin-3 is an alpha-helical cationic host defense peptide with potent antibacterial and lipopolysaccharide-neutralizing activities
    • DOI 10.1111/j.1742-4658.2006.05589.x
    • Bommineni YR, et al. 2007. Fowlicidin-3 is an alpha-helical cationic host defense peptide with potent antibacterial and lipopolysaccharideneutralizing activities. FEBS J. 274:418-428. (Pubitemid 46046651)
    • (2007) FEBS Journal , vol.274 , Issue.2 , pp. 418-428
    • Bommineni, Y.R.1    Dai, H.2    Gong, Y.-X.3    Soulages, J.L.4    Fernando, S.C.5    DeSilva, U.6    Prakash, O.7    Zhang, G.8
  • 5
    • 3342965837 scopus 로고    scopus 로고
    • In vitro activity and potency of an intravenously injected antimicrobial peptide and its DL amino acid analog in mice infected with bacteria
    • DOI 10.1128/AAC.48.8.3127-3129.2004
    • Braunstein A, Papo N, Shai Y. 2004. In vitro activity and potency of an intravenously injected antimicrobial peptide and its DL amino acid analog in mice infected with bacteria. Antimicrob. Agents Chemother. 48:3127-3129. (Pubitemid 38989185)
    • (2004) Antimicrobial Agents and Chemotherapy , vol.48 , Issue.8 , pp. 3127-3129
    • Braunstein, A.1    Papo, N.2    Shai, Y.3
  • 6
    • 14544282377 scopus 로고    scopus 로고
    • Antimicrobial peptides: Pore formers or metabolic inhibitors in bacteria?
    • DOI 10.1038/nrmicro1098
    • Brogden KA. 2005. Antimicrobial peptides: pore formers or metabolic inhibitors in bacteria? Nat. Rev. Microbiol. 3:238-250. (Pubitemid 40298223)
    • (2005) Nature Reviews Microbiology , vol.3 , Issue.3 , pp. 238-250
    • Brogden, K.A.1
  • 7
    • 79955527970 scopus 로고    scopus 로고
    • Host defense peptide LL-37 selectively reduces proinflammatory macrophage responses
    • Brown KL, et al. 2011. Host defense peptide LL-37 selectively reduces proinflammatory macrophage responses. J. Immunol. 186:5497-5505.
    • (2011) J. Immunol. , vol.186 , pp. 5497-5505
    • Brown, K.L.1
  • 9
    • 33646452712 scopus 로고    scopus 로고
    • LL-37 protects rats against lethal sepsis caused by gram-negative bacteria
    • Cirioni O, et al. 2006. LL-37 protects rats against lethal sepsis caused by gram-negative bacteria. Antimicrob. Agents Chemother. 50:1672-1679.
    • (2006) Antimicrob. Agents Chemother. , vol.50 , pp. 1672-1679
    • Cirioni, O.1
  • 10
    • 33646696219 scopus 로고    scopus 로고
    • Clinical and Laboratory Standards Institute. 19th informational supplement. M100-S19. CLSI, Wayne, PA
    • Clinical and Laboratory Standards Institute. 2009. Performance standards for antimicrobial susceptibility testing; 19th informational supplement. M100-S19. CLSI, Wayne, PA.
    • (2009) Performance Standards for Antimicrobial Susceptibility Testing
  • 12
    • 69549111337 scopus 로고    scopus 로고
    • Antibiotics for emerging pathogens
    • Fischbach MA, Walsh CT. 2009. Antibiotics for emerging pathogens. Science 325:1089-1093.
    • (2009) Science , vol.325 , pp. 1089-1093
    • Fischbach, M.A.1    Walsh, C.T.2
  • 15
    • 65549168259 scopus 로고    scopus 로고
    • Killing of trypanosomatid parasites by a modified bovine host defense peptide, BMAP-18
    • Haines LR, et al. 2009. Killing of trypanosomatid parasites by a modified bovine host defense peptide, BMAP-18. PLoS Negl. Trop. Dis. 3:e373.
    • (2009) PLoS Negl. Trop. Dis. , vol.3
    • Haines, L.R.1
  • 16
    • 33845699790 scopus 로고    scopus 로고
    • Antimicrobial and host-defense peptides as new anti-infective therapeutic strategies
    • DOI 10.1038/nbt1267, PII NBT1267
    • Hancock RE, Sahl HG. 2006. Antimicrobial and host-defense peptides as new anti-infective therapeutic strategies. Nat. Biotechnol. 24:1551-1557. (Pubitemid 44967479)
    • (2006) Nature Biotechnology , vol.24 , Issue.12 , pp. 1551-1557
    • Hancock, R.E.W.1    Sahl, H.-G.2
  • 17
    • 23444451770 scopus 로고    scopus 로고
    • High-throughput generation of small antibacterial peptides with improved activity
    • DOI 10.1038/nbt1113
    • Hilpert K, Volkmer-Engert R, Walter T, Hancock RE. 2005. Highthroughput generation of small antibacterial peptides with improved activity. Nat. Biotechnol. 23:1008-1012. (Pubitemid 41114036)
    • (2005) Nature Biotechnology , vol.23 , Issue.8 , pp. 1008-1012
    • Hilpert, K.1    Volkmer-Engert, R.2    Walter, T.3    Hancock, R.E.W.4
  • 18
    • 0032992923 scopus 로고    scopus 로고
    • Range of activity and metabolic stability of synthetic antibacterial glycopeptides from insects
    • DOI 10.1016/S0304-4165(98)00169-X, PII S030441659800169X
    • Hoffmann R, Bulet P, Urge L, Otvos L, Jr. 1999. Range of activity and metabolic stability of synthetic antibacterial glycopeptides from insects. Biochim. Biophys. Acta 1426:459-467. (Pubitemid 29078561)
    • (1999) Biochimica et Biophysica Acta - General Subjects , vol.1426 , Issue.3 , pp. 459-467
    • Hoffmann, R.1    Bulet, P.2    Urge, L.3    Otvos Jr., L.4
  • 20
    • 47249135720 scopus 로고    scopus 로고
    • Salt-resistant homodimeric bactenecin, a cathelicidin-derived antimicrobial peptide
    • DOI 10.1111/j.1742-4658.2008.06536.x
    • Lee JY, et al. 2008. Salt-resistant homodimeric bactenecin, a cathelicidinderived antimicrobial peptide. FEBS J. 275:3911-3920. (Pubitemid 351990953)
    • (2008) FEBS Journal , vol.275 , Issue.15 , pp. 3911-3920
    • Lee, J.Y.1    Yang, S.-T.2    Lee, S.K.3    Jung, H.H.4    Shin, S.Y.5    Hahm, K.-S.6    Kim, J.I.7
  • 21
    • 58449085560 scopus 로고    scopus 로고
    • Neutrophils are essential for rapid clearance of Enterococcus faecium in mice
    • Leendertse M, et al. 2009. Neutrophils are essential for rapid clearance of Enterococcus faecium in mice. Infect. Immun. 77:485-491.
    • (2009) Infect. Immun. , vol.77 , pp. 485-491
    • Leendertse, M.1
  • 23
    • 53049110125 scopus 로고    scopus 로고
    • Lipopolysaccharide neutralization by the antibacterial peptide CM4
    • Lin QP, et al. 2008. Lipopolysaccharide neutralization by the antibacterial peptide CM4. Eur. J. Pharmacol. 596:160-165.
    • (2008) Eur. J. Pharmacol. , vol.596 , pp. 160-165
    • Lin, Q.P.1
  • 24
    • 0028954325 scopus 로고
    • Comparison of the up-and-down, conventional LD50, and fixed-dose acute toxicity procedures
    • Lipnick RL, et al. 1995. Comparison of the up-and-down, conventional LD50, and fixed-dose acute toxicity procedures. Food Chem. Toxicol. 33:223-231.
    • (1995) Food Chem. Toxicol. , vol.33 , pp. 223-231
    • Lipnick, R.L.1
  • 25
    • 56749150574 scopus 로고    scopus 로고
    • Topical versus systemic antimicrobial therapy for treating mildly infected diabetic foot ulcers: A randomized, controlled, double-blinded, multicenter trial of pexiganan cream
    • Lipsky BA, Holroyd KJ, Zasloff M. 2008. Topical versus systemic antimicrobial therapy for treating mildly infected diabetic foot ulcers: a randomized, controlled, double-blinded, multicenter trial of pexiganan cream. Clin. Infect. Dis. 47:1537-1545.
    • (2008) Clin. Infect. Dis. , vol.47 , pp. 1537-1545
    • Lipsky, B.A.1    Holroyd, K.J.2    Zasloff, M.3
  • 30
    • 0036736465 scopus 로고    scopus 로고
    • Analysis of the cytotoxicity of synthetic antimicrobial peptides on mouse leucocytes: Implications for systemic use
    • Pacor S, Giangaspero A, Bacac M, Sava G, Tossi A. 2002. Analysis of the cytotoxicity of synthetic antimicrobial peptides on mouse leucocytes: implications for systemic use. J. Antimicrob. Chemother. 50:339-348.
    • (2002) J. Antimicrob. Chemother. , vol.50 , pp. 339-348
    • Pacor, S.1    Giangaspero, A.2    Bacac, M.3    Sava, G.4    Tossi, A.5
  • 32
    • 77953509929 scopus 로고    scopus 로고
    • A miniature mimic of host defense peptides with systemic antibacterial efficacy
    • Sarig H, et al. 2010. A miniature mimic of host defense peptides with systemic antibacterial efficacy. FASEB J. 24:1904-1913.
    • (2010) FASEB J. , vol.24 , pp. 1904-1913
    • Sarig, H.1
  • 33
    • 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
    • DOI 10.1074/jbc.271.45.28375
    • Skerlavaj B, et al. 1996. Biological characterization of two novel cathelicidin-derived peptides and identification of structural requirements for their antimicrobial and cell lytic activities. J. Biol. Chem. 271:28375-28381. (Pubitemid 26374655)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.45 , pp. 28375-28381
    • Skerlavaj, B.1    Gennaro, R.2    Bagella, L.3    Merluzzi, L.4    Risso, A.5    Zanettit, M.6
  • 34
    • 77049098530 scopus 로고    scopus 로고
    • Antimicrobial and membrane disrupting activities of a peptide derived from the human cathelicidin antimicrobial peptide LL37
    • Thennarasu S, et al. 2010. Antimicrobial and membrane disrupting activities of a peptide derived from the human cathelicidin antimicrobial peptide LL37. Biophys. J. 98:248-257.
    • (2010) Biophys. J. , vol.98 , pp. 248-257
    • Thennarasu, S.1
  • 35
    • 70349496543 scopus 로고    scopus 로고
    • New approaches in peptide antibiotics
    • Vaara M. 2009. New approaches in peptide antibiotics. Curr. Opin. Pharmacol. 9:571-576.
    • (2009) Curr. Opin. Pharmacol. , vol.9 , pp. 571-576
    • Vaara, M.1
  • 36
    • 0033151774 scopus 로고    scopus 로고
    • Mechanism of interaction of different classes of cationic antimicrobial peptides with planar bilayers and with the cytoplasmic membrane of Escherichia coli
    • Wu M, Maier E, Benz R, Hancock RE. 1999. Mechanism of interaction of different classes of cationic antimicrobial peptides with planar bilayers and with the cytoplasmic membrane of Escherichia coli. Biochemistry 38:7235-7242.
    • (1999) Biochemistry , vol.38 , pp. 7235-7242
    • Wu, M.1    Maier, E.2    Benz, R.3    Hancock, R.E.4
  • 37
    • 73549104786 scopus 로고    scopus 로고
    • Antimicrobial and immunomodulatory activities of an ovine proline/arginine-rich cathelicidin
    • Yu PL, Cross ML, Haverkamp RG. 2010. Antimicrobial and immunomodulatory activities of an ovine proline/arginine-rich cathelicidin. Int. J. Antimicrob. Agents 35:288-291.
    • (2010) Int. J. Antimicrob. Agents , vol.35 , pp. 288-291
    • Yu, P.L.1    Cross, M.L.2    Haverkamp, R.G.3
  • 38
    • 0842326097 scopus 로고    scopus 로고
    • Cathelicidins, multifunctional peptides of the innate immunity
    • DOI 10.1189/jlb.0403147
    • Zanetti M. 2004. Cathelicidins, multifunctional peptides of the innate immunity. J. Leukoc. Biol. 75:39-48. (Pubitemid 38166778)
    • (2004) Journal of Leukocyte Biology , vol.75 , Issue.1 , pp. 39-48
    • Zanetti, M.1
  • 39
    • 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. 1995. Cathelicidins: a novel protein family with a common proregion and a variable C-terminal antimicrobial domain. FEBS Lett. 374:1-5.
    • (1995) FEBS Lett. , vol.374 , pp. 1-5
    • Zanetti, M.1    Gennaro, R.2    Romeo, D.3
  • 40
    • 0037165196 scopus 로고    scopus 로고
    • Antimicrobial peptides of multicellular organisms
    • DOI 10.1038/415389a
    • Zasloff M. 2002. Antimicrobial peptides of multicellular organisms. Nature 415:389-395. (Pubitemid 34100944)
    • (2002) Nature , vol.415 , Issue.6870 , pp. 389-395
    • Zasloff, M.1
  • 41
    • 35848948624 scopus 로고    scopus 로고
    • Antimicrobial peptides, innate immunity, and the normally sterile urinary tract
    • DOI 10.1681/ASN.2007050611
    • Zasloff M. 2007. Antimicrobial peptides, innate immunity, and the normally sterile urinary tract. J. Am. Soc. Nephrol. 18:2810-2816. (Pubitemid 350058386)
    • (2007) Journal of the American Society of Nephrology , vol.18 , Issue.11 , pp. 2810-2816
    • Zasloff, M.1
  • 43
    • 78249268795 scopus 로고    scopus 로고
    • Structure-function relationship of king cobra cathelicidin
    • Zhang Y, et al. 2010. Structure-function relationship of king cobra cathelicidin. Peptides 31:1488-1493.
    • (2010) Peptides , vol.31 , pp. 1488-1493
    • Zhang, Y.1
  • 44
    • 52049112301 scopus 로고    scopus 로고
    • Identification and characterization of novel reptile cathelicidins from elapid snakes
    • Zhao H, et al. 2008. Identification and characterization of novel reptile cathelicidins from elapid snakes. Peptides 29:1685-1691.
    • (2008) Peptides , vol.29 , pp. 1685-1691
    • Zhao, H.1


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