메뉴 건너뛰기




Volumn 23, Issue 9, 2017, Pages 676.e1-676.e5

Cross-resistance to human cationic antimicrobial peptides and to polymyxins mediated by the plasmid-encoded MCR-1?

Author keywords

colistin; defensins; Enterobacteriaceae; Escherichia coli; Klebsiella pneumoniae; MCR 1

Indexed keywords

ALPHA DEFENSIN; ALPHA DEFENSIN 5; BETA DEFENSIN 3; CATHELICIDIN ANTIMICROBIAL PEPTIDE LL 37; CATIONIC ANTIMICROBIAL PEPTIDE; COLISTIN; ETHANOLAMINE PHOSPHOTRANSFERASE; LIPOPOLYSACCHARIDE; POLYMYXIN; POLYPEPTIDE ANTIBIOTIC AGENT; UNCLASSIFIED DRUG; ANTIMICROBIAL CATIONIC PEPTIDE; ESCHERICHIA COLI PROTEIN; MCR-1 PROTEIN, E COLI;

EID: 85019110992     PISSN: 1198743X     EISSN: 14690691     Source Type: Journal    
DOI: 10.1016/j.cmi.2017.03.015     Document Type: Article
Times cited : (25)

References (20)
  • 1
    • 36448983944 scopus 로고    scopus 로고
    • Polymyxin B for the treatment of multidrug-resistant pathogens: a critical review
    • Zavascki, A.P., Goldani, L.Z., Li, J., Nation, R.L., Polymyxin B for the treatment of multidrug-resistant pathogens: a critical review. J Antimicrob Chemother 60 (2007), 1206–1215.
    • (2007) J Antimicrob Chemother , vol.60 , pp. 1206-1215
    • Zavascki, A.P.1    Goldani, L.Z.2    Li, J.3    Nation, R.L.4
  • 2
    • 84926336172 scopus 로고    scopus 로고
    • Colistin, mechanisms and prevalence of resistance
    • Bialvaei, A.Z., Samadi Kafil, H., Colistin, mechanisms and prevalence of resistance. Curr Med Res Opin 31 (2015), 707–721.
    • (2015) Curr Med Res Opin , vol.31 , pp. 707-721
    • Bialvaei, A.Z.1    Samadi Kafil, H.2
  • 3
    • 85019777142 scopus 로고    scopus 로고
    • Mechanisms of antimicrobial peptide resistance in Gram-negative bacteria
    • Band, V.I., Weiss, D.S., Mechanisms of antimicrobial peptide resistance in Gram-negative bacteria. Antibiotics 4 (2015), 18–41.
    • (2015) Antibiotics , vol.4 , pp. 18-41
    • Band, V.I.1    Weiss, D.S.2
  • 4
    • 84957433508 scopus 로고    scopus 로고
    • Emergence of plasmid-mediated colistin resistance mechanism MCR-1 in animals and human beings in China: a microbiological and molecular biological study
    • Liu, Y.Y., Wang, Y., Walsh, T.R., Yi, L.X., Zhang, R., Spencer, J., et al. Emergence of plasmid-mediated colistin resistance mechanism MCR-1 in animals and human beings in China: a microbiological and molecular biological study. Lancet Infect Dis 16 (2016), 161–168.
    • (2016) Lancet Infect Dis , vol.16 , pp. 161-168
    • Liu, Y.Y.1    Wang, Y.2    Walsh, T.R.3    Yi, L.X.4    Zhang, R.5    Spencer, J.6
  • 5
    • 84969512848 scopus 로고    scopus 로고
    • Plasmid-mediated colistin resistance; an additional antibiotic resistance menace
    • Nordmann, P., Poirel, L., Plasmid-mediated colistin resistance; an additional antibiotic resistance menace. Clin Microbiol Infect 22 (2016), 398–400.
    • (2016) Clin Microbiol Infect , vol.22 , pp. 398-400
    • Nordmann, P.1    Poirel, L.2
  • 6
    • 0034283216 scopus 로고    scopus 로고
    • The role of cationic antimicrobial peptides in innate host defences
    • Hancock, R.E.W., Diamond, G., The role of cationic antimicrobial peptides in innate host defences. Trends Microbiol 8 (2000), 402–410.
    • (2000) Trends Microbiol , vol.8 , pp. 402-410
    • Hancock, R.E.W.1    Diamond, G.2
  • 7
    • 84966441152 scopus 로고    scopus 로고
    • Mechanisms and consequence of bacterial resistance of antimicrobial peptides
    • Andersson, D.I., Hughes, D., Kubicek-Sutherland, J.Z., Mechanisms and consequence of bacterial resistance of antimicrobial peptides. Drug Resist Updat 26 (2016), 43–57.
    • (2016) Drug Resist Updat , vol.26 , pp. 43-57
    • Andersson, D.I.1    Hughes, D.2    Kubicek-Sutherland, J.Z.3
  • 8
    • 84879590434 scopus 로고    scopus 로고
    • Clinical use of colistin induces cross-resistance to host antimicrobials in Acinetobacter baumannii
    • e00021–13
    • Napier, B.A., Burd, E.M., Satola, S.W., Cagle, S.M., Ray, S.M., McGann, P., et al. Clinical use of colistin induces cross-resistance to host antimicrobials in Acinetobacter baumannii. mBio, 4, 2013 e00021–13.
    • (2013) mBio , vol.4
    • Napier, B.A.1    Burd, E.M.2    Satola, S.W.3    Cagle, S.M.4    Ray, S.M.5    McGann, P.6
  • 9
    • 84930678870 scopus 로고    scopus 로고
    • Phosphoethanolamine transferase LptA in Haemophilus ducreyi modifies lipid A and contributes to human defensin resistance in vitro
    • Trombley, M.P., Post, D.M.B., Rinker, S.D., Reinders, L.M., Fortney, K.R., Zwickl, B.W., et al. Phosphoethanolamine transferase LptA in Haemophilus ducreyi modifies lipid A and contributes to human defensin resistance in vitro. PLoS One, 10, 2015, e0124373.
    • (2015) PLoS One , vol.10 , pp. e0124373
    • Trombley, M.P.1    Post, D.M.B.2    Rinker, S.D.3    Reinders, L.M.4    Fortney, K.R.5    Zwickl, B.W.6
  • 10
    • 84856258886 scopus 로고    scopus 로고
    • Characterization of unique modification of flagellar rod protein FlgG by Campylobacter jejuni/lipidA phosphoethanolamine transferase, linking bacterial locomotion and antimicrobial peptide resistance
    • Cullen, T.W., Madsen, J.A., Ivanov, P.L., Brodbelt, J.S., Trent, M.S., Characterization of unique modification of flagellar rod protein FlgG by Campylobacter jejuni/lipidA phosphoethanolamine transferase, linking bacterial locomotion and antimicrobial peptide resistance. J Biol Chem 287 (2012), 3326–3336.
    • (2012) J Biol Chem , vol.287 , pp. 3326-3336
    • Cullen, T.W.1    Madsen, J.A.2    Ivanov, P.L.3    Brodbelt, J.S.4    Trent, M.S.5
  • 11
    • 77049098530 scopus 로고    scopus 로고
    • Antimicrobial and membrane disrupting activities of a peptide derived from the human cathelicidin antimicrobial peptide LL37
    • Thennarasu, S., Tan, A., Penumatchu, R., Shelburne, C.E., Heyl, D.L., Ramamoorthy, A., Antimicrobial and membrane disrupting activities of a peptide derived from the human cathelicidin antimicrobial peptide LL37. Biophys J 98 (2010), 248–257.
    • (2010) Biophys J , vol.98 , pp. 248-257
    • Thennarasu, S.1    Tan, A.2    Penumatchu, R.3    Shelburne, C.E.4    Heyl, D.L.5    Ramamoorthy, A.6
  • 12
    • 84871027267 scopus 로고    scopus 로고
    • A comprehensive summary of LL-37, the factoctum human cathelicidin peptide
    • Vandamme, D., Landuyt, B., Luyten, W., Schoofs, L., A comprehensive summary of LL-37, the factoctum human cathelicidin peptide. Cell Immunol 280 (2012), 22–35.
    • (2012) Cell Immunol , vol.280 , pp. 22-35
    • Vandamme, D.1    Landuyt, B.2    Luyten, W.3    Schoofs, L.4
  • 13
    • 33749006591 scopus 로고    scopus 로고
    • The human beta-defensin-3, an antibacterial peptide with multiple biological functions
    • Dhople, V., Krukemeyer, A., Ramamoorthy, A., The human beta-defensin-3, an antibacterial peptide with multiple biological functions. Biochim Biophys Acta – Biomembranes 1758 (2006), 1499–1512.
    • (2006) Biochim Biophys Acta – Biomembranes , vol.1758 , pp. 1499-1512
    • Dhople, V.1    Krukemeyer, A.2    Ramamoorthy, A.3
  • 14
    • 84977103302 scopus 로고    scopus 로고
    • Genetic features of MCR-1-producing colistin-resistant Escherichia coli isolates, South Africa
    • Poirel, L., Kieffer, N., Brink, A., Coetze, J., Jayol, A., Nordmann, P., Genetic features of MCR-1-producing colistin-resistant Escherichia coli isolates, South Africa. Antimicrob Agents Chemother 60 (2016), 4394–4397.
    • (2016) Antimicrob Agents Chemother , vol.60 , pp. 4394-4397
    • Poirel, L.1    Kieffer, N.2    Brink, A.3    Coetze, J.4    Jayol, A.5    Nordmann, P.6
  • 15
    • 84964956378 scopus 로고    scopus 로고
    • A universal culture medium for screening polymyxin-resistant Gram-negative isolates
    • Nordmann, P., Jayol, A., Poirel, L., A universal culture medium for screening polymyxin-resistant Gram-negative isolates. J Clin Microbiol 54 (2016), 1395–1399.
    • (2016) J Clin Microbiol , vol.54 , pp. 1395-1399
    • Nordmann, P.1    Jayol, A.2    Poirel, L.3
  • 16
  • 17
    • 79958055551 scopus 로고    scopus 로고
    • Deletion of mtrC in Haemophilus ducreyi increases sensitivity to human antimicrobial peptides and activates the CpxRA regulon
    • Rinker, S.D., Trombley, M.P., Gu, X.P., Fortney, K.R., Bauer, M.E., Deletion of mtrC in Haemophilus ducreyi increases sensitivity to human antimicrobial peptides and activates the CpxRA regulon. Infect Immunity 79 (2011), 2324–2334.
    • (2011) Infect Immunity , vol.79 , pp. 2324-2334
    • Rinker, S.D.1    Trombley, M.P.2    Gu, X.P.3    Fortney, K.R.4    Bauer, M.E.5
  • 18
    • 77957874402 scopus 로고    scopus 로고
    • Breakpoints tables for interpretation of MICs and zone diameters, Version 2.0: The Committee
    • European Committee on Antimicrobial Susceptibility Testing (EUCAST), Breakpoints tables for interpretation of MICs and zone diameters, Version 2.0: The Committee. 2014.
    • (2014)
  • 19
    • 84994399644 scopus 로고    scopus 로고
    • Cathelicidin antimicrobial peptides with reduced activation of Toll-like receptor signaling have potent bactericidal activity against colistin-resistant bacteria
    • e01418–16
    • Kao, C., Lin, X., Yi, G., Zhang, Y., Rowe-Magnus, D.A., Bush, K., Cathelicidin antimicrobial peptides with reduced activation of Toll-like receptor signaling have potent bactericidal activity against colistin-resistant bacteria. mBio, 7, 2016 e01418–16.
    • (2016) mBio , vol.7
    • Kao, C.1    Lin, X.2    Yi, G.3    Zhang, Y.4    Rowe-Magnus, D.A.5    Bush, K.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.