메뉴 건너뛰기




Volumn 1838, Issue 9, 2014, Pages 2198-2204

Lysylated phospholipids stabilize models of bacterial lipid bilayers and protect against antimicrobial peptides

Author keywords

Aminoacylated lipids; Amphipathic peptides; Antimicrobial peptides; Bacterial lipids; Headgroup modified bacterial lipids; Lysyl PG

Indexed keywords

1 PALMITOYL 2 OLEOYL PHOSPHATIDYLCHOLINE; 1 PALMITOYL 2 OLEOYL PHOSPHATIDYLGLYCEROL; CECROPIN A; GLUTAMINE; LYSINE; MASTOPARAN X; MICROORGANISM PROTEIN; PHOSPHATIDYLCHOLINE; PHOSPHATIDYLETHANOLAMINE; PHOSPHATIDYLGLYCEROL; PHOSPHOLIPID; POLYPEPTIDE ANTIBIOTIC AGENT; UNCLASSIFIED DRUG;

EID: 84903697585     PISSN: 00052736     EISSN: 18792642     Source Type: Journal    
DOI: 10.1016/j.bbamem.2014.04.018     Document Type: Article
Times cited : (37)

References (25)
  • 1
    • 0000420475 scopus 로고
    • Gram-positive bacteria
    • C. Ratledge, S.G. Wilkinson, Academic Press San Diego
    • W.M. OLeary, and S.G. Wilkinson Gram-positive bacteria C. Ratledge, S.G. Wilkinson, Microbial Lipids vol. 1 1988 Academic Press San Diego 117 201
    • (1988) Microbial Lipids , vol.1 , pp. 117-201
    • Oleary, W.M.1    Wilkinson, S.G.2
  • 3
    • 9644266728 scopus 로고    scopus 로고
    • Reduced content of lysyl-phosphatidylglycerol in the cytoplasmic membrane affects susceptibility to moenomycin, as well as vancomycin, gentamicin, and antimicrobial peptides, in Staphylococcus aureus
    • DOI 10.1128/AAC.48.12.4800-4807.2004
    • H. Nishi, H. Komatsuzawa, T. Fujiwara, N. McCallum, and M. Sugai Reduced content of lysyl-phosphatidylglycerol in the cytoplasmic membrane affects susceptibility to moenomycin, as well as vancomycin, gentamicin, and antimicrobial peptides, in Staphylococcus aureus Antimicrob. Agents Chemother. 48 2004 4800 4807 (Pubitemid 39577687)
    • (2004) Antimicrobial Agents and Chemotherapy , vol.48 , Issue.12 , pp. 4800-4807
    • Nishi, H.1    Komatsuzawa, H.2    Fujiwara, T.3    McCallum, N.4    Sugai, M.5
  • 4
    • 84863402669 scopus 로고    scopus 로고
    • LC-MS/MS characterization of phospholipid content in daptomycin- susceptible and -resistant isolates of Staphylococcus aureus with mutations in mprF
    • A. Rubio, J. Moore, M. Varoglu, M. Conrad, M. Chu, W. Shaw, and J.A. Silverman LC-MS/MS characterization of phospholipid content in daptomycin-susceptible and -resistant isolates of Staphylococcus aureus with mutations in mprF Mol. Membr. Biol. 29 2012 1 8
    • (2012) Mol. Membr. Biol. , vol.29 , pp. 1-8
    • Rubio, A.1    Moore, J.2    Varoglu, M.3    Conrad, M.4    Chu, M.5    Shaw, W.6    Silverman, J.A.7
  • 5
    • 84872836267 scopus 로고    scopus 로고
    • Correlation of cell membrane lipid profiles with daptomycin resistance in methicillin-resistant Staphylococcus aureus
    • N.N. Mishra, and A.S. Bayer Correlation of cell membrane lipid profiles with daptomycin resistance in methicillin-resistant Staphylococcus aureus Antimicrob. Agents Chemother. 57 2013 1082 1085
    • (2013) Antimicrob. Agents Chemother. , vol.57 , pp. 1082-1085
    • Mishra, N.N.1    Bayer, A.S.2
  • 6
    • 84880393882 scopus 로고    scopus 로고
    • Interactions of antimicrobial peptides with lipid bilayers
    • L. Tamm, Elsevier B. V.
    • P.F. Almeida, and A. Pokorny Interactions of antimicrobial peptides with lipid bilayers L. Tamm, Comprehensive Biophysics vol. 5 2012 Elsevier B. V. 189 222
    • (2012) Comprehensive Biophysics , vol.5 VOL. , pp. 189-222
    • Almeida, P.F.1    Pokorny, A.2
  • 7
    • 84887665716 scopus 로고    scopus 로고
    • Translocation of cationic amphipathic peptides across the membranes of pure phospholipid giant vesicles
    • S.A. Wheaten, F.D. Ablan, B.L. Spaller, J.M. Trieu, and P.F. Almeida Translocation of cationic amphipathic peptides across the membranes of pure phospholipid giant vesicles J. Am. Chem. Soc. 135 2013 16517 16525
    • (2013) J. Am. Chem. Soc. , vol.135 , pp. 16517-16525
    • Wheaten, S.A.1    Ablan, F.D.2    Spaller, B.L.3    Trieu, J.M.4    Almeida, P.F.5
  • 9
    • 0019386682 scopus 로고
    • Sequence and specificity of two antibacterial proteins involved in insect immunity
    • DOI 10.1038/292246a0
    • H. Steiner, D. Hultmark, A. Engström, H. Bennich, and H.G. Boman Sequence and specificity of two antibacterial proteins involved in insect immunity Nature 292 1981 246 248 (Pubitemid 11001840)
    • (1981) Nature , vol.292 , Issue.5820 , pp. 246-248
    • Steiner, H.1    Hultmark, D.2    Engstrom, A.3
  • 10
    • 0020621396 scopus 로고
    • Conformational change of mastoparan from wasp venom on binding with phospholipid membrane
    • DOI 10.1016/0014-5793(83)80385-8
    • T. Higashijima, K. Wakamatsu, M. Takemitsu, M. Fujino, T. Nakajima, and T. Miyazawa Conformational change of mastoparan from wasp venom on binding with phospholipid membrane FEBS Lett. 152 1983 227 230 (Pubitemid 13129700)
    • (1983) FEBS Letters , vol.152 , Issue.2 , pp. 227-230
    • Higashijima, T.1    Wakamatsu, K.2    Takemitsu, M.3
  • 11
    • 0033864862 scopus 로고    scopus 로고
    • Amphipathic, alpha-helical antimicrobial peptides
    • A. Tossi, L. Sandri, and A. Giangaspero Amphipathic, alpha-helical antimicrobial peptides Biopolymers 55 2000 4 30
    • (2000) Biopolymers , vol.55 , pp. 4-30
    • Tossi, A.1    Sandri, L.2    Giangaspero, A.3
  • 12
    • 44049085333 scopus 로고    scopus 로고
    • Structure and thermotropic behavior of the Staphylococcus aureus lipid lysyl-dipalmitoylphosphatidylglycerol
    • S. Danner, G. Pabst, K. Lohner, and A. Hickel Structure and thermotropic behavior of the Staphylococcus aureus lipid lysyl- dipalmitoylphosphatidylglycerol Biophys. J. 94 2008 2150 2159
    • (2008) Biophys. J. , vol.94 , pp. 2150-2159
    • Danner, S.1    Pabst, G.2    Lohner, K.3    Hickel, A.4
  • 13
    • 58149286266 scopus 로고    scopus 로고
    • The activity of the amphipathic peptide delta-lysin correlates with phospholipid acyl chain structure and bilayer elastic properties
    • A. Pokorny, E.M. Kilelee, D. Wu, and P.F. Almeida The activity of the amphipathic peptide delta-lysin correlates with phospholipid acyl chain structure and bilayer elastic properties Biophys. J. 95 2008 4748 4755
    • (2008) Biophys. J. , vol.95 , pp. 4748-4755
    • Pokorny, A.1    Kilelee, E.M.2    Wu, D.3    Almeida, P.F.4
  • 14
    • 40149107726 scopus 로고    scopus 로고
    • A quantitative model for the all-or-none permeabilization of phospholipid vesicles by the antimicrobial peptide cecropin A
    • S.M. Gregory, A.C. Cavenaugh, V. Journigan, A. Pokorny, and P.F.F. Almeida A quantitative model for the all-or-none permeabilization of phospholipid vesicles by the antimicrobial peptide cecropin A Biophys. J. 94 2008 1667 1680
    • (2008) Biophys. J. , vol.94 , pp. 1667-1680
    • Gregory, S.M.1    Cavenaugh, A.C.2    Journigan, V.3    Pokorny, A.4    Almeida, P.F.F.5
  • 16
    • 78651157652 scopus 로고
    • A simple, specific spray for the detection of phospholipids on thin layer chromatograms
    • J.C. Dittmer, and R.L. Lester A simple, specific spray for the detection of phospholipids on thin layer chromatograms J. Lipid Res. 5 1964 126 127
    • (1964) J. Lipid Res. , vol.5 , pp. 126-127
    • Dittmer, J.C.1    Lester, R.L.2
  • 17
    • 0018763612 scopus 로고
    • Modification of the Dittmer-Lester reagent for the detection of phospholipid derivatives on thin-layer chromatograms
    • E.K. Ryu, and M. MacCoss Modification of the Dittmer-Lester reagent for the detection of phospholipid derivatives on thin-layer chromatograms J. Lipid Res. 20 1979 561 563 (Pubitemid 9215384)
    • (1979) Journal of Lipid Research , vol.20 , Issue.4 , pp. 561-563
    • Ryu, E.K.1    MacCoss, M.2
  • 18
    • 70449246528 scopus 로고
    • Phosphorous assay in column chromatography
    • G.R. Bartlett Phosphorous assay in column chromatography J. Biol. Chem. 234 1959 466 468
    • (1959) J. Biol. Chem. , vol.234 , pp. 466-468
    • Bartlett, G.R.1
  • 19
    • 0036712127 scopus 로고    scopus 로고
    • Mechanism and kinetics of δ-lysin interaction with phospholipid vesicles
    • DOI 10.1021/bi020244r
    • A. Pokorny, T.H. Birkbeck, and P.F.F. Almeida Mechanism and kinetics of delta-lysin interaction with phospholipid vesicles Biochemistry 41 2002 11044 11056 (Pubitemid 35001219)
    • (2002) Biochemistry , vol.41 , Issue.36 , pp. 11044-11056
    • Pokorny, A.1    Birkbeck, T.H.2    Almeida, P.F.F.3
  • 20
    • 77950492687 scopus 로고    scopus 로고
    • Binding and permeabilization of model membranes by amphipathic peptides
    • P.F. Almeida, and A. Pokorny Binding and permeabilization of model membranes by amphipathic peptides Methods Mol. Biol. 618 2010 155 169
    • (2010) Methods Mol. Biol. , vol.618 , pp. 155-169
    • Almeida, P.F.1    Pokorny, A.2
  • 21
    • 77957330217 scopus 로고    scopus 로고
    • Lysyl-phosphatidylglycerol attenuates membrane perturbation rather than surface association of the cationic antimicrobial peptide 6W-RP-1 in a model membrane system: Implicationsfor daptomycin resistance
    • E. Kilelee, A. Pokorny, M.R. Yeaman, and A.S. Bayer Lysyl- phosphatidylglycerol attenuates membrane perturbation rather than surface association of the cationic antimicrobial peptide 6W-RP-1 in a model membrane system: implicationsfor daptomycin resistance Antimicrob. Agents Chemother. 54 2010 4476 4479
    • (2010) Antimicrob. Agents Chemother. , vol.54 , pp. 4476-4479
    • Kilelee, E.1    Pokorny, A.2    Yeaman, M.R.3    Bayer, A.S.4
  • 22
    • 0000394858 scopus 로고
    • Percolation properties of random ellipses
    • W. Xia, and M.F. Thorpe Percolation properties of random ellipses Phys. Rev. A 38 1988 2650 2656
    • (1988) Phys. Rev. A , vol.38 , pp. 2650-2656
    • Xia, W.1    Thorpe, M.F.2
  • 23
    • 0036787584 scopus 로고    scopus 로고
    • Intramembrane electrostatic interactions destabilize lipid vesicles
    • S.D. Shoemaker, and T.K. Vanderlick Intramembrane electrostatic interactions destabilize lipid vesicles Biophys. J. 83 2002 2007 2014
    • (2002) Biophys. J. , vol.83 , pp. 2007-2014
    • Shoemaker, S.D.1    Vanderlick, T.K.2
  • 24
    • 0038778549 scopus 로고    scopus 로고
    • Evidence for membrane thinning effect as the mechanism for peptide-induced pore formation
    • F.Y. Chen, M.T. Lee, and H.W. Huang Evidence for membrane thinning effect as the mechanism for peptide-induced pore formation Biophys. J. 84 2003 3751 3758 (Pubitemid 36637870)
    • (2003) Biophysical Journal , vol.84 , Issue.6 , pp. 3751-3758
    • Chen, F.-Y.1    Lee, M.-T.2    Huang, H.W.3
  • 25
    • 0141865601 scopus 로고    scopus 로고
    • Dynamic tension spectroscopy and strength of biomembranes
    • E. Evans, V. Heinrich, F. Ludwig, and W. Rawicz Dynamic tension spectroscopy and strength of biomembranes Biophys. J. 85 2003 2342 2350 (Pubitemid 37210784)
    • (2003) Biophysical Journal , vol.85 , Issue.4 , pp. 2342-2350
    • Evans, E.1    Heinrich, V.2    Ludwig, F.3    Rawicz, W.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.