메뉴 건너뛰기




Volumn 59, Issue 9, 2015, Pages 5641-5646

Pyoverdine and proteases affect the response of pseudomonas aeruginosa to gallium in human serum

Author keywords

[No Author keywords available]

Indexed keywords

CASAMINO ACID; GALLIUM NITRATE; IRON; IRON BINDING PROTEIN; PLASMA PROTEIN; PROTEINASE; PYOVERDINE; ANTIINFECTIVE AGENT; GALLIUM; OLIGOPEPTIDE; PEPTIDE HYDROLASE;

EID: 84940936646     PISSN: 00664804     EISSN: 10986596     Source Type: Journal    
DOI: 10.1128/AAC.01097-15     Document Type: Article
Times cited : (32)

References (44)
  • 1
    • 67349234858 scopus 로고    scopus 로고
    • Iron availability and infection
    • Weinberg ED. 2009. Iron availability and infection. Biochim Biophys Acta 1790:600-605. http://dx.doi.org/10.1016/j.bbagen.2008.07.002.
    • (2009) Biochim Biophys Acta , vol.1790 , pp. 600-605
    • Weinberg, E.D.1
  • 2
    • 0037317173 scopus 로고    scopus 로고
    • Acquisition of siderophores in gram-negative bacteria
    • Faraldo-Gómez JD, Sansom MS. 2003. Acquisition of siderophores in gram-negative bacteria. Nat Rev Mol Cell Biol 4:105-116. http://dx.doi .org/10.1038/nrm1015.
    • (2003) Nat Rev Mol Cell Biol , vol.4 , pp. 105-116
    • Faraldo-Gómez, J.D.1    Sansom, M.S.2
  • 3
    • 9244234392 scopus 로고    scopus 로고
    • Bacterial iron sources: From siderophores to hemophores
    • Wandersman C, Delepelaire P. 2004. Bacterial iron sources: from siderophores to hemophores. Annu Rev Microbiol 58:611-647. http://dx.doi .org/10.1146/annurev.micro.58.030603.123811.
    • (2004) Annu Rev Microbiol , vol.58 , pp. 611-647
    • Wandersman, C.1    Delepelaire, P.2
  • 4
    • 0023947089 scopus 로고
    • Impact of proteases on iron uptake of Pseudomonas aeruginosa pyoverdin from transferrin and lactoferrin
    • Döring G, Pfestorf M, Botzenhart K, Abdallah MA. 1988. Impact of proteases on iron uptake of Pseudomonas aeruginosa pyoverdin from transferrin and lactoferrin. Infect Immun 56:291-293.
    • (1988) Infect Immun , vol.56 , pp. 291-293
    • Döring, G.1    Pfestorf, M.2    Botzenhart, K.3    Abdallah, M.A.4
  • 5
    • 84865529072 scopus 로고    scopus 로고
    • Targeting iron assimilation to develop new antibacterials
    • Foley TL, Simeonov A. 2012. Targeting iron assimilation to develop new antibacterials. Expert Opin Drug Discov 7:831-847. http://dx.doi.org/10 .1517/17460441.2012.708335.
    • (2012) Expert Opin Drug Discov , vol.7 , pp. 831-847
    • Foley, T.L.1    Simeonov, A.2
  • 7
    • 0032445152 scopus 로고    scopus 로고
    • Mechanisms of therapeutic activity for gallium
    • Bernstein LR. 1998. Mechanisms of therapeutic activity for gallium. Pharmacol Rev 50:665-682.
    • (1998) Pharmacol Rev , vol.50 , pp. 665-682
    • Bernstein, L.R.1
  • 8
    • 34147096980 scopus 로고    scopus 로고
    • The transition metal gallium disrupts Pseudomonas aeruginosa iron metabolism and has antimicrobial and antibiofilm activity
    • Kaneko Y, Thoendel M, Olakanmi O, Britigan BE, Singh PK. 2007. The transition metal gallium disrupts Pseudomonas aeruginosa iron metabolism and has antimicrobial and antibiofilm activity. J Clin Invest 117:877-888. http://dx.doi.org/10.1172/JCI30783.
    • (2007) J Clin Invest , vol.117 , pp. 877-888
    • Kaneko, Y.1    Thoendel, M.2    Olakanmi, O.3    Britigan, B.E.4    Singh, P.K.5
  • 11
    • 84899503151 scopus 로고    scopus 로고
    • Promises and failures of gallium as an antibacterial agent
    • Minandri F, Bonchi C, Frangipani E, Imperi F, Visca P. 2014. Promises and failures of gallium as an antibacterial agent. Future Microbiol 9:379-397. http://dx.doi.org/10.2217/fmb.14.3.
    • (2014) Future Microbiol , vol.9 , pp. 379-397
    • Minandri, F.1    Bonchi, C.2    Frangipani, E.3    Imperi, F.4    Visca, P.5
  • 14
    • 84902553986 scopus 로고    scopus 로고
    • Repurposing of gallium-based drugs for antibacterial therapy
    • Bonchi C, Imperi F, Minandri F, Visca P, Frangipani E. 2014. Repurposing of gallium-based drugs for antibacterial therapy. Biofactors 40: 303-312. http://dx.doi.org/10.1002/biof.1159.
    • (2014) Biofactors , vol.40 , pp. 303-312
    • Bonchi, C.1    Imperi, F.2    Minandri, F.3    Visca, P.4    Frangipani, E.5
  • 17
    • 0027484113 scopus 로고
    • Iron-regulated salicylate synthesis by Pseudomonas spp
    • Visca P, Ciervo A, Sanfilippo V, Orsi N. 1993. Iron-regulated salicylate synthesis by Pseudomonas spp. J Gen Microbiol 139:1995-2001. http://dx .doi.org/10.1099/00221287-139-9-1995.
    • (1993) J Gen Microbiol , vol.139 , pp. 1995-2001
    • Visca, P.1    Ciervo, A.2    Sanfilippo, V.3    Orsi, N.4
  • 18
    • 84868012115 scopus 로고    scopus 로고
    • In vitro and in vivo antimicrobial activities of gallium nitrate against multidrug-resistant Acinetobacter baumannii
    • Antunes LC, Imperi F, Minandri F, Visca P. 2012. In vitro and in vivo antimicrobial activities of gallium nitrate against multidrug-resistant Acinetobacter baumannii. Antimicrob Agents Chemother 56:5961-5970. http://dx.doi.org/10.1128/AAC.01519-12.
    • (2012) Antimicrob Agents Chemother , vol.56 , pp. 5961-5970
    • Antunes, L.C.1    Imperi, F.2    Minandri, F.3    Visca, P.4
  • 19
    • 73949146114 scopus 로고    scopus 로고
    • Molecular basis of pyoverdine siderophore recycling in Pseudomonas aeruginosa
    • Imperi F, Tiburzi F, Visca P. 2009. Molecular basis of pyoverdine siderophore recycling in Pseudomonas aeruginosa. Proc Natl Acad SciUSA 106:20440-20445. http://dx.doi.org/10.1073/pnas.0908760106.
    • (2009) Proc Natl Acad SciUSA , vol.106 , pp. 20440-20445
    • Imperi, F.1    Tiburzi, F.2    Visca, P.3
  • 20
    • 0031026355 scopus 로고    scopus 로고
    • Use of siderophores to type pseudomonads: The three Pseudomonas aeruginosa pyoverdine systems
    • Meyer JM, Stintzi A, De Vos D, Cornelis P, Tappe R, Taraz K, Budzikiewicz H. 1997. Use of siderophores to type pseudomonads: the three Pseudomonas aeruginosa pyoverdine systems. Microbiology 143:35-43. http://dx.doi.org/10.1099/00221287-143-1-35.
    • (1997) Microbiology , vol.143 , pp. 35-43
    • Meyer, J.M.1    Stintzi, A.2    De Vos, D.3    Cornelis, P.4    Tappe, R.5    Taraz, K.6    Budzikiewicz, H.7
  • 21
    • 21144446020 scopus 로고    scopus 로고
    • Mutational analysis of a bifunctional ferrisiderophore receptor and signal-transducing protein from Pseudomonas aeruginosa
    • James HE, Beare PA, Martin LW, Lamont IL. 2005. Mutational analysis of a bifunctional ferrisiderophore receptor and signal-transducing protein from Pseudomonas aeruginosa. J Bacteriol 187:4514-4520. http://dx.doi .org/10.1128/JB.187.13.4514-4520.2005.
    • (2005) J Bacteriol , vol.187 , pp. 4514-4520
    • James, H.E.1    Beare, P.A.2    Martin, L.W.3    Lamont, I.L.4
  • 23
    • 0023543302 scopus 로고
    • Characterization of non-TCA-precipitable 'Lowry protein' in plasma of patients with acute renal failure
    • Haag M, Meyer HE, Schollmeyer P, Hörl WH. 1987. Characterization of non-TCA-precipitable 'Lowry protein' in plasma of patients with acute renal failure. Clin Chim Acta 170:181-186. http://dx.doi.org/10.1016 /0009-8981(87)90126-4.
    • (1987) Clin Chim Acta , vol.170 , pp. 181-186
    • Haag, M.1    Meyer, H.E.2    Schollmeyer, P.3    Hörl, W.H.4
  • 25
    • 0346366452 scopus 로고    scopus 로고
    • Expression of L-ornithine Ndelta-oxygenase (PvdA) in fluorescent Pseudomonas species: An immunochemical and in silico study
    • Putignani L, Ambrosi C, Ascenzi P, Visca P. 2004. Expression of L-ornithine Ndelta-oxygenase (PvdA) in fluorescent Pseudomonas species: an immunochemical and in silico study. Biochem Biophys Res Commun 313:245-257. http://dx.doi.org/10.1016/j.bbrc.2003.11.116.
    • (2004) Biochem Biophys Res Commun , vol.313 , pp. 245-257
    • Putignani, L.1    Ambrosi, C.2    Ascenzi, P.3    Visca, P.4
  • 26
    • 34347375107 scopus 로고    scopus 로고
    • Environmental regulation of Pseudomonas aeruginosa PAO1 Las and Rhl quorum-sensing systems
    • Duan K, Surette MG. 2007. Environmental regulation of Pseudomonas aeruginosa PAO1 Las and Rhl quorum-sensing systems. J Bacteriol 189: 4827-4836. http://dx.doi.org/10.1128/JB.00043-07.
    • (2007) J Bacteriol , vol.189 , pp. 4827-4836
    • Duan, K.1    Surette, M.G.2
  • 27
    • 79952814455 scopus 로고    scopus 로고
    • A multitask biosensor for micro-volumetric detection of N-3-oxododecanoyl-homoserine lactone quorum sensing signal
    • Massai F, Imperi F, Quattrucci S, Zennaro E, Visca P, Leoni L. 2011. A multitask biosensor for micro-volumetric detection of N-3-oxododecanoyl-homoserine lactone quorum sensing signal. Biosens Bioelectron 26:3444-3449. http://dx.doi.org/10.1016/j.bios.2011.01.022.
    • (2011) Biosens Bioelectron , vol.26 , pp. 3444-3449
    • Massai, F.1    Imperi, F.2    Quattrucci, S.3    Zennaro, E.4    Visca, P.5    Leoni, L.6
  • 28
    • 0021796364 scopus 로고
    • Effects of siderophores on the growth of Pseudomonas aeruginosa in human serum and transferrin
    • Ankenbauer R, Sriyosachati S, Cox CD. 1985. Effects of siderophores on the growth of Pseudomonas aeruginosa in human serum and transferrin. Infect Immun 49:132-140.
    • (1985) Infect Immun , vol.49 , pp. 132-140
    • Ankenbauer, R.1    Sriyosachati, S.2    Cox, C.D.3
  • 29
    • 0028157711 scopus 로고
    • Cloning and nucleotide sequence of the pvdA gene encoding the pyoverdin biosynthetic enzyme L-ornithine N5 -oxygenase in Pseudomonas aeruginosa
    • Visca P, Ciervo A, Orsi N. 1994. Cloning and nucleotide sequence of the pvdA gene encoding the pyoverdin biosynthetic enzyme L-ornithine N5 -oxygenase in Pseudomonas aeruginosa. J Bacteriol 176:1128-1140.
    • (1994) J Bacteriol , vol.176 , pp. 1128-1140
    • Visca, P.1    Ciervo, A.2    Orsi, N.3
  • 30
    • 0022538733 scopus 로고
    • Phenotypic comparison of Pseudomonas aeruginosa strains isolated from a variety of clinical sites
    • Woods DE, Schaffer MS, Rabin HR, Campbell GD, Sokol PA. 1986. Phenotypic comparison of Pseudomonas aeruginosa strains isolated from a variety of clinical sites. J Clin Microbiol 24:260-264.
    • (1986) J Clin Microbiol , vol.24 , pp. 260-264
    • Woods, D.E.1    Schaffer, M.S.2    Rabin, H.R.3    Campbell, G.D.4    Sokol, P.A.5
  • 32
    • 53449085207 scopus 로고    scopus 로고
    • Membrane-association determinants of the omega-amino acid monooxygenase PvdA, a pyoverdine biosynthetic enzyme from Pseudomonas aeruginosa
    • Imperi F, Putignani L, Tiburzi F, Ambrosi C, Cipollone R, Ascenzi P, Visca P. 2008. Membrane-association determinants of the omega-amino acid monooxygenase PvdA, a pyoverdine biosynthetic enzyme from Pseudomonas aeruginosa. Microbiology 154:2804-2813. http://dx.doi.org/10 .1099/mic.0.2008/018804-0.
    • (2008) Microbiology , vol.154 , pp. 2804-2813
    • Imperi, F.1    Putignani, L.2    Tiburzi, F.3    Ambrosi, C.4    Cipollone, R.5    Ascenzi, P.6    Visca, P.7
  • 33
    • 84906074895 scopus 로고    scopus 로고
    • Pyochelin potentiates the inhibitory activity of gallium on Pseudomonas aeruginosa
    • Frangipani E, Bonchi C, Minandri F, Imperi F, Visca P. 2014. Pyochelin potentiates the inhibitory activity of gallium on Pseudomonas aeruginosa. Antimicrob Agents Chemother 58:5572-5575. http://dx.doi.org/10.1128 /AAC.03154-14.
    • (2014) Antimicrob Agents Chemother , vol.58 , pp. 5572-5575
    • Frangipani, E.1    Bonchi, C.2    Minandri, F.3    Imperi, F.4    Visca, P.5
  • 34
    • 84876216561 scopus 로고    scopus 로고
    • The dual personality of iron chelators: Growth inhibitors or promoters?
    • Visca P, Bonchi C, Minandri F, Frangipani E, Imperi F. 2013. The dual personality of iron chelators: growth inhibitors or promoters? Antimicrob Agents Chemother 57:2432-2433. http://dx.doi.org/10 .1128/AAC.02529-12.
    • (2013) Antimicrob Agents Chemother , vol.57 , pp. 2432-2433
    • Visca, P.1    Bonchi, C.2    Minandri, F.3    Frangipani, E.4    Imperi, F.5
  • 36
    • 0034462883 scopus 로고    scopus 로고
    • Transcriptional control of the hydrogen cyanide biosynthetic genes hcnABC by the anaerobic regulator ANR and the quorumsensing regulators LasR and RhlR in Pseudomonas aeruginosa
    • Pessi G, Haas D. 2000. Transcriptional control of the hydrogen cyanide biosynthetic genes hcnABC by the anaerobic regulator ANR and the quorumsensing regulators LasR and RhlR in Pseudomonas aeruginosa. J Bacteriol 182:6940-6949. http://dx.doi.org/10.1128/JB.182.24.6940-6949.2000.
    • (2000) J Bacteriol , vol.182 , pp. 6940-6949
    • Pessi, G.1    Haas, D.2
  • 37
    • 0042925520 scopus 로고    scopus 로고
    • Mutation of lasA and lasB reduces Pseudomonas aeruginosa invasion of epithelial cells
    • Cowell BA, Twining SS, Hobden JA, Kwong MS, Fleiszig SM. 2003. Mutation of lasA and lasB reduces Pseudomonas aeruginosa invasion of epithelial cells. Microbiology 143:2291-2299.
    • (2003) Microbiology , vol.143 , pp. 2291-2299
    • Cowell, B.A.1    Twining, S.S.2    Hobden, J.A.3    Kwong, M.S.4    Fleiszig, S.M.5
  • 39
    • 0034873465 scopus 로고    scopus 로고
    • Characterization of an endoprotease (PrpL) encoded by a PvdS-regulated gene in Pseudomonas aeruginosa
    • Wilderman PJ, Vasil AI, Johnson Z, Wilson MJ, Cunliffe HE, Lamont IL, Vasil ML. 2001. Characterization of an endoprotease (PrpL) encoded by a PvdS-regulated gene in Pseudomonas aeruginosa. Infect Immun 69: 5385-5394. http://dx.doi.org/10.1128/IAI.69.9.5385-5394.2001.
    • (2001) Infect Immun , vol.69 , pp. 5385-5394
    • Wilderman, P.J.1    Vasil, A.I.2    Johnson, Z.3    Wilson, M.J.4    Cunliffe, H.E.5    Lamont, I.L.6    Vasil, M.L.7
  • 40
    • 84862739931 scopus 로고    scopus 로고
    • Cation concentration variability of four distinct Mueller-Hinton agar brands influences polymyxin B susceptibility results
    • Girardello R, Bispo PJ, Yamanaka TM, Gales AC. 2012. Cation concentration variability of four distinct Mueller-Hinton agar brands influences polymyxin B susceptibility results. J Clin Microbiol 50:2414-2418. http: //dx.doi.org/10.1128/JCM.06686-11.
    • (2012) J Clin Microbiol , vol.50 , pp. 2414-2418
    • Girardello, R.1    Bispo, P.J.2    Yamanaka, T.M.3    Gales, A.C.4
  • 41
    • 79960936358 scopus 로고    scopus 로고
    • Deciphering the multifactorial nature of Acinetobacter baumannii pathogenicity
    • Antunes LC, Imperi F, Carattoli A, Visca P. 2011. Deciphering the multifactorial nature of Acinetobacter baumannii pathogenicity. PLoS One 6:e22674. http://dx.doi.org/10.1371/journal.pone.0022674.
    • (2011) PLoS One , vol.6 , pp. e22674
    • Antunes, L.C.1    Imperi, F.2    Carattoli, A.3    Visca, P.4
  • 42
    • 84866326661 scopus 로고    scopus 로고
    • In vitro and in vivo biological activities of iron chelators and gallium nitrate against Acinetobacter baumannii
    • de Léséleuc L, Harris G, KuoLee R, Chen W. 2012. In vitro and in vivo biological activities of iron chelators and gallium nitrate against Acinetobacter baumannii. Antimicrob Agents Chemother 56:5397-5400. http: //dx.doi.org/10.1128/AAC.00778-12.
    • (2012) Antimicrob Agents Chemother , vol.56 , pp. 5397-5400
    • De Léséleuc, L.1    Harris, G.2    KuoLee, R.3    Chen, W.4
  • 44
    • 0014057524 scopus 로고
    • Effect of the hemolysin of Pseudomonas aeruginosa on phosphatides and on phospholipase c activity
    • Kurioka S, Liu PV. 1967. Effect of the hemolysin of Pseudomonas aeruginosa on phosphatides and on phospholipase c activity. J Bacteriol 93:670-674.
    • (1967) J Bacteriol , vol.93 , pp. 670-674
    • Kurioka, S.1    Liu, P.V.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.