메뉴 건너뛰기




Volumn 54, Issue 10, 2010, Pages 4335-4342

Antimicrobial mechanism of action of transferrins: Selective inhibition of H+-ATPase

Author keywords

[No Author keywords available]

Indexed keywords

2,6 DICHLOROPHENOLINDOPHENOL; ADENOSINE TRIPHOSPHATASE; APOTRANSFERRIN; LACTOFERRIN; PROTON; TRANSFERRIN;

EID: 77957373613     PISSN: 00664804     EISSN: 10986596     Source Type: Journal    
DOI: 10.1128/AAC.01620-09     Document Type: Article
Times cited : (44)

References (33)
  • 1
    • 0019474039 scopus 로고
    • Lactoferrin enhances hydroxyl radical production by human neutrophils, neutrophil particulate fractions, and an enzymatic generating system
    • Ambruso, D. R., and R. B. Johnston. 1981. Lactoferrin enhances hydroxyl radical production by human neutrophils, neutrophil particulate fractions, and an enzymatic generating system. J. Clin. Invest. 67:352-360.
    • (1981) J. Clin. Invest. , vol.67 , pp. 352-360
    • Ambruso, D.R.1    Johnston, R.B.2
  • 2
    • 16244364337 scopus 로고    scopus 로고
    • Antibiotic tolerance induced by lactoferrin in clinical Pseudomonas aeruginosa isolates from cystic fibrosis patients
    • Andrés, M. T., M. Viejo-Díaz, F. Pérez, and J. F. Fierro. 2005. Antibiotic tolerance induced by lactoferrin in clinical Pseudomonas aeruginosa isolates from cystic fibrosis patients. Antimicrob. Agents Chemother. 49:1613-1616.
    • (2005) Antimicrob. Agents Chemother. , vol.49 , pp. 1613-1616
    • Andrés, M.T.1    Viejo-Díaz, M.2    Pérez, F.3    Fierro, J.F.4
  • 3
    • 0001428082 scopus 로고
    • Determination of citrulline and allantoin and demonstration of citrulline in blood plasma
    • Archibald, R. M. 1944. Determination of citrulline and allantoin and demonstration of citrulline in blood plasma. J. Biol. Chem. 156:121-142.
    • (1944) J. Biol. Chem. , vol.156 , pp. 121-142
    • Archibald, R.M.1
  • 4
    • 0018868141 scopus 로고
    • Bactericidal activity of human lactoferrin: Sensitivity of a variety of microorganisms
    • Arnold, R. R., M. Brewer, and J. J. Gauthier. 1980. Bactericidal activity of human lactoferrin: sensitivity of a variety of microorganisms. Infect. Immun. 28:893-898.
    • (1980) Infect. Immun. , vol.28 , pp. 893-898
    • Arnold, R.R.1    Brewer, M.2    Gauthier, J.J.3
  • 5
    • 0017389761 scopus 로고
    • A bactericidal effect for human lactoferrin
    • Arnold, R. R., M. F. Cole, and J. R. McGhee. 1977. A bactericidal effect for human lactoferrin. Science 197:263-265.
    • (1977) Science , vol.197 , pp. 263-265
    • Arnold, R.R.1    Cole, M.F.2    McGhee, J.R.3
  • 6
    • 0019432648 scopus 로고
    • Bactericidal activity of human lactoferrin: Influence of physical condition and metabolic state of the target microorganisms
    • Arnold, R. R., J. E. Russell, W. J. Champion, and J. J. Gauthier. 1981. Bactericidal activity of human lactoferrin: influence of physical condition and metabolic state of the target microorganisms. Infect. Immun. 32:655-660.
    • (1981) Infect. Immun. , vol.32 , pp. 655-660
    • Arnold, R.R.1    Russell, J.E.2    Champion, W.J.3    Gauthier, J.J.4
  • 9
    • 0038192048 scopus 로고    scopus 로고
    • Regulation of expression of the cyanide-insensitive terminal oxidase in Pseudomonas aeruginosa
    • Cooper, M., G. R. Tavankar, and H. D. Williams. 2003. Regulation of expression of the cyanide-insensitive terminal oxidase in Pseudomonas aeruginosa. Microbiology 149:1275-1284.
    • (2003) Microbiology , vol.149 , pp. 1275-1284
    • Cooper, M.1    Tavankar, G.R.2    Williams, H.D.3
  • 10
    • 0141789637 scopus 로고    scopus 로고
    • Surviving the acid test: Responses of Gram-positive bacteria to low pH
    • Cotter, P. D., and C. Hill. 2003. Surviving the acid test: responses of Gram-positive bacteria to low pH. Microbiol. Mol. Biol. Rev. 67:429-453.
    • (2003) Microbiol. Mol. Biol. Rev. , vol.67 , pp. 429-453
    • Cotter, P.D.1    Hill, C.2
  • 11
  • 13
    • 0023815539 scopus 로고
    • Damage of the outer membrane of enteric Gram-negative bacteria by lactoferrin and transferrin
    • Ellison, R. T., T. J. Giehl, and F. M. LaForce. 1988. Damage of the outer membrane of enteric Gram-negative bacteria by lactoferrin and transferrin. Infect. Immun. 56:2774-2781.
    • (1988) Infect. Immun. , vol.56 , pp. 2774-2781
    • Ellison, R.T.1    Giehl, T.J.2    LaForce, F.M.3
  • 14
    • 0141918811 scopus 로고    scopus 로고
    • Lactoferrin - A multifunctional protein with antimicrobial properties
    • Farnaud, S., and R. W. Evans. 2003. Lactoferrin - a multifunctional protein with antimicrobial properties. Mol. Immunol. 40:395-405.
    • (2003) Mol. Immunol. , vol.40 , pp. 395-405
    • Farnaud, S.1    Evans, R.W.2
  • 15
    • 0023079986 scopus 로고
    • Cell culture assay of biological activity of lactoferrin and transferrin
    • Hashizume, S., K. Kuroda, and H. Murakami. 1987. Cell culture assay of biological activity of lactoferrin and transferrin. Methods Enzymol. 147:302-314.
    • (1987) Methods Enzymol. , vol.147 , pp. 302-314
    • Hashizume, S.1    Kuroda, K.2    Murakami, H.3
  • 16
    • 0023092245 scopus 로고
    • Oxygen regulation of nitrate uptake in denitrifying Pseudomonas aeruginosa
    • Hernandez, D., and J. J. Rowe. 1987. Oxygen regulation of nitrate uptake in denitrifying Pseudomonas aeruginosa. Appl. Environ. Microbiol. 53:745-750.
    • (1987) Appl. Environ. Microbiol. , vol.53 , pp. 745-750
    • Hernandez, D.1    Rowe, J.J.2
  • 17
    • 0023736956 scopus 로고
    • Killing of Actinobacillus actinomycetemcomitans by human lactoferrin
    • Kalmar, J. R., and R. R. Arnold. 1988. Killing of Actinobacillus actinomycetemcomitans by human lactoferrin. Infect. Immun. 56:2552-2557.
    • (1988) Infect. Immun. , vol.56 , pp. 2552-2557
    • Kalmar, J.R.1    Arnold, R.R.2
  • 18
    • 0021990909 scopus 로고
    • A proton-translocating ATPase regulates pH of the bacterial cytoplasm
    • Kobayashi, H. 1985. A proton-translocating ATPase regulates pH of the bacterial cytoplasm. J. Biol. Chem. 260:72-76.
    • (1985) J. Biol. Chem. , vol.260 , pp. 72-76
    • Kobayashi, H.1
  • 21
    • 0026015262 scopus 로고
    • Malolactic fermentation: Electrogenic malate uptake and malate/lactate antiport generate metabolic energy
    • Poolman, B., D. Molenaar, E. J. Smid, T. Ubbink, T. Abee, P. P. Renault, and W. N. Konings. 1991. Malolactic fermentation: electrogenic malate uptake and malate/lactate antiport generate metabolic energy. J. Bacteriol. 173:6030-6037.
    • (1991) J. Bacteriol. , vol.173 , pp. 6030-6037
    • Poolman, B.1    Molenaar, D.2    Smid, E.J.3    Ubbink, T.4    Abee, T.5    Renault, P.P.6    Konings, W.N.7
  • 22
    • 21844435978 scopus 로고    scopus 로고
    • 0-ATP synthase of Mycobacterium smegmatis is essential for growth
    • 0-ATP synthase of Mycobacterium smegmatis is essential for growth. J. Bacteriol. 187:5023-5028.
    • (2005) J. Bacteriol. , vol.187 , pp. 5023-5028
    • Tran, S.L.1    Cook, G.M.2
  • 23
    • 0021664042 scopus 로고
    • Pseudomonas aeruginosa mutants affected in anaerobic growth on arginine: Evidence for a four-gene cluster encoding the arginine deiminase pathway
    • Vander Wauven, C., A. Piérard, M. Kley-Raymann, and D. Haas. 1984. Pseudomonas aeruginosa mutants affected in anaerobic growth on arginine: evidence for a four-gene cluster encoding the arginine deiminase pathway. J. Bacteriol. 160:928-934.
    • (1984) J. Bacteriol. , vol.160 , pp. 928-934
    • Vander Wauven, C.1    Piérard, A.2    Kley-Raymann, M.3    Haas, D.4
  • 24
    • 0037725162 scopus 로고    scopus 로고
    • Potassium-efflux induced by a new lactoferrin-derived peptide mimicking the effect of native human lactoferrin on the bacterial cytoplasmic membrane
    • Moscow
    • Viejo-Díaz, M., M. T. Andrés, J. Pérez-Gil, M. Sánchez, and J. F. Fierro. 2003. Potassium-efflux induced by a new lactoferrin-derived peptide mimicking the effect of native human lactoferrin on the bacterial cytoplasmic membrane. Biochemistry (Moscow) 68:217-227.
    • (2003) Biochemistry , vol.68 , pp. 217-227
    • Viejo-Díaz, M.1    Andrés, M.T.2    Pérez-Gil, J.3    Sánchez, M.4    Fierro, J.F.5
  • 25
    • 18344408431 scopus 로고    scopus 로고
    • Modulation of in vitro fungicidal activity of human lactoferrin against Candida albicans by extracellular cation concentration and target cell metabolic activity
    • Viejo-Díaz, M., M. T. Andrés, and J. F. Fierro. 2004. Modulation of in vitro fungicidal activity of human lactoferrin against Candida albicans by extracellular cation concentration and target cell metabolic activity. Antimicrob. Agents Chemother. 48:1242-1248.
    • (2004) Antimicrob. Agents Chemother. , vol.48 , pp. 1242-1248
    • Viejo-Díaz, M.1    Andrés, M.T.2    Fierro, J.F.3
  • 26
    • 0027104114 scopus 로고
    • The NADH:ubiquinone oxidoreductase (complex I) of respiratory chains
    • Walker, J. E. 1992. The NADH:ubiquinone oxidoreductase (complex I) of respiratory chains. Q. Rev. Biophys. 25:253-324.
    • (1992) Q. Rev. Biophys. , vol.25 , pp. 253-324
    • Walker, J.E.1
  • 27
    • 0016227934 scopus 로고
    • Iron and susceptibility to infectious disease
    • Weimberg, E. D. 1974. Iron and susceptibility to infectious disease. Science 184:952-956.
    • (1974) Science , vol.184 , pp. 952-956
    • Weimberg, E.D.1
  • 28
    • 33749255145 scopus 로고    scopus 로고
    • Oxygen, cyanide and energy generation in the cystic fibrosis pathogen Pseudomonas aeruginosa
    • Williams, H. D., J. E. A. Zlosnik, and B. Ryall. 2007. Oxygen, cyanide and energy generation in the cystic fibrosis pathogen Pseudomonas aeruginosa. Adv. Microb. Physiol. 52:3-71.
    • (2007) Adv. Microb. Physiol. , vol.52 , pp. 3-71
    • Williams, H.D.1    Zlosnik, J.E.A.2    Ryall, B.3
  • 29
    • 2442515355 scopus 로고    scopus 로고
    • Multidimensional signatures in antimicrobial peptides
    • Yount, N. Y., and M. R. Yeaman. 2004. Multidimensional signatures in antimicrobial peptides. Proc. Natl. Acad. Sci. U. S. A. 101:7363-7368.
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , pp. 7363-7368
    • Yount, N.Y.1    Yeaman, M.R.2
  • 30
    • 35848965269 scopus 로고    scopus 로고
    • The γ-core motif correlates with antimicrobial activity in cysteine-containing kaliocin-1 originating from transferrins
    • Yount, N. Y., M. T. Andrés, J. F. Fierro, and M. R. Yeaman. 2007. The γ-core motif correlates with antimicrobial activity in cysteine-containing kaliocin-1 originating from transferrins. Biochim. Biophys. Acta 1768:2862-2872.
    • (2007) Biochim. Biophys. Acta , vol.1768 , pp. 2862-2872
    • Yount, N.Y.1    Andrés, M.T.2    Fierro, J.F.3    Yeaman, M.R.4
  • 32
    • 0024379499 scopus 로고
    • The respiratory chains of pathogenic pseudomonads
    • Zannoni, D. 1989. The respiratory chains of pathogenic pseudomonads. Biochim. Biophys. Acta 975:299-316.
    • (1989) Biochim. Biophys. Acta , vol.975 , pp. 299-316
    • Zannoni, D.1
  • 33
    • 0028631943 scopus 로고
    • Proposed mechanisms for the involvement of lactoferrin in hydrolysis of nucleic acid
    • Zhao, X. Y., and T. W. Hutchens. 1994. Proposed mechanisms for the involvement of lactoferrin in hydrolysis of nucleic acid. Adv. Exp. Med. Biol. 357:271-278.
    • (1994) Adv. Exp. Med. Biol. , vol.357 , pp. 271-278
    • Zhao, X.Y.1    Hutchens, T.W.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.