메뉴 건너뛰기




Volumn 159, Issue PART 12, 2013, Pages 2639-2650

Role of porin proteins in acquisition of transferrin iron by enteropathogens

Author keywords

[No Author keywords available]

Indexed keywords

CATECHOLAMINE; IRON; PORIN; TRANSFERRIN BINDING PROTEIN;

EID: 84888874813     PISSN: 13500872     EISSN: 14652080     Source Type: Journal    
DOI: 10.1099/mic.0.071928-0     Document Type: Article
Times cited : (20)

References (30)
  • 1
    • 0028846011 scopus 로고
    • Biochemical characterization of a Haemophilus influenzae periplasmic iron transport operon
    • Adhikari, P., Kirby, S. D., Nowalk, A. J., Veraldi, K. L., Schryvers, A. B. & Mietzner, T. A. (1995). Biochemical characterization of a Haemophilus influenzae periplasmic iron transport operon. J Biol Chem 270, 25142-25149.
    • (1995) J Biol Chem , vol.270 , pp. 25142-25149
    • Adhikari, P.1    Kirby, S.D.2    Nowalk, A.J.3    Veraldi, K.L.4    Schryvers, A.B.5    Mietzner, T.A.6
  • 2
    • 0030976398 scopus 로고    scopus 로고
    • Immunomodulatory properties of porins of some members of the family Enterobacteriaceae
    • Alurkar, V. & Kamat, R. (1997). Immunomodulatory properties of porins of some members of the family Enterobacteriaceae. Infect Immun 65, 2382-2388.
    • (1997) Infect Immun , vol.65 , pp. 2382-2388
    • Alurkar, V.1    Kamat, R.2
  • 5
    • 0034612342 scopus 로고    scopus 로고
    • One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products
    • Datsenko, K. A. & Wanner, B. L. (2000). One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products. Proc Natl Acad Sci U S A 97, 6640-6645.
    • (2000) Proc Natl Acad Sci U S A , vol.97 , pp. 6640-6645
    • Datsenko, K.A.1    Wanner, B.L.2
  • 6
    • 34447283105 scopus 로고    scopus 로고
    • Identification of transferrin-binding domains in TbpB expressed by Neisseria gonorrhoeae
    • DeRocco, A. J. & Cornelissen, C. N. (2007). Identification of transferrin-binding domains in TbpB expressed by Neisseria gonorrhoeae. Infect Immun 75, 3220-3232.
    • (2007) Infect Immun , vol.75 , pp. 3220-3232
    • DeRocco, A.J.1    Cornelissen, C.N.2
  • 8
    • 0033765763 scopus 로고    scopus 로고
    • The mammalian neuroendocrine hormone norepinephrine supplies iron for bacterial growth in the presence of transferrin or lactoferrin
    • Freestone, P. P. E., Lyte, M., Neal, C. P., Maggs, A. F., Haigh, R. D. & Williams, P. H. (2000). The mammalian neuroendocrine hormone norepinephrine supplies iron for bacterial growth in the presence of transferrin or lactoferrin. J Bacteriol 182, 6091-6098.
    • (2000) J Bacteriol , vol.182 , pp. 6091-6098
    • Freestone, P.P.E.1    Lyte, M.2    Neal, C.P.3    Maggs, A.F.4    Haigh, R.D.5    Williams, P.H.6
  • 9
    • 0036835441 scopus 로고    scopus 로고
    • Growth stimulation of intestinal commensal Escherichia coli by catecholamines: A possible contributory factor in trauma-induced sepsis
    • Freestone, P. P. E., Williams, P. H., Haigh, R. D., Maggs, A. F., Neal, C. P. & Lyte, M. (2002). Growth stimulation of intestinal commensal Escherichia coli by catecholamines: a possible contributory factor in trauma-induced sepsis. Shock 18, 465-470.
    • (2002) Shock , vol.18 , pp. 465-470
    • Freestone, P.P.E.1    Williams, P.H.2    Haigh, R.D.3    Maggs, A.F.4    Neal, C.P.5    Lyte, M.6
  • 10
    • 0038325672 scopus 로고    scopus 로고
    • Involvement of enterobactin in norepinephrine-mediated iron supply from transferrin to enterohaemorrhagic Escherichia coli
    • Freestone, P. P. E., Haigh, R. D., Williams, P. H. & Lyte, M. (2003). Involvement of enterobactin in norepinephrine-mediated iron supply from transferrin to enterohaemorrhagic Escherichia coli. FEMS Microbiol Lett 222, 39-43.
    • (2003) FEMS Microbiol Lett , vol.222 , pp. 39-43
    • Freestone, P.P.E.1    Haigh, R.D.2    Williams, P.H.3    Lyte, M.4
  • 11
    • 33847034492 scopus 로고    scopus 로고
    • Specificity of catecholamine-induced growth in Escherichia coli O157: H7, Salmonella enterica and Yersinia enterocolitica
    • Freestone, P. P. E., Haigh, R. D. & Lyte, M. (2007). Specificity of catecholamine-induced growth in Escherichia coli O157: H7, Salmonella enterica and Yersinia enterocolitica. FEMS Microbiol Lett 269, 221-228.
    • (2007) FEMS Microbiol Lett , vol.269 , pp. 221-228
    • Freestone, P.P.E.1    Haigh, R.D.2    Lyte, M.3
  • 12
    • 84868619886 scopus 로고    scopus 로고
    • Pseudomonas aeruginosacatecholamine inotrope interactions: A contributory factor in the development of ventilator-associated pneumonia?
    • Freestone, P. P., Hirst, R. A., Sandrini, S. M., Sharaff, F., Fry, H., Hyman, S. & O'Callaghan, C. (2012). Pseudomonas aeruginosacatecholamine inotrope interactions: a contributory factor in the development of ventilator-associated pneumonia? Chest 142, 1200-1210.
    • (2012) Chest , vol.142 , pp. 1200-1210
    • Freestone, P.P.1    Hirst, R.A.2    Sandrini, S.M.3    Sharaff, F.4    Fry, H.5    Hyman, S.6    O'Callaghan, C.7
  • 14
    • 0028846507 scopus 로고
    • Human antibody response to meningococcal transferrin binding proteins: Evidence for vaccine potential
    • Gorringe, A. R., Borrow, R., Fox, A. J. & Robinson, A. (1995). Human antibody response to meningococcal transferrin binding proteins: evidence for vaccine potential. Vaccine 13, 1207-1212.
    • (1995) Vaccine , vol.13 , pp. 1207-1212
    • Gorringe, A.R.1    Borrow, R.2    Fox, A.J.3    Robinson, A.4
  • 16
    • 0020959710 scopus 로고
    • Studies on transformation of Escherichia coli with plasmids
    • Hanahan, D. (1983). Studies on transformation of Escherichia coli with plasmids. J Mol Biol 166, 557-580.
    • (1983) J Mol Biol , vol.166 , pp. 557-580
    • Hanahan, D.1
  • 17
    • 80052329723 scopus 로고    scopus 로고
    • Bacterial virulence in the moonlight: Multitasking bacterial moonlighting proteins are virulence determinants in infectious disease
    • Henderson, B. & Martin, A. (2011). Bacterial virulence in the moonlight: multitasking bacterial moonlighting proteins are virulence determinants in infectious disease. Infect Immun 79, 3476-3491.
    • (2011) Infect Immun , vol.79 , pp. 3476-3491
    • Henderson, B.1    Martin, A.2
  • 18
    • 0037137566 scopus 로고    scopus 로고
    • Outer membrane protein A (OmpA): A new pathogen-associated molecular pattern that interacts with antigen presenting cells-impact on vaccine strategies
    • Jeannin, P. G., Magistrelli, G., Goetsch, L., Haeuw, J. F., Thieblemont, N., Bonnefoy, J. Y. & Delneste, Y. (2002). Outer membrane protein A (OmpA): a new pathogen-associated molecular pattern that interacts with antigen presenting cells-impact on vaccine strategies. Vaccine 20 (Suppl. 4), A23-A27.
    • (2002) Vaccine , vol.20 , Issue.SUPPL. 4
    • Jeannin, P.G.1    Magistrelli, G.2    Goetsch, L.3    Haeuw, J.F.4    Thieblemont, N.5    Bonnefoy, J.Y.6    Delneste, Y.7
  • 19
    • 50049089034 scopus 로고    scopus 로고
    • Structural biology of bacterial iron uptake
    • Krewulak, K. D. & Vogel, H. J. (2007). Structural biology of bacterial iron uptake. Biochim Biophys Acta 1778, 1781-1804.
    • (2007) Biochim Biophys Acta , vol.1778 , pp. 1781-1804
    • Krewulak, K.D.1    Vogel, H.J.2
  • 21
    • 21544480290 scopus 로고    scopus 로고
    • Intranasal administration of recombinant Neisseria gonorrhoeae transferrin binding proteins A and B conjugated to the cholera toxin B subunit induces systemic and vaginal antibodies in mice
    • Price, G. A., Russell, M. W. & Cornelissen, C. N. (2005). Intranasal administration of recombinant Neisseria gonorrhoeae transferrin binding proteins A and B conjugated to the cholera toxin B subunit induces systemic and vaginal antibodies in mice. Infect Immun 73, 3945-3953.
    • (2005) Infect Immun , vol.73 , pp. 3945-3953
    • Price, G.A.1    Russell, M.W.2    Cornelissen, C.N.3
  • 22
    • 0033759220 scopus 로고    scopus 로고
    • Iron metabolism in pathogenic bacteria
    • Ratledge, C. & Dover, L. G. (2000). Iron metabolism in pathogenic bacteria. Annu Rev Microbiol 54, 881-941.
    • (2000) Annu Rev Microbiol , vol.54 , pp. 881-941
    • Ratledge, C.1    Dover, L.G.2
  • 23
    • 0031763457 scopus 로고    scopus 로고
    • Both the full-length and the N-terminal domain of the meningococcal transferrin-binding protein B discriminate between human iron-loaded and apo-transferrin
    • Renauld-Mongénie, G., Latour, M., Poncet, D., Naville, S. & Quentin-Millet, M. J. (1998). Both the full-length and the N-terminal domain of the meningococcal transferrin-binding protein B discriminate between human iron-loaded and apo-transferrin. FEMS Microbiol Lett 169, 171-177.
    • (1998) FEMS Microbiol Lett , vol.169 , pp. 171-177
    • Renauld-Mongénie, G.1    Latour, M.2    Poncet, D.3    Naville, S.4    Quentin-Millet, M.J.5
  • 24
    • 84858452024 scopus 로고    scopus 로고
    • Insights into the structure and assembly of Escherichia coli outer membrane protein A
    • Reusch, R. N. (2012). Insights into the structure and assembly of Escherichia coli outer membrane protein A. FEBS J 279, 894-909.
    • (2012) FEBS J , vol.279 , pp. 894-909
    • Reusch, R.N.1
  • 25
    • 0033522876 scopus 로고    scopus 로고
    • Porins OmpC and PhoE of Escherichia coli as specific cell-surface targets of human lactoferrin. Binding characteristics and biological effects
    • Sallmann, F. R., Baveye-Descamps, S., Pattus, F., Salmon, V., Branza, N., Spik, G. & Legrand, D. (1999). Porins OmpC and PhoE of Escherichia coli as specific cell-surface targets of human lactoferrin. Binding characteristics and biological effects. J Biol Chem 274, 16107-16114.
    • (1999) J Biol Chem , vol.274 , pp. 16107-16114
    • Sallmann, F.R.1    Baveye-Descamps, S.2    Pattus, F.3    Salmon, V.4    Branza, N.5    Spik, G.6    Legrand, D.7
  • 26
    • 73649092092 scopus 로고    scopus 로고
    • Elucidation of the mechanism by which catecholamine stress hormones liberate iron from the innate immune defense proteins transferrin and lactoferrin
    • Sandrini, S. M., Shergill, R., Woodward, J., Muralikuttan, R., Haigh, R. D., Lyte, M. & Freestone, P. P. E. (2010). Elucidation of the mechanism by which catecholamine stress hormones liberate iron from the innate immune defense proteins transferrin and lactoferrin. J Bacteriol 192, 587-594.
    • (2010) J Bacteriol , vol.192 , pp. 587-594
    • Sandrini, S.M.1    Shergill, R.2    Woodward, J.3    Muralikuttan, R.4    Haigh, R.D.5    Lyte, M.6    Freestone, P.P.E.7
  • 27
    • 17044432201 scopus 로고    scopus 로고
    • Escherichia coli outer membrane protein A adheres to human brain microvascular endothelial cells
    • Shin, S., Lu, G., Cai, M. & Kim, K. S. (2005). Escherichia coli outer membrane protein A adheres to human brain microvascular endothelial cells. Biochem Biophys Res Commun 330, 1199-1204.
    • (2005) Biochem Biophys Res Commun , vol.330 , pp. 1199-1204
    • Shin, S.1    Lu, G.2    Cai, M.3    Kim, K.S.4
  • 28
    • 0021027842 scopus 로고
    • A broad host range mobilization system for in vivo engineering: Transposon mutagenesis in Gram negative bacteria
    • Simon, R., Priefer, U. & Puhler, A. (1983). A broad host range mobilization system for in vivo engineering: transposon mutagenesis in Gram negative bacteria. Nat Biotechnol 1, 784-791.
    • (1983) Nat Biotechnol , vol.1 , pp. 784-791
    • Simon, R.1    Priefer, U.2    Puhler, A.3
  • 30
    • 0036291172 scopus 로고    scopus 로고
    • The function of OmpA in Escherichia coli
    • Wang, Y. (2002). The function of OmpA in Escherichia coli. Biochem Biophys Res Commun 292, 396-401.
    • (2002) Biochem Biophys Res Commun , vol.292 , pp. 396-401
    • Wang, Y.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.