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Volumn 28, Issue 8, 2005, Pages 963-969

Utilization of ferroproteins by Candida albicans during candidastasis by apotransferrin

Author keywords

Candida albicans; Ferroproteins; Haptoglobin; Heme; Transferrin

Indexed keywords


EID: 30644471160     PISSN: 02536269     EISSN: 02536269     Source Type: Journal    
DOI: 10.1007/BF02973884     Document Type: Article
Times cited : (12)

References (36)
  • 1
    • 0019640696 scopus 로고
    • The significance of iron in infection
    • Bullen, J. J. The significance of iron in infection. Rev. Infec. Dis., 3, 1127-1138 (1981).
    • (1981) Rev. Infec. Dis. , vol.3 , pp. 1127-1138
    • Bullen, J.J.1
  • 4
    • 30644459492 scopus 로고
    • Differential effects of on the growth of Listeria monocytogens: Minimum requirements and mechanism if acquistion
    • Cowart, R. E. and Foster, B. G. Differential effects of on the growth of Listeria monocytogens: minimum requirements and mechanism if acquistion. J. Bacteriol., 142, 581-587 (1985).
    • (1985) J. Bacteriol. , vol.142 , pp. 581-587
    • Cowart, R.E.1    Foster, B.G.2
  • 5
    • 0002284487 scopus 로고    scopus 로고
    • Fungal factors implicated in pathogenesis
    • (Eds: Howard, D. H. and Miller, J). Springer-Verlag, Berlin
    • Cutler, J. E. and Han, Y. Fungal factors implicated in pathogenesis. In The mycota VI: human and animal relationship (Eds: Howard, D. H. and Miller, J). Springer-Verlag, Berlin. pp 1-29 (1996).
    • (1996) The Mycota VI: Human and Animal Relationship , pp. 1-29
    • Cutler, J.E.1    Han, Y.2
  • 6
    • 0020034471 scopus 로고
    • Haptoglobin: A natural bacteriostat
    • Eaton, J. W., Brandt, P., and Mahoney, J. R. Haptoglobin: a natural bacteriostat. Science, 215, 691-692 (1982).
    • (1982) Science , vol.215 , pp. 691-692
    • Eaton, J.W.1    Brandt, P.2    Mahoney, J.R.3
  • 7
    • 0014153849 scopus 로고
    • Relationship of transferrin and iron to serum inhibition of Candida albicans
    • Esterly, N. B., Bramner, S. R., and Crounse, R. G. Relationship of transferrin and iron to serum inhibition of Candida albicans. J. Invest. Dermatol. 49, 437-442 (1967).
    • (1967) J. Invest. Dermatol. , vol.49 , pp. 437-442
    • Esterly, N.B.1    Bramner, S.R.2    Crounse, R.G.3
  • 8
    • 0014434108 scopus 로고
    • Function of transferrin
    • Fletcher, J. and Huehns, E. R. Function of transferrin. Nature, 218, 1211-1214 (1986).
    • (1986) Nature , vol.218 , pp. 1211-1214
    • Fletcher, J.1    Huehns, E.R.2
  • 10
    • 0014405913 scopus 로고
    • Chitin in the new wall of regenerating protoplasts of Candida utilis
    • Garcia-Mendoza, C. and Novales-Lidieu, M. Chitin in the new wall of regenerating protoplasts of Candida utilis. Nature, 220, 1035-1036 (1968).
    • (1968) Nature , vol.220 , pp. 1035-1036
    • Garcia-Mendoza, C.1    Novales-Lidieu, M.2
  • 11
    • 0022774566 scopus 로고
    • Cytotoxin (leukotoxin) production by Pasteurella haemolytica: Requirement for as iron-containing compound
    • Gentry, M. J., Confer, A. W., Weinberg, E. D., and Homer, J. T. Cytotoxin (leukotoxin) production by Pasteurella haemolytica: requirement for as iron-containing compound. Am. J. Vet. Res., 47, 1919-1923 (1986).
    • (1986) Am. J. Vet. Res. , vol.47 , pp. 1919-1923
    • Gentry, M.J.1    Confer, A.W.2    Weinberg, E.D.3    Homer, J.T.4
  • 12
    • 0017199479 scopus 로고
    • Approaches to the standardization of serum unsaturated iron-binding capacity
    • Graham, G. F. and Bates, G. W. Approaches to the standardization of serum unsaturated iron-binding capacity. J. Lab. Clin. Med., 88, 477-486 (1976).
    • (1976) J. Lab. Clin. Med. , vol.88 , pp. 477-486
    • Graham, G.F.1    Bates, G.W.2
  • 13
    • 0015119090 scopus 로고
    • Lactoferrin-specific localization in the nuclei of human polymorphonuclear neutrophilic leukocytes
    • Green, I., Kirkpatrick, C. H., and Dale, D. C. Lactoferrin-specific localization in the nuclei of human polymorphonuclear neutrophilic leukocytes. Proc. Soc. Exp. Biol. Med., 137, 1311-1317 (1971).
    • (1971) Proc. Soc. Exp. Biol. Med. , vol.137 , pp. 1311-1317
    • Green, I.1    Kirkpatrick, C.H.2    Dale, D.C.3
  • 14
    • 0642379746 scopus 로고
    • Availability of iron and survival of bacteria in infection
    • Eds. Easmon, C. S. F. et al. Academic press. London
    • Griffiths, E. Availability of iron and survival of bacteria in infection. In Medical Microbiology. (Eds. Easmon, C. S. F. et al.). Vol. 3, pp 153-157. Academic press. London, (1983).
    • (1983) Medical Microbiology , vol.3 , pp. 153-157
    • Griffiths, E.1
  • 15
    • 0015219592 scopus 로고
    • Some spectra properties of the human hemoglobin-haptoglobin complex
    • Hamaguchi, H., Isomoto, A., Miyake, Y., and Nakajima, H. Some spectra properties of the human hemoglobin-haptoglobin complex. Biochemistry, 10, 1741-1745 (1971).
    • (1971) Biochemistry , vol.10 , pp. 1741-1745
    • Hamaguchi, H.1    Isomoto, A.2    Miyake, Y.3    Nakajima, H.4
  • 16
    • 0033983051 scopus 로고    scopus 로고
    • Protection against candidiasis by an immunoglobulin G3 monoclonal antibody specific for the same mannotriose as an IgM protective antibody
    • Han, Y., Riesselman, M. H., and Cutler, J. E. Protection against candidiasis by an immunoglobulin G3 monoclonal antibody specific for the same mannotriose as an IgM protective antibody. Infect. Immun., 68, 1649-1654 (2000).
    • (2000) Infect. Immun. , vol.68 , pp. 1649-1654
    • Han, Y.1    Riesselman, M.H.2    Cutler, J.E.3
  • 17
    • 0035424137 scopus 로고    scopus 로고
    • Complement is essential for protection by an IgM and an IgG3 monoclonal antibody against experimental, hematogenously disseminated candidiasis
    • Han, Y., Kozel, T. R., Zhang, M. X., MacGill, R. S., Caroll, M. C., and Cutler, J. E. Complement is essential for protection by an IgM and an IgG3 monoclonal antibody against experimental, hematogenously disseminated candidiasis. J. Immunol., 167, 1550-1557 (2001).
    • (2001) J. Immunol. , vol.167 , pp. 1550-1557
    • Han, Y.1    Kozel, T.R.2    Zhang, M.X.3    MacGill, R.S.4    Caroll, M.C.5    Cutler, J.E.6
  • 18
    • 21144453570 scopus 로고    scopus 로고
    • Berberine synergy with amphotericin B against disseminated candidiasis
    • Han, Y. and Lee, J. Berberine synergy with amphotericin B against disseminated candidiasis. Biol. Pharm. Bull., 28, 541-544 (2005a).
    • (2005) Biol. Pharm. Bull. , vol.28 , pp. 541-544
    • Han, Y.1    Lee, J.2
  • 19
    • 17044366188 scopus 로고    scopus 로고
    • Ginkgo terpene component has an anti-inflammatory effect on Candida albicans-caused arthritic inflammation
    • Han, Y. Ginkgo terpene component has an anti-inflammatory effect on Candida albicans-caused arthritic inflammation. Int. Immunopharm., 5, 1049-1056 (2005b).
    • (2005) Int. Immunopharm. , vol.5 , pp. 1049-1056
    • Han, Y.1
  • 20
    • 0032808171 scopus 로고    scopus 로고
    • Acqusition, transport, and storage of iron by pathogenic fungi
    • Howard, D. H. Acqusition, transport, and storage of iron by pathogenic fungi. Clin. Microbiol. Rev., 12, 394-404 (1999).
    • (1999) Clin. Microbiol. Rev. , vol.12 , pp. 394-404
    • Howard, D.H.1
  • 21
    • 0015225776 scopus 로고
    • Lactoferrin in milk from different species
    • Masson, P. J. and Heremans, J. F. Lactoferrin in milk from different species. Comp. Biochem. Physiol., 39B, 119-129 (1971).
    • (1971) Comp. Biochem. Physiol. , vol.39 B , pp. 119-129
    • Masson, P.J.1    Heremans, J.F.2
  • 22
    • 0009665799 scopus 로고
    • An iron-binding protein common to many external secretions
    • Masson, P. J., Heremans, J. F., and Dive, C. H. An iron-binding protein common to many external secretions. Clin. Chim. Acta, 14, 729-734 (1966).
    • (1966) Clin. Chim. Acta , vol.14 , pp. 729-734
    • Masson, P.J.1    Heremans, J.F.2    Dive, C.H.3
  • 24
    • 0942287210 scopus 로고    scopus 로고
    • Heme oxygenase in Candida albicans is regulated by hemoglobin and is necessary for metabolism of exogenous heme and hemoglobin to -biliverdin
    • Pendrak, M. L., Chao, M. P., Yan, S. S., and Roberts, D. D. Heme oxygenase in Candida albicans is regulated by hemoglobin and is necessary for metabolism of exogenous heme and hemoglobin to -biliverdin. J. Biol. Chem., 279, 3426-3433 (2004).
    • (2004) J. Biol. Chem. , vol.279 , pp. 3426-3433
    • Pendrak, M.L.1    Chao, M.P.2    Yan, S.S.3    Roberts, D.D.4
  • 25
    • 0018388363 scopus 로고
    • Accumulation of iron by Yersiniae
    • Perry, R. D. and Brubaker, R. R. Accumulation of iron by Yersiniae. J. Bacteriol. 137, 1290-1298 (1979).
    • (1979) J. Bacteriol. , vol.137 , pp. 1290-1298
    • Perry, R.D.1    Brubaker, R.R.2
  • 26
    • 0016835863 scopus 로고
    • A study of the kinetics of iron and copper binding to hen ovotrasferrin
    • Phelps, C. F. and Antonini, E. A study of the kinetics of iron and copper binding to hen ovotrasferrin. J. Biochem., 147, 385-391 (1975).
    • (1975) J. Biochem. , vol.147 , pp. 385-391
    • Phelps, C.F.1    Antonini, E.2
  • 28
    • 30644472859 scopus 로고
    • Inhibition of growth of pathogenic yeast by human serum
    • Roth, F. J. Jr. and Goldstein, M. I. Inhibition of growth of pathogenic yeast by human serum. J. Invest. Dermatol., 36, 383-387 (1961).
    • (1961) J. Invest. Dermatol. , vol.36 , pp. 383-387
    • Roth Jr., F.J.1    Goldstein, M.I.2
  • 29
    • 0037352408 scopus 로고    scopus 로고
    • Hemin uptake and use as an iron source by Candida albicans: Role of CAHMX1-encoded haem oxygenase
    • Santos, R., Buisson, N., Knight, S., Dancis, A., Camadro, J. M., and Lesuisse, E. Hemin uptake and use as an iron source by Candida albicans: role of CAHMX1-encoded haem oxygenase. Microbiol., 149, 579-588 (2003).
    • (2003) Microbiol. , vol.149 , pp. 579-588
    • Santos, R.1    Buisson, N.2    Knight, S.3    Dancis, A.4    Camadro, J.M.5    Lesuisse, E.6
  • 30
    • 0020045384 scopus 로고
    • Expression of a high affinity mechanism for acquisition of transferrin iron by Neisseria meningutudis
    • Simonson, C., Brener, D., and Devoe, I. W. Expression of a high affinity mechanism for acquisition of transferrin iron by Neisseria meningutudis. Infect. Immun., 36, 107-113 (1982).
    • (1982) Infect. Immun. , vol.36 , pp. 107-113
    • Simonson, C.1    Brener, D.2    Devoe, I.W.3
  • 31
    • 0023082839 scopus 로고    scopus 로고
    • Protein sources of heme for Haemophilus influenza
    • Stull, T. Protein sources of heme for Haemophilus influenza. Infect. Immun., 55, 148-153 (1997).
    • (1997) Infect. Immun. , vol.55 , pp. 148-153
    • Stull, T.1
  • 32
    • 0022574292 scopus 로고
    • Interaction between lactoferrin and ovotransferrin and candida cell
    • Valenti, P., Visca, P., Giovani, A., and Oris, N. Interaction between lactoferrin and ovotransferrin and candida cell. FEMS Microbiol. Lett., 33, 271- 275 (1986).
    • (1986) FEMS Microbiol. Lett. , vol.33 , pp. 271-275
    • Valenti, P.1    Visca, P.2    Giovani, A.3    Oris, N.4
  • 33
    • 0015138422 scopus 로고
    • Role of iron in host-parasite interaction
    • Weinberg, E. D. Role of iron in host-parasite interaction. J. Infect. Dis., 124, 401-410 (1971).
    • (1971) J. Infect. Dis. , vol.124 , pp. 401-410
    • Weinberg, E.D.1
  • 34
    • 0018102319 scopus 로고
    • Iron and interaction
    • Weinberg, E. D. Iron and interaction. Microbiol. Rev., 42, 45-66 (1978).
    • (1978) Microbiol. Rev. , vol.42 , pp. 45-66
    • Weinberg, E.D.1
  • 35
    • 0014216886 scopus 로고
    • 2,3-Dihydroxy-benzoate as bacterial growth factor and its route of biosynthesis
    • Young, I. G., Cox, G. B., and Gibson, F. 2,3-Dihydroxy-benzoate as bacterial growth factor and its route of biosynthesis. Biochim. Biophys. Acta, 441, 319-331 (1967).
    • (1967) Biochim. Biophys. Acta , vol.441 , pp. 319-331
    • Young, I.G.1    Cox, G.B.2    Gibson, F.3


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