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Volumn 70, Issue 1, 2008, Pages 127-139

The Histoplasma capsulatum vacuolar ATPase is required for iron homeostasis, intracellular replication in macrophages and virulence in a murine model of histoplasmosis

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATASE; BAFILOMYCIN; IRON; PROTEIN VMA1; UNCLASSIFIED DRUG;

EID: 51649086978     PISSN: 0950382X     EISSN: 13652958     Source Type: Journal    
DOI: 10.1111/j.1365-2958.2008.06395.x     Document Type: Article
Times cited : (47)

References (50)
  • 1
    • 33644947546 scopus 로고    scopus 로고
    • Histoplasmosis among human immunodeficiency virus-infected people in Europe: Report of 4 cases and review of the literature
    • Antinori, S., Magni, C., Nebuloni, M., Parravicini, C., Corbellino, M., Sollima, S., et al. (2006) Histoplasmosis among human immunodeficiency virus-infected people in Europe: report of 4 cases and review of the literature. Medicine (Baltimore) 85 : 22 36.
    • (2006) Medicine (Baltimore) , vol.85 , pp. 22-36
    • Antinori, S.1    Magni, C.2    Nebuloni, M.3    Parravicini, C.4    Corbellino, M.5    Sollima, S.6
  • 2
    • 0014851040 scopus 로고
    • Rhodotorulic acid from species of Leucosporidium, Rhodosporidium, Rhodotorula, Sporidiobolus, and Sporobolomyces, and a new alanine-containing ferrichrome from Cryptococcus melibiosum
    • Atkin, C.L., Neilands, J.B. Phaff, H.J. (1970) Rhodotorulic acid from species of Leucosporidium, Rhodosporidium, Rhodotorula, Sporidiobolus, and Sporobolomyces, and a new alanine-containing ferrichrome from Cryptococcus melibiosum. J Bacteriol 103 : 722 733.
    • (1970) J Bacteriol , vol.103 , pp. 722-733
    • Atkin, C.L.1    Neilands, J.B.2    Phaff, H.J.3
  • 3
    • 0028938278 scopus 로고
    • Iron sequestration by the yeast vacuole. a study with vacuolar mutants of Saccharomyces cerevisiae
    • Bode, H.P., Dumschat, M., Garotti, S. Fuhrmann, G.F. (1995) Iron sequestration by the yeast vacuole. A study with vacuolar mutants of Saccharomyces cerevisiae. Eur J Biochem 228 : 337 342.
    • (1995) Eur J Biochem , vol.228 , pp. 337-342
    • Bode, H.P.1    Dumschat, M.2    Garotti, S.3    Fuhrmann, G.F.4
  • 4
    • 34249909212 scopus 로고    scopus 로고
    • RNA interference-mediated silencing of the YPS3 gene of Histoplasma capsulatum reveals virulence defects
    • Bohse, M.L. Woods, J.P. (2007) RNA interference-mediated silencing of the YPS3 gene of Histoplasma capsulatum reveals virulence defects. Infect Immun 75 : 2811 2817.
    • (2007) Infect Immun , vol.75 , pp. 2811-2817
    • Bohse, M.L.1    Woods, J.P.2
  • 6
    • 0011913143 scopus 로고
    • Bafilomycins: A class of inhibitors of membrane ATPases from microorganisms, animal cells, and plant cells
    • Bowman, E.J., Siebers, A. Altendorf, K. (1988) Bafilomycins: a class of inhibitors of membrane ATPases from microorganisms, animal cells, and plant cells. Proc Natl Acad Sci USA 85 : 7972 7976.
    • (1988) Proc Natl Acad Sci USA , vol.85 , pp. 7972-7976
    • Bowman, E.J.1    Siebers, A.2    Altendorf, K.3
  • 7
    • 0034614496 scopus 로고    scopus 로고
    • Disruption of vma-1, the gene encoding the catalytic subunit of the vacuolar H(+)-ATPase, causes severe morphological changes in Neurospora crassa
    • Bowman, E.J., Kendle, R. Bowman, B.J. (2000) Disruption of vma-1, the gene encoding the catalytic subunit of the vacuolar H(+)-ATPase, causes severe morphological changes in Neurospora crassa. J Biol Chem 275 : 167 176.
    • (2000) J Biol Chem , vol.275 , pp. 167-176
    • Bowman, E.J.1    Kendle, R.2    Bowman, B.J.3
  • 8
    • 0242666433 scopus 로고    scopus 로고
    • Identification of a new chondropsin class of antitumor compound that selectively inhibits V-ATPases
    • Bowman, E.J., Gustafson, K.R., Bowman, B.J. Boyd, M.R. (2003) Identification of a new chondropsin class of antitumor compound that selectively inhibits V-ATPases. J Biol Chem 278 : 44147 44152.
    • (2003) J Biol Chem , vol.278 , pp. 44147-44152
    • Bowman, E.J.1    Gustafson, K.R.2    Bowman, B.J.3    Boyd, M.R.4
  • 9
    • 0023146087 scopus 로고
    • Role of the adherence-promoting receptors, CR3, LFA-1, and p150,95, in binding of Histoplasma capsulatum by human macrophages
    • Bullock, W.E. Wright, S.D. (1987) Role of the adherence-promoting receptors, CR3, LFA-1, and p150,95, in binding of Histoplasma capsulatum by human macrophages. J Exp Med 165 : 195 210.
    • (1987) J Exp Med , vol.165 , pp. 195-210
    • Bullock, W.E.1    Wright, S.D.2
  • 11
    • 0027508062 scopus 로고
    • The vacuolar H(+)-ATPase of Saccharomyces cerevisiae is required for efficient copper detoxification, mitochondrial function, and iron metabolism
    • Eide, D.J., Bridgham, J.T., Zhao, Z. Mattoon, J.R. (1993) The vacuolar H(+)-ATPase of Saccharomyces cerevisiae is required for efficient copper detoxification, mitochondrial function, and iron metabolism. Mol Gen Genet 241 : 447 456.
    • (1993) Mol Gen Genet , vol.241 , pp. 447-456
    • Eide, D.J.1    Bridgham, J.T.2    Zhao, Z.3    Mattoon, J.R.4
  • 12
    • 33644945987 scopus 로고    scopus 로고
    • Characterization of the yeast ionome: A genome-wide analysis of nutrient mineral and trace element homeostasis in Saccharomyces cerevisiae
    • Eide, D.J., Clark, S., Nair, T.M., Gehl, M., Gribskov, M., Guerinot, M.L. Harper, J.F. (2005) Characterization of the yeast ionome: a genome-wide analysis of nutrient mineral and trace element homeostasis in Saccharomyces cerevisiae. Genome Biol 6 : R77.
    • (2005) Genome Biol , vol.6
    • Eide, D.J.1    Clark, S.2    Nair, T.M.3    Gehl, M.4    Gribskov, M.5    Guerinot, M.L.6    Harper, J.F.7
  • 13
    • 0038162590 scopus 로고    scopus 로고
    • The siderophore system is essential for viability of Aspergillus nidulans: Functional analysis of two genes encoding 1-ornithine N 5-monooxygenase (sidA) and a non-ribosomal peptide synthetase (sidC)
    • Eisendle, M., Oberegger, H., Zadra, I. Haas, H. (2003) The siderophore system is essential for viability of Aspergillus nidulans: functional analysis of two genes encoding 1-ornithine N 5-monooxygenase (sidA) and a non-ribosomal peptide synthetase (sidC). Mol Microbiol 49 : 359 375.
    • (2003) Mol Microbiol , vol.49 , pp. 359-375
    • Eisendle, M.1    Oberegger, H.2    Zadra, I.3    Haas, H.4
  • 14
    • 0037277456 scopus 로고    scopus 로고
    • Large-scale functional genomic analysis of sporulation and meiosis in Saccharomyces cerevisiae
    • Enyenihi, A.H. Saunders, W.S. (2003) Large-scale functional genomic analysis of sporulation and meiosis in Saccharomyces cerevisiae. Genetics 163 : 47 54.
    • (2003) Genetics , vol.163 , pp. 47-54
    • Enyenihi, A.H.1    Saunders, W.S.2
  • 15
    • 0037940408 scopus 로고    scopus 로고
    • Physiological consequence of disruption of the VMA1 gene in the riboflavin overproducer Ashbya gossypii
    • Forster, C., Santos, M.A., Ruffert, S., Kramer, R. Revuelta, J.L. (1999) Physiological consequence of disruption of the VMA1 gene in the riboflavin overproducer Ashbya gossypii. J Biol Chem 274 : 9442 9448.
    • (1999) J Biol Chem , vol.274 , pp. 9442-9448
    • Forster, C.1    Santos, M.A.2    Ruffert, S.3    Kramer, R.4    Revuelta, J.L.5
  • 17
    • 0034059728 scopus 로고    scopus 로고
    • The hydroxamate siderophores of Histoplasma capsulatum
    • Howard, D.H., Rafie, R., Tiwari, A. Faull, K.F. (2000) The hydroxamate siderophores of Histoplasma capsulatum. Infect Immun 68 : 2338 2343.
    • (2000) Infect Immun , vol.68 , pp. 2338-2343
    • Howard, D.H.1    Rafie, R.2    Tiwari, A.3    Faull, K.F.4
  • 18
    • 1842787818 scopus 로고    scopus 로고
    • Characterization of Schizosaccharomyces pombe mutants defective in vacuolar acidification and protein sorting
    • Iwaki, T., Goa, T., Tanaka, N. Takegawa, K. (2004) Characterization of Schizosaccharomyces pombe mutants defective in vacuolar acidification and protein sorting. Mol Genet Genomics 271 : 197 207.
    • (2004) Mol Genet Genomics , vol.271 , pp. 197-207
    • Iwaki, T.1    Goa, T.2    Tanaka, N.3    Takegawa, K.4
  • 19
    • 33646898774 scopus 로고    scopus 로고
    • Reactivation histoplasmosis after treatment with anti-tumor necrosis factor alpha in a patient from a nonendemic area
    • Jain, V.V., Evans, T. Peterson, M.W. (2006) Reactivation histoplasmosis after treatment with anti-tumor necrosis factor alpha in a patient from a nonendemic area. Respir Med 100 : 1291 1293.
    • (2006) Respir Med , vol.100 , pp. 1291-1293
    • Jain, V.V.1    Evans, T.2    Peterson, M.W.3
  • 20
    • 0023135945 scopus 로고
    • Isolation and characterization of spontaneous avirulent variants of Histoplasma capsulatum
    • Klimpel, K.R. Goldman, W.E. (1987) Isolation and characterization of spontaneous avirulent variants of Histoplasma capsulatum. Infect Immun 55 : 528 533.
    • (1987) Infect Immun , vol.55 , pp. 528-533
    • Klimpel, K.R.1    Goldman, W.E.2
  • 21
    • 0025170681 scopus 로고
    • The fungal vacuole: Composition, function, and biogenesis
    • Klionsky, D.J., Herman, P.K. Emr, S.D. (1990) The fungal vacuole: composition, function, and biogenesis. Microbiol Rev 54 : 266 292.
    • (1990) Microbiol Rev , vol.54 , pp. 266-292
    • Klionsky, D.J.1    Herman, P.K.2    Emr, S.D.3
  • 22
    • 0035800856 scopus 로고    scopus 로고
    • CCC1 is a transporter that mediates vacuolar iron storage in yeast
    • Li, L., Chen, O.S., McVey Ward, D. Kaplan, J. (2001) CCC1 is a transporter that mediates vacuolar iron storage in yeast. J Biol Chem 276 : 29515 29519.
    • (2001) J Biol Chem , vol.276 , pp. 29515-29519
    • Li, L.1    Chen, O.S.2    McVey Ward, D.3    Kaplan, J.4
  • 23
    • 33750480548 scopus 로고    scopus 로고
    • An alpha-(1,4)-amylase is essential for alpha-(1,3)-glucan production and virulence in Histoplasma capsulatum
    • Marion, C.L., Rappleye, C.A., Engle, J.T. Goldman, W.E. (2006) An alpha-(1,4)-amylase is essential for alpha-(1,3)-glucan production and virulence in Histoplasma capsulatum. Mol Microbiol 62 : 970 983.
    • (2006) Mol Microbiol , vol.62 , pp. 970-983
    • Marion, C.L.1    Rappleye, C.A.2    Engle, J.T.3    Goldman, W.E.4
  • 24
    • 1642308586 scopus 로고    scopus 로고
    • Disruption of the gene encoding the V-ATPase subunit a results in inhibition of normal growth and abolished sporulation in Aspergillus nidulans
    • Melin, P., Schnurer, J. Wagner, E.G. (2004) Disruption of the gene encoding the V-ATPase subunit A results in inhibition of normal growth and abolished sporulation in Aspergillus nidulans. Microbiology 150 : 743 748.
    • (2004) Microbiology , vol.150 , pp. 743-748
    • Melin, P.1    Schnurer, J.2    Wagner, E.G.3
  • 25
    • 0022555867 scopus 로고
    • Acidification of the endocytic and exocytic pathways
    • Mellman, I., Fuchs, R. Helenius, A. (1986) Acidification of the endocytic and exocytic pathways. Annu Rev Biochem 55 : 663 700.
    • (1986) Annu Rev Biochem , vol.55 , pp. 663-700
    • Mellman, I.1    Fuchs, R.2    Helenius, A.3
  • 26
    • 34147107933 scopus 로고    scopus 로고
    • Loss of vacuolar proton-translocating ATPase activity in yeast results in chronic oxidative stress
    • Milgrom, E., Diab, H., Middleton, F. Kane, P.M. (2007) Loss of vacuolar proton-translocating ATPase activity in yeast results in chronic oxidative stress. J Biol Chem 282 : 7125 7136.
    • (2007) J Biol Chem , vol.282 , pp. 7125-7136
    • Milgrom, E.1    Diab, H.2    Middleton, F.3    Kane, P.M.4
  • 27
    • 0025358278 scopus 로고
    • Disruption of genes encoding subunits of yeast vacuolar H(+)-ATPase causes conditional lethality
    • Nelson, H. Nelson, N. (1990) Disruption of genes encoding subunits of yeast vacuolar H(+)-ATPase causes conditional lethality. Proc Natl Acad Sci USA 87 : 3503 3507.
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 3503-3507
    • Nelson, H.1    Nelson, N.2
  • 28
    • 0034954008 scopus 로고    scopus 로고
    • Cell-mediated immunity to Histoplasma capsulatum
    • Newman, S.L. (2001) Cell-mediated immunity to Histoplasma capsulatum. Semin Respir Infect 16 : 102 108.
    • (2001) Semin Respir Infect , vol.16 , pp. 102-108
    • Newman, S.L.1
  • 29
    • 0026463563 scopus 로고
    • Colony-stimulating factors activate human macrophages to inhibit intracellular growth of Histoplasma capsulatum yeasts
    • Newman, S.L. Gootee, L. (1992) Colony-stimulating factors activate human macrophages to inhibit intracellular growth of Histoplasma capsulatum yeasts. Infect Immun 60 : 4593 4597.
    • (1992) Infect Immun , vol.60 , pp. 4593-4597
    • Newman, S.L.1    Gootee, L.2
  • 30
    • 0018953651 scopus 로고
    • Development of functional complement receptors during in vitro maturation of human monocytes into macrophages
    • Newman, S.L., Musson, R.A. Henson, P.M. (1980) Development of functional complement receptors during in vitro maturation of human monocytes into macrophages. J Immunol 125 : 2236 2244.
    • (1980) J Immunol , vol.125 , pp. 2236-2244
    • Newman, S.L.1    Musson, R.A.2    Henson, P.M.3
  • 31
    • 0025099677 scopus 로고
    • Phagocytosis of Histoplasma capsulatum yeasts and microconidia by human cultured macrophages and alveolar macrophages. Cellular cytoskeleton requirement for attachment and ingestion
    • Newman, S.L., Bucher, C., Rhodes, J. Bullock, W.E. (1990) Phagocytosis of Histoplasma capsulatum yeasts and microconidia by human cultured macrophages and alveolar macrophages. Cellular cytoskeleton requirement for attachment and ingestion. J Clin Invest 85 : 223 230.
    • (1990) J Clin Invest , vol.85 , pp. 223-230
    • Newman, S.L.1    Bucher, C.2    Rhodes, J.3    Bullock, W.E.4
  • 32
    • 0026777096 scopus 로고
    • Digestion of Histoplasma capsulatum yeasts by human macrophages
    • [published erratum appears in J Immunol 1992; 149: 3127].
    • Newman, S.L., Gootee, L., Morris, R. Bullock, W.E. (1992) Digestion of Histoplasma capsulatum yeasts by human macrophages. J Immunol 149 : 574 580 [published erratum appears in J Immunol 1992; 149: 3127].
    • (1992) J Immunol , vol.149 , pp. 574-580
    • Newman, S.L.1    Gootee, L.2    Morris, R.3    Bullock, W.E.4
  • 33
    • 0028350193 scopus 로고
    • Chloroquine induces human macrophage killing of Histoplasma capsulatum by limiting the availability of intracellular iron and is therapeutic in a murine model of histoplasmosis
    • Jr (
    • Newman, S.L., Gootee, L., Brunner, G. Deepe, G.S., Jr (1994) Chloroquine induces human macrophage killing of Histoplasma capsulatum by limiting the availability of intracellular iron and is therapeutic in a murine model of histoplasmosis. J Clin Invest 93 : 1422 1429.
    • (1994) J Clin Invest , vol.93 , pp. 1422-1429
    • Newman, S.L.1    Gootee, L.2    Brunner, G.3    Deepe, G.S.4
  • 34
    • 0029046492 scopus 로고
    • Inhibition of growth of Histoplasma capsulatum yeast cells in human macrophages by the iron chelator VUF 8514 and comparison of VUF 8514 with deferoxamine
    • Newman, S.L., Gootee, L., Stroobant, V., van der Goot, H. Boelaert, J.R. (1995) Inhibition of growth of Histoplasma capsulatum yeast cells in human macrophages by the iron chelator VUF 8514 and comparison of VUF 8514 with deferoxamine. Antimicrob Agents Chemother 39 : 1824 1829.
    • (1995) Antimicrob Agents Chemother , vol.39 , pp. 1824-1829
    • Newman, S.L.1    Gootee, L.2    Stroobant, V.3    Van Der Goot, H.4    Boelaert, J.R.5
  • 35
    • 31144467053 scopus 로고    scopus 로고
    • Human macrophages do not require phagosome acidification to mediate fungistatic/fungicidal activity against Histoplasma capsulatum
    • Newman, S.L., Gootee, L., Hilty, J. Morris, R.E. (2006) Human macrophages do not require phagosome acidification to mediate fungistatic/fungicidal activity against Histoplasma capsulatum. J Immunol 176 : 1806 1813.
    • (2006) J Immunol , vol.176 , pp. 1806-1813
    • Newman, S.L.1    Gootee, L.2    Hilty, J.3    Morris, R.E.4
  • 36
    • 0036481562 scopus 로고    scopus 로고
    • The vacuolar (H+)-ATPases - Nature's most versatile proton pumps
    • Nishi, T. Forgac, M. (2002) The vacuolar (H+)-ATPases - nature's most versatile proton pumps. Nat Rev Mol Cell Biol 3 : 94 103.
    • (2002) Nat Rev Mol Cell Biol , vol.3 , pp. 94-103
    • Nishi, T.1    Forgac, M.2
  • 37
    • 0028287443 scopus 로고
    • Detection, isolation, and characterization of siderophores
    • Payne, S.M. (1994) Detection, isolation, and characterization of siderophores. Methods Enzymol 235 : 329 344.
    • (1994) Methods Enzymol , vol.235 , pp. 329-344
    • Payne, S.M.1
  • 38
    • 19044365896 scopus 로고    scopus 로고
    • The putative vacuolar ATPase subunit Vma7p of Candida albicans is involved in vacuole acidification, hyphal development and virulence
    • Poltermann, S., Nguyen, M., Gunther, J., Wendland, J., Hartl, A., Kunkel, W., et al. (2005) The putative vacuolar ATPase subunit Vma7p of Candida albicans is involved in vacuole acidification, hyphal development and virulence. Microbiology 151 : 1645 1655.
    • (2005) Microbiology , vol.151 , pp. 1645-1655
    • Poltermann, S.1    Nguyen, M.2    Gunther, J.3    Wendland, J.4    Hartl, A.5    Kunkel, W.6
  • 39
    • 0016715330 scopus 로고
    • Difference between the two iron-binding sites of transferrin
    • Princiotto, J.V. Zapolski, E.J. (1975) Difference between the two iron-binding sites of transferrin. Nature 255 : 87 88.
    • (1975) Nature , vol.255 , pp. 87-88
    • Princiotto, J.V.1    Zapolski, E.J.2
  • 40
    • 3142621221 scopus 로고    scopus 로고
    • RNA interference in Histoplasma capsulatum demonstrates a role for alpha-(1,3)-glucan in virulence
    • Rappleye, C.A., Engle, J.T. Goldman, W.E. (2004) RNA interference in Histoplasma capsulatum demonstrates a role for alpha-(1,3)-glucan in virulence. Mol Microbiol 53 : 153 165.
    • (2004) Mol Microbiol , vol.53 , pp. 153-165
    • Rappleye, C.A.1    Engle, J.T.2    Goldman, W.E.3
  • 41
    • 0034680884 scopus 로고    scopus 로고
    • Intracellular parasitism by Histoplasma capsulatum: Fungal virulence and calcium dependence
    • Sebghati, T.S., Engle, J.T. Goldman, W.E. (2000) Intracellular parasitism by Histoplasma capsulatum: fungal virulence and calcium dependence. Science 290 : 1368 1372.
    • (2000) Science , vol.290 , pp. 1368-1372
    • Sebghati, T.S.1    Engle, J.T.2    Goldman, W.E.3
  • 42
    • 1542653185 scopus 로고    scopus 로고
    • High-throughput TAIL-PCR as a tool to identify DNA flanking insertions
    • Singer, T. Burke, E. (2003) High-throughput TAIL-PCR as a tool to identify DNA flanking insertions. Methods Mol Biol 236 : 241 272.
    • (2003) Methods Mol Biol , vol.236 , pp. 241-272
    • Singer, T.1    Burke, E.2
  • 43
    • 0031452168 scopus 로고    scopus 로고
    • Structure, function and regulation of the vacuolar (H+)-ATPase
    • Stevens, T.H. Forgac, M. (1997) Structure, function and regulation of the vacuolar (H+)-ATPase. Annu Rev Cell Dev Biol 13 : 779 808.
    • (1997) Annu Rev Cell Dev Biol , vol.13 , pp. 779-808
    • Stevens, T.H.1    Forgac, M.2
  • 44
    • 0011155271 scopus 로고    scopus 로고
    • Agrobacterium tumefaciens integrates transfer DNA into single chromosomal sites of dimorphic fungi and yields homokaryotic progeny from multinucleate yeast
    • Sullivan, T.D., Rooney, P.J. Klein, B.S. (2002) Agrobacterium tumefaciens integrates transfer DNA into single chromosomal sites of dimorphic fungi and yields homokaryotic progeny from multinucleate yeast. Eukaryot Cell 1 : 895 905.
    • (2002) Eukaryot Cell , vol.1 , pp. 895-905
    • Sullivan, T.D.1    Rooney, P.J.2    Klein, B.S.3
  • 45
    • 2342487990 scopus 로고    scopus 로고
    • Cells have distinct mechanisms to maintain protection against different reactive oxygen species: Oxidative-stress-response genes
    • Thorpe, G.W., Fong, C.S., Alic, N., Higgins, V.J. Dawes, I.W. (2004) Cells have distinct mechanisms to maintain protection against different reactive oxygen species: oxidative-stress-response genes. Proc Natl Acad Sci USA 101 : 6564 6569.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 6564-6569
    • Thorpe, G.W.1    Fong, C.S.2    Alic, N.3    Higgins, V.J.4    Dawes, I.W.5
  • 46
    • 0036548302 scopus 로고    scopus 로고
    • The mold-specific MS8 gene is required for normal hypha formation in the dimorphic pathogenic fungus Histoplasma capsulatum
    • Jr (
    • Tian, X. Shearer, G., Jr (2002) The mold-specific MS8 gene is required for normal hypha formation in the dimorphic pathogenic fungus Histoplasma capsulatum. Eukaryot Cell 1 : 249 256.
    • (2002) Eukaryot Cell , vol.1 , pp. 249-256
    • Tian, X.1    Shearer, G.2
  • 47
    • 0032702583 scopus 로고    scopus 로고
    • Ferric reduction is a potential iron acquisition mechanism for Histoplasma capsulatum
    • Timmerman, M.M. Woods, J.P. (1999) Ferric reduction is a potential iron acquisition mechanism for Histoplasma capsulatum. Infect Immun 67 : 6403 6408.
    • (1999) Infect Immun , vol.67 , pp. 6403-6408
    • Timmerman, M.M.1    Woods, J.P.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.