메뉴 건너뛰기




Volumn 11, Issue 4, 2008, Pages 318-324

Histoplasma capsulatum pathogenesis: making a lifestyle switch

Author keywords

[No Author keywords available]

Indexed keywords

BETA GLUCAN; CALCIUM BINDING PROTEIN; HEAT SHOCK PROTEIN 60;

EID: 48749117456     PISSN: 13695274     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.mib.2008.05.010     Document Type: Review
Times cited : (45)

References (49)
  • 2
    • 0030731699 scopus 로고    scopus 로고
    • Calcium dependence and binding in cultures of Histoplasma capsulatum
    • Batanghari J.W., and Goldman W.E. Calcium dependence and binding in cultures of Histoplasma capsulatum. Infect Immun 65 (1997) 5257-5261
    • (1997) Infect Immun , vol.65 , pp. 5257-5261
    • Batanghari, J.W.1    Goldman, W.E.2
  • 3
    • 0024286741 scopus 로고
    • Purification of membranes and identification of phase-specific proteins of the dimorphic pathogenic fungus Histoplasma capsulatum
    • Kumar B.V., and Maresca B. Purification of membranes and identification of phase-specific proteins of the dimorphic pathogenic fungus Histoplasma capsulatum. Arch Biochem Biophys 261 (1988) 212-221
    • (1988) Arch Biochem Biophys , vol.261 , pp. 212-221
    • Kumar, B.V.1    Maresca, B.2
  • 4
    • 0024577763 scopus 로고
    • Variable expression of a yeast-phase-specific gene in Histoplasma capsulatum strains differing in thermotolerance and virulence
    • Keath E.J., Painter A.A., Kobayashi G.S., and Medoff G. Variable expression of a yeast-phase-specific gene in Histoplasma capsulatum strains differing in thermotolerance and virulence. Infect Immun 57 (1989) 1384-1390
    • (1989) Infect Immun , vol.57 , pp. 1384-1390
    • Keath, E.J.1    Painter, A.A.2    Kobayashi, G.S.3    Medoff, G.4
  • 5
    • 0028269272 scopus 로고
    • Molecular cloning and sequence analysis of yps-3, a yeast-phase-specific gene in the dimorphic fungal pathogen Histoplasma capsulatum
    • Keath E.J., and Abidi F.E. Molecular cloning and sequence analysis of yps-3, a yeast-phase-specific gene in the dimorphic fungal pathogen Histoplasma capsulatum. Microbiology 140 (1994) 759-767
    • (1994) Microbiology , vol.140 , pp. 759-767
    • Keath, E.J.1    Abidi, F.E.2
  • 6
    • 0037632910 scopus 로고    scopus 로고
    • Identifying phase-specific genes in the fungal pathogen Histoplasma capsulatum using a genomic shotgun microarray
    • Hwang L., Hocking-Murray D., Bahrami A.K., Andersson M., Rine J., and Sil A. Identifying phase-specific genes in the fungal pathogen Histoplasma capsulatum using a genomic shotgun microarray. Mol Biol Cell 14 (2003) 2314-2326
    • (2003) Mol Biol Cell , vol.14 , pp. 2314-2326
    • Hwang, L.1    Hocking-Murray, D.2    Bahrami, A.K.3    Andersson, M.4    Rine, J.5    Sil, A.6
  • 7
    • 0031704439 scopus 로고    scopus 로고
    • Identification and isolation by DDRT-PCR of genes differentially expressed by Histoplasma capsulatum during macrophages infection
    • Colonna-Romano S., Porta A., Franco A., Kobayashi G.S., and Maresca B. Identification and isolation by DDRT-PCR of genes differentially expressed by Histoplasma capsulatum during macrophages infection. Microb Pathog 25 (1998) 55-66
    • (1998) Microb Pathog , vol.25 , pp. 55-66
    • Colonna-Romano, S.1    Porta, A.2    Franco, A.3    Kobayashi, G.S.4    Maresca, B.5
  • 8
    • 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., and Klein B.S. Agrobacterium tumefaciens integrates transfer DNA into single chromosomal sites of dimorphic fungi and yields homokaryotic progeny from multinucleate yeast. Eukaryot Cell 1 (2002) 895-905
    • (2002) Eukaryot Cell , vol.1 , pp. 895-905
    • Sullivan, T.D.1    Rooney, P.J.2    Klein, B.S.3
  • 9
    • 33646253928 scopus 로고    scopus 로고
    • Global control of dimorphism and virulence in fungi
    • By employing insertional mutagenesis, the authors identify the first regulatory protein required for transition of Histoplasma and Blastomyces to the yeast phase and confirm that this switch is necessary for virulence in mice.
    • Nemecek J.C., Wuthrich M., and Klein B.S. Global control of dimorphism and virulence in fungi. Science 312 (2006) 583-588. By employing insertional mutagenesis, the authors identify the first regulatory protein required for transition of Histoplasma and Blastomyces to the yeast phase and confirm that this switch is necessary for virulence in mice.
    • (2006) Science , vol.312 , pp. 583-588
    • Nemecek, J.C.1    Wuthrich, M.2    Klein, B.S.3
  • 10
    • 42449127140 scopus 로고    scopus 로고
    • Temperature-induced switch to the pathogenic yeast form of Histoplasma capsulatum requires Ryp1, a conserved transcriptional regulator
    • This study identifies RYP1 as a DNA-binding protein homolgous to Candida WOR1 that is necessary for the switch of Histoplasma from mycelial to the yeast phase. The authors further show through transcriptional profiling of the mutant cells that in the absence of RYP1, cells remain locked in a mycelial-like state. These results highlight a mechanism by which differentiation into the yeast phase is triggered and maintained at the transcriptional level.
    • Nguyen V.Q., and Sil A. Temperature-induced switch to the pathogenic yeast form of Histoplasma capsulatum requires Ryp1, a conserved transcriptional regulator. Proc Natl Acad Sci U S A 105 (2008) 4880-4885. This study identifies RYP1 as a DNA-binding protein homolgous to Candida WOR1 that is necessary for the switch of Histoplasma from mycelial to the yeast phase. The authors further show through transcriptional profiling of the mutant cells that in the absence of RYP1, cells remain locked in a mycelial-like state. These results highlight a mechanism by which differentiation into the yeast phase is triggered and maintained at the transcriptional level.
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 4880-4885
    • Nguyen, V.Q.1    Sil, A.2
  • 12
    • 35648964750 scopus 로고    scopus 로고
    • Interlocking transcriptional feedback loops control white-opaque switching in Candida albicans
    • Zordan R.E., Miller M.G., Galgoczy D.J., Tuch B.B., and Johnson A.D. Interlocking transcriptional feedback loops control white-opaque switching in Candida albicans. PLoS Biol 5 (2007) e256
    • (2007) PLoS Biol , vol.5
    • Zordan, R.E.1    Miller, M.G.2    Galgoczy, D.J.3    Tuch, B.B.4    Johnson, A.D.5
  • 13
    • 0028961046 scopus 로고
    • The essential transcription factor, Mcm1, is a downstream target of Sln1, a yeast "two-component" regulator
    • Yu G., Deschenes R.J., and Fassler J.S. The essential transcription factor, Mcm1, is a downstream target of Sln1, a yeast "two-component" regulator. J Biol Chem 270 (1995) 8739-8743
    • (1995) J Biol Chem , vol.270 , pp. 8739-8743
    • Yu, G.1    Deschenes, R.J.2    Fassler, J.S.3
  • 15
    • 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., and Bullock W.E. 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 (1990) 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
  • 16
    • 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., and Wright SD. Role of the adherence-promoting receptors, CR3, LFA-1, and p150,95, in binding of Histoplasma capsulatum by human macrophages. J Exp Med 165 (1987) 195-210
    • (1987) J Exp Med , vol.165 , pp. 195-210
    • Bullock, W.E.1    Wright SD2
  • 17
    • 0034122721 scopus 로고    scopus 로고
    • CR3: a general purpose adhesion-recognition receptor essential for innate immunity
    • Ehlers M.R. CR3: a general purpose adhesion-recognition receptor essential for innate immunity. Microbes Infect 2 (2000) 289-294
    • (2000) Microbes Infect , vol.2 , pp. 289-294
    • Ehlers, M.R.1
  • 18
    • 0037223264 scopus 로고    scopus 로고
    • Identification of heat shock protein 60 as the ligand on Histoplasma capsulatum that mediates binding to CD18 receptors on human macrophages
    • Long K.H., Gomez F.J., Morris R.E., and Newman S.L. Identification of heat shock protein 60 as the ligand on Histoplasma capsulatum that mediates binding to CD18 receptors on human macrophages. J Immunol 170 (2003) 487-494
    • (2003) J Immunol , vol.170 , pp. 487-494
    • Long, K.H.1    Gomez, F.J.2    Morris, R.E.3    Newman, S.L.4
  • 21
    • 37849045813 scopus 로고    scopus 로고
    • C-type lectin receptors in antifungal immunity
    • Willment J.A., and Brown G.D. C-type lectin receptors in antifungal immunity. Trends Microbiol 16 (2008) 27-32
    • (2008) Trends Microbiol , vol.16 , pp. 27-32
    • Willment, J.A.1    Brown, G.D.2
  • 22
    • 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., and Goldman W.E. RNA interference in Histoplasma capsulatum demonstrates a role for alpha-(1,3)-glucan in virulence. Mol Microbiol 53 (2004) 153-165
    • (2004) Mol Microbiol , vol.53 , pp. 153-165
    • Rappleye, C.A.1    Engle, J.T.2    Goldman, W.E.3
  • 23
    • 33846573404 scopus 로고    scopus 로고
    • Histoplasma capsulatum alpha-(1,3)-glucan blocks innate immune recognition by the beta-glucan receptor
    • This study demonstrates that Histoplasma α-glucan creates an outer cell wall layer that hides cell wall β-glucans from detection by macrophage Dectin-1 receptors. These results establish the molecular mechanism by which α-glucan contributes to Histoplasma virulence and provide an explanation for the decreased virulence of strains lacking α-glucan.
    • Rappleye C.A., Eissenberg L.G., and Goldman W.E. Histoplasma capsulatum alpha-(1,3)-glucan blocks innate immune recognition by the beta-glucan receptor. Proc Natl Acad Sci U S A 104 (2007) 1366-1370. This study demonstrates that Histoplasma α-glucan creates an outer cell wall layer that hides cell wall β-glucans from detection by macrophage Dectin-1 receptors. These results establish the molecular mechanism by which α-glucan contributes to Histoplasma virulence and provide an explanation for the decreased virulence of strains lacking α-glucan.
    • (2007) Proc Natl Acad Sci U S A , vol.104 , pp. 1366-1370
    • Rappleye, C.A.1    Eissenberg, L.G.2    Goldman, W.E.3
  • 25
    • 33750480548 scopus 로고    scopus 로고
    • An alpha-(1,4)-amylase is essential for alpha-(1,3)-glucan production and virulence in Histoplasma capsulatum
    • This genetic study of the biosynthesis of the α-glucan virulence factor identifies two enzymes that contribute to the formation of the cell wall polysaccharide and suggests that Histoplasma α-glucan may contain α-(1,4)-linked glucans in addition to the predominant α-(1,3)-linked polysaccharides.
    • Marion C.L., Rappleye C.A., Engle J.T., and Goldman W.E. An alpha-(1,4)-amylase is essential for alpha-(1,3)-glucan production and virulence in Histoplasma capsulatum. Mol Microbiol 62 (2006) 970-983. This genetic study of the biosynthesis of the α-glucan virulence factor identifies two enzymes that contribute to the formation of the cell wall polysaccharide and suggests that Histoplasma α-glucan may contain α-(1,4)-linked glucans in addition to the predominant α-(1,3)-linked polysaccharides.
    • (2006) Mol Microbiol , vol.62 , pp. 970-983
    • Marion, C.L.1    Rappleye, C.A.2    Engle, J.T.3    Goldman, W.E.4
  • 27
    • 33745483791 scopus 로고    scopus 로고
    • An alpha-amylase homologue, aah3, encodes a GPI-anchored membrane protein required for cell wall integrity and morphogenesis in Schizosaccharomyces pombe
    • Morita T., Tanaka N., Hosomi A., Giga-Hama Y., and Takegawa K. An alpha-amylase homologue, aah3, encodes a GPI-anchored membrane protein required for cell wall integrity and morphogenesis in Schizosaccharomyces pombe. Biosci Biotechnol Biochem 70 (2006) 1454-1463
    • (2006) Biosci Biotechnol Biochem , vol.70 , pp. 1454-1463
    • Morita, T.1    Tanaka, N.2    Hosomi, A.3    Giga-Hama, Y.4    Takegawa, K.5
  • 28
    • 0029609797 scopus 로고
    • Genomic cloning, characterization, and functional analysis of the major surface adhesin WI-1 on Blastomyces dermatitidis yeasts
    • Hogan L.H., Josvai S., and Klein B.S. Genomic cloning, characterization, and functional analysis of the major surface adhesin WI-1 on Blastomyces dermatitidis yeasts. J Biol Chem 270 (1995) 30725-30732
    • (1995) J Biol Chem , vol.270 , pp. 30725-30732
    • Hogan, L.H.1    Josvai, S.2    Klein, B.S.3
  • 29
    • 18044392276 scopus 로고    scopus 로고
    • Surface localization of the Yps3p protein of Histoplasma capsulatum
    • Bohse M.L., and Woods J.P. Surface localization of the Yps3p protein of Histoplasma capsulatum. Eukaryot Cell 4 (2005) 685-693
    • (2005) Eukaryot Cell , vol.4 , pp. 685-693
    • Bohse, M.L.1    Woods, J.P.2
  • 30
    • 0037384573 scopus 로고    scopus 로고
    • A C-terminal EGF-like domain governs BAD1 localization to the yeast surface and fungal adherence to phagocytes, but is dispensable in immune modulation and pathogenicity of Blastomyces dermatitidis
    • Brandhorst T., Wuthrich M., Finkel-Jimenez B., and Klein B. A C-terminal EGF-like domain governs BAD1 localization to the yeast surface and fungal adherence to phagocytes, but is dispensable in immune modulation and pathogenicity of Blastomyces dermatitidis. Mol Microbiol 48 (2003) 53-65
    • (2003) Mol Microbiol , vol.48 , pp. 53-65
    • Brandhorst, T.1    Wuthrich, M.2    Finkel-Jimenez, B.3    Klein, B.4
  • 31
    • 34249909212 scopus 로고    scopus 로고
    • RNA interference-mediated silencing of the YPS3 gene of Histoplasma capsulatum reveals virulence defects
    • The authors of this study provide evidence that YPS3 contributes to the virulence of Histoplasma by facilitating dissemination of yeast from the lung.
    • Bohse M.L., and Woods J.P. RNA interference-mediated silencing of the YPS3 gene of Histoplasma capsulatum reveals virulence defects. Infect Immun 75 (2007) 2811-2817. The authors of this study provide evidence that YPS3 contributes to the virulence of Histoplasma by facilitating dissemination of yeast from the lung.
    • (2007) Infect Immun , vol.75 , pp. 2811-2817
    • Bohse, M.L.1    Woods, J.P.2
  • 32
    • 34247893840 scopus 로고    scopus 로고
    • Expression and interstrain variability of the YPS3 gene of Histoplasma capsulatum
    • Bohse M.L., and Woods J.P. Expression and interstrain variability of the YPS3 gene of Histoplasma capsulatum. Eukaryot Cell 6 (2007) 609-615
    • (2007) Eukaryot Cell , vol.6 , pp. 609-615
    • Bohse, M.L.1    Woods, J.P.2
  • 33
    • 0015335837 scopus 로고
    • Comparative pathogenicity of albino and brown types of Histoplasma capsulatum for mice
    • Tewari R.P., and Berkhout F.J. Comparative pathogenicity of albino and brown types of Histoplasma capsulatum for mice. J Infect Dis 125 (1972) 504-508
    • (1972) J Infect Dis , vol.125 , pp. 504-508
    • Tewari, R.P.1    Berkhout, F.J.2
  • 34
    • 34548433981 scopus 로고    scopus 로고
    • The genetic basis of variation in susceptibility to infection with Histoplasma capsulatum in the mouse
    • Mayfield J.A., and Rine J. The genetic basis of variation in susceptibility to infection with Histoplasma capsulatum in the mouse. Genes Immun 8 (2007) 468-474
    • (2007) Genes Immun , vol.8 , pp. 468-474
    • Mayfield, J.A.1    Rine, J.2
  • 35
    • 0036604083 scopus 로고    scopus 로고
    • BAD1, an essential virulence factor of Blastomyces dermatitidis, suppresses host TNF-alpha production through TGF-beta-dependent and -independent mechanisms
    • Finkel-Jimenez B., Wuthrich M., and Klein B.S. BAD1, an essential virulence factor of Blastomyces dermatitidis, suppresses host TNF-alpha production through TGF-beta-dependent and -independent mechanisms. J Immunol 168 (2002) 5746-5755
    • (2002) J Immunol , vol.168 , pp. 5746-5755
    • Finkel-Jimenez, B.1    Wuthrich, M.2    Klein, B.S.3
  • 36
    • 0035865065 scopus 로고    scopus 로고
    • The WI-1 adhesin blocks phagocyte TNF-alpha production, imparting pathogenicity on Blastomyces dermatitidis
    • Finkel-Jimenez B., Wuthrich M., Brandhorst T., and Klein B.S. The WI-1 adhesin blocks phagocyte TNF-alpha production, imparting pathogenicity on Blastomyces dermatitidis. J Immunol 166 (2001) 2665-2673
    • (2001) J Immunol , vol.166 , pp. 2665-2673
    • Finkel-Jimenez, B.1    Wuthrich, M.2    Brandhorst, T.3    Klein, B.S.4
  • 38
    • 0347988036 scopus 로고    scopus 로고
    • Antibodies to a cell surface histone-like protein protect against Histoplasma capsulatum
    • Nosanchuk J.D., Steenbergen J.N., Shi L., Deepe Jr. G.S., and Casadevall A. Antibodies to a cell surface histone-like protein protect against Histoplasma capsulatum. J Clin Invest 112 (2003) 1164-1175
    • (2003) J Clin Invest , vol.112 , pp. 1164-1175
    • Nosanchuk, J.D.1    Steenbergen, J.N.2    Shi, L.3    Deepe Jr., G.S.4    Casadevall, A.5
  • 39
    • 0000116620 scopus 로고    scopus 로고
    • Histoplasma acquisition of calcium and expression of CBP1 during intracellular parasitism
    • Batanghari J.W., Deepe Jr. G.S., Di Cera E., and Goldman W.E. Histoplasma acquisition of calcium and expression of CBP1 during intracellular parasitism. Mol Microbiol 27 (1998) 531-539
    • (1998) Mol Microbiol , vol.27 , pp. 531-539
    • Batanghari, J.W.1    Deepe Jr., G.S.2    Di Cera, E.3    Goldman, W.E.4
  • 40
    • 0034522850 scopus 로고    scopus 로고
    • Monitoring phase-specific gene expression in Histoplasma capsulatum with telomeric GFP fusion plasmids
    • Kugler S., Young B., Miller V.L., and Goldman W.E. Monitoring phase-specific gene expression in Histoplasma capsulatum with telomeric GFP fusion plasmids. Cell Microbiol 2 (2000) 537-547
    • (2000) Cell Microbiol , vol.2 , pp. 537-547
    • Kugler, S.1    Young, B.2    Miller, V.L.3    Goldman, W.E.4
  • 41
    • 0031953491 scopus 로고    scopus 로고
    • Probing the yeast phase-specific expression of the CBP1 gene in Histoplasma capsulatum
    • Patel J.B., Batanghari J.W., and Goldman W.E. Probing the yeast phase-specific expression of the CBP1 gene in Histoplasma capsulatum. J Bacteriol 180 (1998) 1786-1792
    • (1998) J Bacteriol , vol.180 , pp. 1786-1792
    • Patel, J.B.1    Batanghari, J.W.2    Goldman, W.E.3
  • 42
    • 0034680884 scopus 로고    scopus 로고
    • Intracellular parasitism by Histoplasma capsulatum: fungal virulence and calcium dependence
    • Sebghati T.S., Engle J.T., and Goldman W.E. Intracellular parasitism by Histoplasma capsulatum: fungal virulence and calcium dependence. Science 290 (2000) 1368-1372
    • (2000) Science , vol.290 , pp. 1368-1372
    • Sebghati, T.S.1    Engle, J.T.2    Goldman, W.E.3
  • 43
    • 42049113174 scopus 로고    scopus 로고
    • Structural features responsible for the biological stability of Histoplasma's virulence factor CBP
    • This study characterizes the CBP virulence factor biochemically and establishes the parameters for calcium binding as well as the folding and multimeric state of CBP. The CBP protein is surprisingly resistant to proteolysis and other harsh treatments that the authors suggest contribute to its function within the phagolysosome.
    • Beck M.R., Dekoster G.T., Hambly D.M., Gross M.L., Cistola D.P., and Goldman W.E. Structural features responsible for the biological stability of Histoplasma's virulence factor CBP. Biochemistry 47 (2008) 4427-4438. This study characterizes the CBP virulence factor biochemically and establishes the parameters for calcium binding as well as the folding and multimeric state of CBP. The CBP protein is surprisingly resistant to proteolysis and other harsh treatments that the authors suggest contribute to its function within the phagolysosome.
    • (2008) Biochemistry , vol.47 , pp. 4427-4438
    • Beck, M.R.1    Dekoster, G.T.2    Hambly, D.M.3    Gross, M.L.4    Cistola, D.P.5    Goldman, W.E.6
  • 44
    • 48749126518 scopus 로고    scopus 로고
    • Beck MR, DeKoster GT, Cistola DP, Goldman WE: NMR structure of a fungal virulence factor reveals structural homology with mammalian saposin B. 2008, submitted for publication
    • Beck MR, DeKoster GT, Cistola DP, Goldman WE: NMR structure of a fungal virulence factor reveals structural homology with mammalian saposin B. 2008, submitted for publication. This study describes the first high-resolution structure of a fungal virulence protein. The authors' use of structure-based comparisons instead of amino acid sequence identify CBP as a member of the saposin-like protein family, revealing an unsuspected role for CBP in lipid interactions.
  • 45
    • 34548563758 scopus 로고    scopus 로고
    • Production of extracellular proteolytic activity by Histoplasma capsulatum grown in Histoplasma-macrophage medium is limited to restriction fragment length polymorphism class 1 isolates
    • Zarnowski R., Connolly P.A., Wheat L.J., and Woods J.P. Production of extracellular proteolytic activity by Histoplasma capsulatum grown in Histoplasma-macrophage medium is limited to restriction fragment length polymorphism class 1 isolates. Diagn Microbiol Infect Dis 59 (2007) 39-47
    • (2007) Diagn Microbiol Infect Dis , vol.59 , pp. 39-47
    • Zarnowski, R.1    Connolly, P.A.2    Wheat, L.J.3    Woods, J.P.4
  • 46
    • 0032702583 scopus 로고    scopus 로고
    • Ferric reduction is a potential iron acquisition mechanism for Histoplasma capsulatum
    • Timmerman M.M., and Woods J.P. Ferric reduction is a potential iron acquisition mechanism for Histoplasma capsulatum. Infect Immun 67 (1999) 6403-6408
    • (1999) Infect Immun , vol.67 , pp. 6403-6408
    • Timmerman, M.M.1    Woods, J.P.2
  • 47
    • 0034059728 scopus 로고    scopus 로고
    • Hydroxamate siderophores of Histoplasma capsulatum
    • Howard D.H., Rafie R., Tiwari A., and Faull K.F. Hydroxamate siderophores of Histoplasma capsulatum. Infect Immun 68 (2000) 2338-2343
    • (2000) Infect Immun , vol.68 , pp. 2338-2343
    • Howard, D.H.1    Rafie, R.2    Tiwari, A.3    Faull, K.F.4
  • 48
    • 0035189288 scopus 로고    scopus 로고
    • Potential role for extracellular glutathione-dependent ferric reductase in utilization of environmental and host ferric compounds by Histoplasma capsulatum
    • Timmerman M.M., and Woods J.P. Potential role for extracellular glutathione-dependent ferric reductase in utilization of environmental and host ferric compounds by Histoplasma capsulatum. Infect Immun 69 (2001) 7671-7678
    • (2001) Infect Immun , vol.69 , pp. 7671-7678
    • Timmerman, M.M.1    Woods, J.P.2
  • 49
    • 22144479376 scopus 로고    scopus 로고
    • Glutathione-dependent extracellular ferric reductase activities in dimorphic zoopathogenic fungi
    • Zarnowski R., and Woods J.P. Glutathione-dependent extracellular ferric reductase activities in dimorphic zoopathogenic fungi. Microbiology 151 (2005) 2233-2240
    • (2005) Microbiology , vol.151 , pp. 2233-2240
    • Zarnowski, R.1    Woods, J.P.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.