메뉴 건너뛰기
Infection and Immunity
Volumn 82, Issue 1, 2014, Pages 393-404
Histoplasma capsulatum depends on de novo vitamin biosynthesis for intraphagosomal proliferation
Author keywords

[No Author keywords available]
Indexed keywords

BIOTIN; GENOMIC DNA; HYGROMYCIN; INOSITOL; NICOTINIC ACID; PANTOTHENATE CALCIUM; RIBOFLAVIN; RNA; THIAMINE; URACIL; VITAMIN;
EID: 84890850924     PISSN: 00199567     EISSN: 10985522     Source Type: Journal    
DOI: 10.1128/IAI.00824-13     Document Type: Article
Times cited : (43)
References (74)
  • 1
    • 33846535287 scopus 로고    scopus 로고
    • Histoplasmosis: a clinical and laboratory update
    • Kauffman CA. 2007. Histoplasmosis: a clinical and laboratory update. Clin. Microbiol. Rev. 20:115-132. http://dx.doi.org/10.1128/CMR.00027-06.
    • (2007) Clin. Microbiol. Rev. , vol.20 , pp. 115-132
    • Kauffman, C.A.1
  • 2
    • 42449127140 scopus 로고    scopus 로고
    • Temperature-induced switch to the pathogenic yeast form of Histoplasma capsulatum requires Ryp1, a conserved transcriptional regulator
    • Nguyen VQ, Sil A. 2008. Temperature-induced switch to the pathogenic yeast form of Histoplasma capsulatum requires Ryp1, a conserved transcriptional regulator. Proc. Natl. Acad. Sci. U.S.A. 105:4880-4885. http://dx.doi.org/10.1073/pnas.0710448105.
    • (2008) Proc. Natl. Acad. Sci. U.S.A. , vol.105 , pp. 4880-4885
    • Nguyen, V.Q.1    Sil, A.2
  • 3
    • 0023146087 scopus 로고
    • Role of the adherence-promoting receptors, CR3, LFA-1, and p150,95, in binding of Histoplasma capsulatum by human macrophages
    • Bullock WE, Wright SD. 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. http://dx.doi.org/10.1084/jem.165.1.195.
    • (1987) J. Exp. Med. , vol.165 , pp. 195-210
    • Bullock, W.E.1    Wright, S.D.2
  • 4
    • 77954686993 scopus 로고    scopus 로고
    • Distinct roles of complement receptor 3, Dectin-1, and sialic acids in murine macrophage interaction with Histoplasma yeast
    • Lin J-S, Huang J-H, Hung L-Y, Wu S-Y, Wu-Hsieh BA. 2010. Distinct roles of complement receptor 3, Dectin-1, and sialic acids in murine macrophage interaction with Histoplasma yeast. J. Leukoc. Biol. 88:95-106. http://dx.doi.org/10.1189/jlb.1109717.
    • (2010) J. Leukoc. Biol. , vol.88 , pp. 95-106
    • Lin, J.-S.1    Huang, J.-H.2    Hung, L.-Y.3    Wu, S.-Y.4    Wu-Hsieh, B.A.5
  • 5
    • 84879438579 scopus 로고    scopus 로고
    • Redundant catalases detoxify phagocyte reactive oxygen and facilitate Histoplasma pathogenesis
    • Holbrook ED, Smolnycki KA, Youseff BH, Rappleye CA. 2013. Redundant catalases detoxify phagocyte reactive oxygen and facilitate Histoplasma pathogenesis. Infect. Immun. 81:2334-2346. http://dx.doi.org/10.1128/IAI.00173-13.
    • (2013) Infect. Immun. , vol.81 , pp. 2334-2346
    • Holbrook, E.D.1    Smolnycki, K.A.2    Youseff, B.H.3    Rappleye, C.A.4
  • 6
    • 84863692804 scopus 로고    scopus 로고
    • Extracellular superoxide dismutase protects Histoplasma yeast cells from hostderived oxidative stress
    • Youseff BH, Holbrook ED, Smolnycki KA, Rappleye CA. 2012. Extracellular superoxide dismutase protects Histoplasma yeast cells from hostderived oxidative stress. PLoS Pathog. 8:e1002713. http://dx.doi.org/10.1371/journal.ppat.1002713.
    • (2012) PLoS Pathog. , vol.8
    • Youseff, B.H.1    Holbrook, E.D.2    Smolnycki, K.A.3    Rappleye, C.A.4
  • 7
    • 0036777063 scopus 로고    scopus 로고
    • Life and death in a macrophage: role of the glyoxylate cycle in virulence
    • Lorenz MC, Fink GR. 2002. Life and death in a macrophage: role of the glyoxylate cycle in virulence. Eukaryot. Cell 1:657-662. http://dx.doi.org/10.1128/EC.1.5.657-662.2002.
    • (2002) Eukaryot. Cell , vol.1 , pp. 657-662
    • Lorenz, M.C.1    Fink, G.R.2
  • 8
    • 38049129044 scopus 로고    scopus 로고
    • The Leishmania-macrophage interaction: a metabolic perspective
    • Naderer T, McConville MJ. 2008. The Leishmania-macrophage interaction: a metabolic perspective. Cell. Microbiol. 10:301-308. http://dx.doi.org/10.1111/j.1462-5822.2007.01096.x.
    • (2008) Cell. Microbiol. , vol.10 , pp. 301-308
    • Naderer, T.1    McConville, M.J.2
  • 9
    • 33644819211 scopus 로고    scopus 로고
    • Carbon metabolism of intracellular bacteria
    • Muñoz-Elías EJ, McKinney JD. 2006. Carbon metabolism of intracellular bacteria. Cell. Microbiol. 8:10-22. http://dx.doi.org/10.1111/j.1462-5822.2005.00648.x.
    • (2006) Cell. Microbiol. , vol.8 , pp. 10-22
    • Muñoz-Elías, E.J.1    McKinney, J.D.2
  • 10
    • 34548591486 scopus 로고    scopus 로고
    • Mycobacterium tuberculosis and the environment within the phagosome
    • Rohde K, Yates RM, Purdy GE, Russell DG. 2007. Mycobacterium tuberculosis and the environment within the phagosome. Immunol. Rev. 219:37-54. http://dx.doi.org/10.1111/j.1600-065X.2007.00547.x.
    • (2007) Immunol. Rev. , vol.219 , pp. 37-54
    • Rohde, K.1    Yates, R.M.2    Purdy, G.E.3    Russell, D.G.4
  • 11
    • 0242268400 scopus 로고    scopus 로고
    • Genetic requirements for mycobacterial survival during infection
    • Sassetti CM, Rubin EJ. 2003. Genetic requirements for mycobacterial survival during infection. Proc. Natl. Acad. Sci. U.S.A. 100:12989-12994. http://dx.doi.org/10.1073/pnas.2134250100.
    • (2003) Proc. Natl. Acad. Sci. U.S.A. , vol.100 , pp. 12989-12994
    • Sassetti, C.M.1    Rubin, E.J.2
  • 12
    • 23844483451 scopus 로고    scopus 로고
    • Cryptococcus neoformans gene expression during murine macrophage infection
    • Fan W, Kraus PR, Boily M-J, Heitman J. 2005. Cryptococcus neoformans gene expression during murine macrophage infection. Eukaryot. Cell 4:1420-1433. http://dx.doi.org/10.1128/EC.4.8.1420-1433.2005.
    • (2005) Eukaryot. Cell , vol.4 , pp. 1420-1433
    • Fan, W.1    Kraus, P.R.2    Boily, M.-J.3    Heitman, J.4
  • 13
    • 50049125079 scopus 로고    scopus 로고
    • Metabolic adaptation in Cryptococcus neoformans during early murine pulmonary infection
    • Hu G, Cheng P-Y, Sham A, Perfect JR, Kronstad JW. 2008. Metabolic adaptation in Cryptococcus neoformans during early murine pulmonary infection. Mol. Microbiol. 69:1456-1475. http://dx.doi.org/10.1111/j.1365-2958.2008.06374.x.
    • (2008) Mol. Microbiol. , vol.69 , pp. 1456-1475
    • Hu, G.1    Cheng, P.-Y.2    Sham, A.3    Perfect, J.R.4    Kronstad, J.W.5
  • 14
    • 84858001166 scopus 로고    scopus 로고
    • Legionella pneumophila transcriptome during intracellular multiplication in human macrophages
    • Faucher SP, Mueller CA, Shuman HA. 2011. Legionella pneumophila transcriptome during intracellular multiplication in human macrophages. Front. Microbiol. 2:60. http://dx.doi.org/10.3389/fmicb.2011.00060.
    • (2011) Front. Microbiol. , vol.2 , pp. 60
    • Faucher, S.P.1    Mueller, C.A.2    Shuman, H.A.3
  • 15
    • 22244434967 scopus 로고    scopus 로고
    • The phagosomal transporter A couples threonine acquisition to differentiation and replication of Legionella pneumophila in macrophages
    • Sauer J-D, Bachman MA, Swanson MS. 2005. The phagosomal transporter A couples threonine acquisition to differentiation and replication of Legionella pneumophila in macrophages. Proc. Natl. Acad. Sci. U.S.A. 102:9924-9929. http://dx.doi.org/10.1073/pnas.0502767102.
    • (2005) Proc. Natl. Acad. Sci. U.S.A. , vol.102 , pp. 9924-9929
    • Sauer, J.-D.1    Bachman, M.A.2    Swanson, M.S.3
  • 16
    • 84855196338 scopus 로고    scopus 로고
    • Cryptococcus neoformans requires a functional glycolytic pathway for disease but not persistence in the host
    • Price MS, Betancourt-Quiroz M, Price JL, Toffaletti DL, Vora H, Hu G, Kronstad JW, Perfect JR. 2011. Cryptococcus neoformans requires a functional glycolytic pathway for disease but not persistence in the host. mBio 2(3):e00103- 00111. http://dx.doi.org/10.1128/mBio.00103-11.
    • (2011) mBio , vol.2 , Issue.3
    • Price, M.S.1    Betancourt-Quiroz, M.2    Price, J.L.3    Toffaletti, D.L.4    Vora, H.5    Hu, G.6    Kronstad, J.W.7    Perfect, J.R.8
  • 17
    • 6344285788 scopus 로고    scopus 로고
    • Transcriptional response of Candida albicans upon internalization by macrophages
    • Lorenz MC, Bender JA, Fink GR. 2004. Transcriptional response of Candida albicans upon internalization by macrophages. Eukaryot. Cell 3:1076-1087. http://dx.doi.org/10.1128/EC.3.5.1076-1087.2004.
    • (2004) Eukaryot. Cell , vol.3 , pp. 1076-1087
    • Lorenz, M.C.1    Bender, J.A.2    Fink, G.R.3
  • 20
    • 33748655254 scopus 로고    scopus 로고
    • Mycobacterial mutants with defective control of phagosomal acidification
    • Stewart GR, Patel J, Robertson BD, Rae A, Young DB. 2005. Mycobacterial mutants with defective control of phagosomal acidification. PLoS Pathog. 1:269-278. http://dx.doi.org/10.1371/journal.ppat.0010033.
    • (2005) PLoS Pathog. , vol.1 , pp. 269-278
    • Stewart, G.R.1    Patel, J.2    Robertson, B.D.3    Rae, A.4    Young, D.B.5
  • 22
    • 0034011567 scopus 로고    scopus 로고
    • The putative iron transport system SitABCD encoded on SPI1 is required for full virulence of Salmonella typhimurium
    • Janakiraman A, Slauch JM. 2000. The putative iron transport system SitABCD encoded on SPI1 is required for full virulence of Salmonella typhimurium. Mol. Microbiol. 35:1146-1155. http://dx.doi.org/10.1046/j.1365-2958.2000.01783.x.
    • (2000) Mol. Microbiol. , vol.35 , pp. 1146-1155
    • Janakiraman, A.1    Slauch, J.M.2
  • 23
    • 11144250804 scopus 로고    scopus 로고
    • Tuberculosis-metabolism and respiration in the absence of growth
    • Boshoff HIM, Barry CE, III. 2005. Tuberculosis-metabolism and respiration in the absence of growth. Nat. Rev. Microbiol. 3:70-80. http://dx.doi.org/10.1038/nrmicro1065.
    • (2005) Nat. Rev. Microbiol. , vol.3 , pp. 70-80
    • Boshoff, H.I.M.1    Barry I.I.I, C.E.2
  • 24
    • 34548622179 scopus 로고    scopus 로고
    • Infection-related gene expres-sion in Candida albicans
    • Brown AJP, Odds FC, Gow NAR. 2007. Infection-related gene expres-sion in Candida albicans. Curr. Opin. Microbiol. 10:307-313. http://dx.doi.org/10.1016/j.mib.2007.04.001.
    • (2007) Curr. Opin. Microbiol. , vol.10 , pp. 307-313
    • Brown, A.J.P.1    Odds, F.C.2    Gow, N.A.R.3
  • 25
    • 34249887901 scopus 로고    scopus 로고
    • Legionella pneumophila adaptation to intracellular life and the host response: clues from genomics and transcriptomics
    • Jules M, Buchrieser C. 2007. Legionella pneumophila adaptation to intracellular life and the host response: clues from genomics and transcriptomics. FEBS Lett. 581:2829-2838. http://dx.doi.org/10.1016/j.febslet.2007.05.026.
    • (2007) FEBS Lett. , vol.581 , pp. 2829-2838
    • Jules, M.1    Buchrieser, C.2
  • 27
  • 28
    • 0011146965 scopus 로고
    • Cysteine and related compounds in the growth of the yeast like phase of Histoplasma capsulatum
    • Salvin SB. 1949. Cysteine and related compounds in the growth of the yeast like phase of Histoplasma capsulatum. J. Infect. Dis. 84:275-283. http://dx.doi.org/10.1093/infdis/84.3.275.
    • (1949) J. Infect. Dis. , vol.84 , pp. 275-283
    • Salvin, S.B.1
  • 29
    • 0018844929 scopus 로고
    • Cysteine transport and sulfite reductase activity in a germination-defective mutant of Histoplasma capsulatum
    • Howard DH, Dabrowa N, Otto V, Rhodes J. 1980. Cysteine transport and sulfite reductase activity in a germination-defective mutant of Histoplasma capsulatum. J. Bacteriol. 141:417-421.
    • (1980) J. Bacteriol. , vol.141 , pp. 417-421
    • Howard, D.H.1    Dabrowa, N.2    Otto, V.3    Rhodes, J.4
  • 30
    • 0017157995 scopus 로고
    • Possible role for cysteine biosynthesis in conversion from mycelial to yeast form of Histoplasma capsulatum
    • Boguslawski G, Akagi JM, Ward LG. 1976. Possible role for cysteine biosynthesis in conversion from mycelial to yeast form of Histoplasma capsulatum. Nature 261:336-338. http://dx.doi.org/10.1038/261336a0.
    • (1976) Nature , vol.261 , pp. 336-338
    • Boguslawski, G.1    Akagi, J.M.2    Ward, L.G.3
  • 31
    • 0018372580 scopus 로고
    • Cysteine biosynthesis in a fungus, Histoplasma capsulatum
    • Stetler DA, Boguslawski G. 1979. Cysteine biosynthesis in a fungus, Histoplasma capsulatum. Sabouraudia 17:23-34. http://dx.doi.org/10.1080/00362177985380041.
    • (1979) Sabouraudia , vol.17 , pp. 23-34
    • Stetler, D.A.1    Boguslawski, G.2
  • 32
    • 0018354230 scopus 로고
    • Aspects of physiology of Histoplasma capsulatum. (A review)
    • Boguslawski G, Stetler DA. 1979. Aspects of physiology of Histoplasma capsulatum. (A review). Mycopathologia 67:17-24. http://dx.doi.org/10.1007/BF00436235.
    • (1979) Mycopathologia , vol.67 , pp. 17-24
    • Boguslawski, G.1    Stetler, D.A.2
  • 33
    • 0015509264 scopus 로고
    • Factors affecting mycelial to yeast phase conversion and growth of the yeast phase of Histoplasma capsulatum
    • McVeigh I, Houston WE. 1972. Factors affecting mycelial to yeast phase conversion and growth of the yeast phase of Histoplasma capsulatum. Mycopathol. Mycol. Appl. 47:135-151. http://dx.doi.org/10.1007/BF02126161.
    • (1972) Mycopathol. Mycol. Appl. , vol.47 , pp. 135-151
    • McVeigh, I.1    Houston, W.E.2
  • 34
    • 0014725223 scopus 로고
    • The uptake of low molecular weight sulfur-containing compounds by Histoplasma capsulatum and related dimorphic fungi
    • Garrison RG, Dodd HT, Hamilton JW. 1970. The uptake of low molecular weight sulfur-containing compounds by Histoplasma capsulatum and related dimorphic fungi. Mycopathol. Mycol. Appl. 40:171-180. http://dx.doi.org/10.1007/BF02051995.
    • (1970) Mycopathol. Mycol. Appl. , vol.40 , pp. 171-180
    • Garrison, R.G.1    Dodd, H.T.2    Hamilton, J.W.3
  • 35
    • 0014234060 scopus 로고
    • Monitored environment system to control cell growth, morphology, and metabolic rate in fungi by oxidation-reduction potentials
    • Rippon JW. 1968. Monitored environment system to control cell growth, morphology, and metabolic rate in fungi by oxidation-reduction potentials. Appl. Microbiol. 16:114-121.
    • (1968) Appl. Microbiol. , vol.16 , pp. 114-121
    • Rippon, J.W.1
  • 36
    • 0026321552 scopus 로고
    • Intracellular growth inhibition of Histoplasma capsulatum induced in murine macrophages by recombinant gamma interferon is not due to a limitation of the supply of methionine or cysteine to the fungus
    • Wu-Hsieh BA, Howard DH. 1992. Intracellular growth inhibition of Histoplasma capsulatum induced in murine macrophages by recombinant gamma interferon is not due to a limitation of the supply of methionine or cysteine to the fungus. Infect. Immun. 60:698-700.
    • (1992) Infect. Immun. , vol.60 , pp. 698-700
    • Wu-Hsieh, B.A.1    Howard, D.H.2
  • 37
    • 0020024546 scopus 로고
    • Cysteine-independent and cysteinerequiring yeast-strains of Histoplasma capsulatum
    • Jacobson ES, Harrell AC. 1982. Cysteine-independent and cysteinerequiring yeast-strains of Histoplasma capsulatum. Mycopathologia 77: 69-73. http://dx.doi.org/10.1007/BF00437386.
    • (1982) Mycopathologia , vol.77 , pp. 69-73
    • Jacobson, E.S.1    Harrell, A.C.2
  • 38
    • 0020078713 scopus 로고
    • A prototrophic yeast-strain of Histoplasma capsulatum
    • Jacobson ES, Harrell AC. 1982. A prototrophic yeast-strain of Histoplasma capsulatum. Mycopathologia 77:65-68. http://dx.doi.org/10.1007/BF00437385.
    • (1982) Mycopathologia , vol.77 , pp. 65-68
    • Jacobson, E.S.1    Harrell, A.C.2
  • 39
    • 0032038703 scopus 로고    scopus 로고
    • Electrotransformation and expression of bacterial genes encoding hygromycin phosphotransferase and β-galactosidase in the pathogenic fungus Histoplasma capsulatum
    • Woods JP, Heinecke EL, Goldman WE. 1998. Electrotransformation and expression of bacterial genes encoding hygromycin phosphotransferase and β-galactosidase in the pathogenic fungus Histoplasma capsulatum. Infect. Immun. 66:1697-1707.
    • (1998) Infect. Immun. , vol.66 , pp. 1697-1707
    • Woods, J.P.1    Heinecke, E.L.2    Goldman, W.E.3
  • 40
    • 0032932156 scopus 로고    scopus 로고
    • The URA5 gene is necessary for Histoplasma capsulatum growth during infection of mouse and human cells
    • Retallack DM, Heinecke EL, Gibbons R, Deepe GS, Jr, Woods JP. 1999. The URA5 gene is necessary for Histoplasma capsulatum growth during infection of mouse and human cells. Infect. Immun. 67:624-629.
    • (1999) Infect. Immun. , vol.67 , pp. 624-629
    • Retallack, D.M.1    Heinecke, E.L.2    Gibbons, R.3    Deepe Jr., G.S.4    Woods, J.P.5
  • 41
    • 0032702583 scopus 로고    scopus 로고
    • Ferric reduction is a potential iron acquisition mechanism for Histoplasma capsulatum
    • Timmerman MM, Woods JP. 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
  • 42
    • 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 MM, Woods JP. 2001. Potential role for extracellular glutathione-dependent ferric reductase in utilization of environmental and host ferric compounds by Histoplasma capsulatum. Infect. Immun. 69:7671-7678. http://dx.doi.org/10.1128/IAI.69.12.7671-7678.2001.
    • (2001) Infect. Immun. , vol.69 , pp. 7671-7678
    • Timmerman, M.M.1    Woods, J.P.2
  • 43
    • 43049121756 scopus 로고    scopus 로고
    • Histoplasma requires SID1, a member of an iron-regulated siderophore gene cluster, for host colonization
    • Hwang LH, Mayfield JA, Rine J, Sil A. 2008. Histoplasma requires SID1, a member of an iron-regulated siderophore gene cluster, for host colonization. PLoS Pathog. 4:31000044. http://dx.doi.org/10.1371/journal.ppat.1000044.
    • (2008) PLoS Pathog. , vol.4 , pp. 31000044
    • Hwang, L.H.1    Mayfield, J.A.2    Rine, J.3    Sil, A.4
  • 44
    • 51649086978 scopus 로고    scopus 로고
    • The Histoplasma capsulatum vacuolar ATPase is required for iron homeostasis, intracellular replication in macrophages, and virulence in a murine model of histoplasmosis
    • Hilty J, Smulian AG, Newman SL. 2008. The Histoplasma capsulatum vacuolar ATPase is required for iron homeostasis, intracellular replication in macrophages, and virulence in a murine model of histoplasmosis. Mol. Microbiol. 70:127-139. http://dx.doi.org/10.1111/j.1365-2958.2008.06395.x.
    • (2008) Mol. Microbiol. , vol.70 , pp. 127-139
    • Hilty, J.1    Smulian, A.G.2    Newman, S.L.3
  • 45
    • 52649152402 scopus 로고    scopus 로고
    • Histoplasma capsulatum secreted γ-glutamyltransferase reduces iron by generating an efficient ferric reductant
    • Zarnowski R, Cooper KG, Brunold LS, Calaycay J, Woods JP. 2008. Histoplasma capsulatum secreted γ-glutamyltransferase reduces iron by generating an efficient ferric reductant. Mol. Microbiol. 70:352-368. http://dx.doi.org/10.1111/j.1365-2958.2008.06410.x.
    • (2008) Mol. Microbiol. , vol.70 , pp. 352-368
    • Zarnowski, R.1    Cooper, K.G.2    Brunold, L.S.3    Calaycay, J.4    Woods, J.P.5
  • 46
    • 84907123709 scopus 로고
    • Quantitative plating of Histoplasma capsulatum without addition of conditioned medium or siderophores
    • Worsham PL, Goldman WE. 1988. Quantitative plating of Histoplasma capsulatum without addition of conditioned medium or siderophores. Med. Mycol. 26:137-143. http://dx.doi.org/10.1080/02681218880000211.
    • (1988) Med. Mycol. , vol.26 , pp. 137-143
    • Worsham, P.L.1    Goldman, W.E.2
  • 47
    • 84858121094 scopus 로고    scopus 로고
    • Agrobacterium-mediated insertional mutagenesis in Histoplasma capsulatum
    • Brand, AC, MacCallum, DM (ed). Humana Press, New York, NY.
    • Zemska O, Rappleye CA. 2012. Agrobacterium-mediated insertional mutagenesis in Histoplasma capsulatum, p 51-66. In Brand, AC, MacCallum, DM (ed), Host-fungus interactions. Humana Press, New York, NY.
    • (2012) Host-fungus interactions , pp. 51-66
    • Zemska, O.1    Rappleye, C.A.2
  • 48
    • 79961103495 scopus 로고    scopus 로고
    • Discovery of a role for Hsp82 in histoplasma virulence through a quantitative screen for macrophage lethality
    • Edwards JA, Zemska O, Rappleye CA. 2011. Discovery of a role for Hsp82 in histoplasma virulence through a quantitative screen for macrophage lethality. Infect. Immun. 79:3348-3357. http://dx.doi.org/10.1128/IAI.05124-11.
    • (2011) Infect. Immun. , vol.79 , pp. 3348-3357
    • Edwards, J.A.1    Zemska, O.2    Rappleye, C.A.3
  • 49
    • 84872619971 scopus 로고    scopus 로고
    • Spectrum of T-DNA integrations for insertional mutagenesis of Histoplasma capsulatum
    • Kemski MM, Stevens B, Rappleye CA. 2013. Spectrum of T-DNA integrations for insertional mutagenesis of Histoplasma capsulatum. Fungal Biol. 117:41-51. http://dx.doi.org/10.1016/j.funbio.2012.11.004.
    • (2013) Fungal Biol. , vol.117 , pp. 41-51
    • Kemski, M.M.1    Stevens, B.2    Rappleye, C.A.3
  • 50
    • 36448931584 scopus 로고    scopus 로고
    • High-efficiency thermal asymmetric interlaced PCR for amplification of unknown flanking sequences
    • 654 passim
    • Liu Y-G, Chen Y. 2007. High-efficiency thermal asymmetric interlaced PCR for amplification of unknown flanking sequences. Biotechniques 43:649-650, 652, 654 passim. http://dx.doi.org/10.2144/000112601.
    • (2007) Biotechniques , vol.43
    • Liu, Y.-G.1    Chen, Y.2
  • 51
    • 34547588704 scopus 로고    scopus 로고
    • KAAS: an automatic genome annotation and pathway reconstruction server
    • Moriya Y, Itoh M, Okuda S, Yoshizawa AC, Kanehisa M. 2007. KAAS: an automatic genome annotation and pathway reconstruction server. Nucleic Acids Res. 35:W182-W185. http://dx.doi.org/10.1093/nar/gkm321.
    • (2007) Nucleic Acids Res. , vol.35
    • Moriya, Y.1    Itoh, M.2    Okuda, S.3    Yoshizawa, A.C.4    Kanehisa, M.5
  • 52
    • 84885094068 scopus 로고    scopus 로고
    • Histoplasma yeast and mycelial transcriptomes reveal pathogenicphase and lineage-specific gene expression profiles
    • Edwards JA, Chen C, Kemski MM, Hu J, Mitchell TK, Rappleye CA. 2013. Histoplasma yeast and mycelial transcriptomes reveal pathogenicphase and lineage-specific gene expression profiles. BMC Genomics 14: 695. http://dx.doi.org/10.1186/1471-2164-14-695.
    • (2013) BMC Genomics , vol.14 , pp. 695
    • Edwards, J.A.1    Chen, C.2    Kemski, M.M.3    Hu, J.4    Mitchell, T.K.5    Rappleye, C.A.6
  • 53
    • 84858130222 scopus 로고    scopus 로고
    • RNAi-based gene silencing using a GFP sentinel system in Histoplasma capsulatum
    • Brand AC, MacCallum DM (ed). Humana Press, New York, NY.
    • Youseff BH, Rappleye CA. 2012. RNAi-based gene silencing using a GFP sentinel system in Histoplasma capsulatum, p 151-164. In Brand AC, MacCallum DM (ed), Host-fungus interactions. Humana Press, New York, NY.
    • (2012) Host-fungus interactions , pp. 151-164
    • Youseff, B.H.1    Rappleye, C.A.2
  • 54
    • 30444455439 scopus 로고    scopus 로고
    • Internalization and phagosome escape required for Francisella to induce human monocyte IL-1β processing and release
    • Gavrilin MA, Bouakl IJ, Knatz NL, Duncan MD, Hall MW, Gunn JS, Wewers MD. 2006. Internalization and phagosome escape required for Francisella to induce human monocyte IL-1β processing and release. Proc. Natl. Acad. Sci. U.S.A. 103:141-146. http://dx.doi.org/10.1073/pnas.0504271103.
    • (2006) Proc. Natl. Acad. Sci. U.S.A. , vol.103 , pp. 141-146
    • Gavrilin, M.A.1    Bouakl, I.J.2    Knatz, N.L.3    Duncan, M.D.4    Hall, M.W.5    Gunn, J.S.6    Wewers, M.D.7
  • 55
    • 44949231424 scopus 로고    scopus 로고
    • Analyzing real-time PCR data by the comparative C(T) method
    • Schmittgen TD, Livak KJ. 2008. Analyzing real-time PCR data by the comparative C(T) method. Nat. Protoc. 3:1101-1108. http://dx.doi.org/10.1038/nprot.2008.73.
    • (2008) Nat. Protoc. , vol.3 , pp. 1101-1108
    • Schmittgen, T.D.1    Livak, K.J.2
  • 56
    • 33750480548 scopus 로고    scopus 로고
    • An α-(1,4)-amylase is essential for α-(1,3)-glucan production and virulence in Histoplasma capsulatum
    • Marion CL, Rappleye CA, Engle JT, Goldman WE. 2006. An α-(1,4)-amylase is essential for α-(1,3)-glucan production and virulence in Histoplasma capsulatum. Mol. Microbiol. 62:970-983. http://dx.doi.org/10.1111/j.1365-2958.2006.05436.x.
    • (2006) Mol. Microbiol. , vol.62 , pp. 970-983
    • Marion, C.L.1    Rappleye, C.A.2    Engle, J.T.3    Goldman, W.E.4
  • 57
    • 0014642157 scopus 로고
    • Biochemical and genetic classification of riboflavine deficient mutants of Saccharomyces cerevisiae
    • Oltmanns O, Bacher A, Lingens F, Zimmermann FK. 1969. Biochemical and genetic classification of riboflavine deficient mutants of Saccharomyces cerevisiae. Mol. Gen. Genet. 105:306-313. http://dx.doi.org/10.1007/BF00277585.
    • (1969) Mol. Gen. Genet. , vol.105 , pp. 306-313
    • Oltmanns, O.1    Bacher, A.2    Lingens, F.3    Zimmermann, F.K.4
  • 58
    • 0013847218 scopus 로고
    • Nutritional studies of Histoplasma capsulatum
    • McVeigh I, Morton K. 1965. Nutritional studies of Histoplasma capsulatum. Mycopathol. Mycol. Appl. 25:294-308. http://dx.doi.org/10.1007/BF02049917.
    • (1965) Mycopathol. Mycol. Appl. , vol.25 , pp. 294-308
    • McVeigh, I.1    Morton, K.2
  • 59
    • 3142621221 scopus 로고    scopus 로고
    • RNA interference in Histoplasma capsulatum demonstrates a role for α-(1,3)-glucan in virulence
    • Rappleye CA, Engle JT, Goldman WE. 2004. RNA interference in Histoplasma capsulatum demonstrates a role for α-(1,3)-glucan in virulence. Mol. Microbiol. 53:153-165. http://dx.doi.org/10.1111/j.1365-2958.2004.04131.x.
    • (2004) Mol. Microbiol. , vol.53 , pp. 153-165
    • Rappleye, C.A.1    Engle, J.T.2    Goldman, W.E.3
  • 60
    • 78651483688 scopus 로고    scopus 로고
    • The yeast-phase virulence requirement for α-glucan synthase differs among Histoplasma capsulatum chemotypes
    • Edwards JA, Alore EA, Rappleye CA. 2011. The yeast-phase virulence requirement for α-glucan synthase differs among Histoplasma capsulatum chemotypes. Eukaryot. Cell 10:87-97. http://dx.doi.org/10.1128/EC.00214-10.
    • (2011) Eukaryot. Cell , vol.10 , pp. 87-97
    • Edwards, J.A.1    Alore, E.A.2    Rappleye, C.A.3
  • 61
    • 0034917354 scopus 로고    scopus 로고
    • Cu,Zn superoxide dismutase of Mycobacterium tuberculosis contributes to survival in activated macrophages that are generating an oxidative burst
    • Piddington DL, Fang FC, Laessig T, Cooper AM, Orme IM, Buchmeier NA. 2001. Cu,Zn superoxide dismutase of Mycobacterium tuberculosis contributes to survival in activated macrophages that are generating an oxidative burst. Infect. Immun. 69:4980-4987. http://dx.doi.org/10.1128/IAI.69.8.4980-4987.2001.
    • (2001) Infect. Immun. , vol.69 , pp. 4980-4987
    • Piddington, D.L.1    Fang, F.C.2    Laessig, T.3    Cooper, A.M.4    Orme, I.M.5    Buchmeier, N.A.6
  • 62
    • 17144368786 scopus 로고    scopus 로고
    • Granulocytes govern the transcriptional response, morphology and proliferation of Candida albicans in human blood
    • Fradin C, De Groot P, MacCallum D, Schaller M, Klis F, Odds FC, Hube B. 2005. Granulocytes govern the transcriptional response, morphology and proliferation of Candida albicans in human blood. Mol. Microbiol. 56:397-415. http://dx.doi.org/10.1111/j.1365-2958.2005.04557.x.
    • (2005) Mol. Microbiol. , vol.56 , pp. 397-415
    • Fradin, C.1    De Groot, P.2    MacCallum, D.3    Schaller, M.4    Klis, F.5    Odds, F.C.6    Hube, B.7
  • 63
    • 70350449301 scopus 로고    scopus 로고
    • Identification of Francisella tularensis live vaccine strain CuZn superoxide dismutase as critical for resistance to extracellularly generated reactive oxygen species
    • Melillo AA, Mahawar M, Sellati TJ, Malik M, Metzger DW, Melendez JA, Bakshi CS. 2009. Identification of Francisella tularensis live vaccine strain CuZn superoxide dismutase as critical for resistance to extracellularly generated reactive oxygen species. J. Bacteriol. 191:6447-6456. http://dx.doi.org/10.1128/JB.00534-09.
    • (2009) J. Bacteriol. , vol.191 , pp. 6447-6456
    • Melillo, A.A.1    Mahawar, M.2    Sellati, T.J.3    Malik, M.4    Metzger, D.W.5    Melendez, J.A.6    Bakshi, C.S.7
  • 65
    • 0742288065 scopus 로고    scopus 로고
    • Superoxide dismutases in Candida albicans: transcriptional regulation and functional characterization of the hyphal-induced SOD5 gene
    • Martchenko M, Alarco A-M, Harcus D, Whiteway M. 2004. Superoxide dismutases in Candida albicans: transcriptional regulation and functional characterization of the hyphal-induced SOD5 gene. Mol. Biol. Cell 15: 456-467. http://dx.doi.org/10.1091/mbc.E03-03-0179.
    • (2004) Mol. Biol. Cell , vol.15 , pp. 456-467
    • Martchenko, M.1    Alarco, A.-M.2    Harcus, D.3    Whiteway, M.4
  • 68
    • 20444419421 scopus 로고    scopus 로고
    • Genome-wide requirements for Mycobacterium tuberculosis adaptation and survival in macrophages
    • Rengarajan J, Bloom BR, Rubin EJ. 2005. Genome-wide requirements for Mycobacterium tuberculosis adaptation and survival in macrophages. Proc. Natl. Acad. Sci. U.S.A. 102:8327-8332. http://dx.doi.org/10.1073/pnas.0503272102.
    • (2005) Proc. Natl. Acad. Sci. U.S.A. , vol.102 , pp. 8327-8332
    • Rengarajan, J.1    Bloom, B.R.2    Rubin, E.J.3
  • 69
    • 0036796061 scopus 로고    scopus 로고
    • A pantothenate auxotroph of Mycobacterium tuberculosis is highly attenuated and protects mice against tuberculosis
    • Sambandamurthy VK, Wang X, Chen B, Russell RG, Derrick S, Collins FM, Morris SL, Jacobs WR. 2002. A pantothenate auxotroph of Mycobacterium tuberculosis is highly attenuated and protects mice against tuberculosis. Nat. Med. 8:1171-1174. http://dx.doi.org/10.1038/nm765.
    • (2002) Nat. Med. , vol.8 , pp. 1171-1174
    • Sambandamurthy, V.K.1    Wang, X.2    Chen, B.3    Russell, R.G.4    Derrick, S.5    Collins, F.M.6    Morris, S.L.7    Jacobs, W.R.8
  • 71
    • 0242488961 scopus 로고    scopus 로고
    • Development of a synthetic minimal medium for Listeria monocytogenes
    • Tsai H-N, Hodgson DA. 2003. Development of a synthetic minimal medium for Listeria monocytogenes. Appl. Environ. Microbiol. 69:6943-6945. http://dx.doi.org/10.1128/AEM.69.11.6943-6945.2003.
    • (2003) Appl. Environ. Microbiol. , vol.69 , pp. 6943-6945
    • Tsai, H.-N.1    Hodgson, D.A.2
  • 72
    • 78650610793 scopus 로고    scopus 로고
    • MMAR_2770, a new enzyme involved in biotin biosynthesis, is essential for the growth of Mycobacterium marinum in macrophages and zebrafish
    • Yu J, Niu C, Wang D, Li M, Teo W, Sun G, Wang J, Liu J, Gao Q. 2011. MMAR_2770, a new enzyme involved in biotin biosynthesis, is essential for the growth of Mycobacterium marinum in macrophages and zebrafish. Microbes Infect. Inst. Pasteur 13:33-41. http://dx.doi.org/10.1016/j.micinf.2010.08.010.
    • (2011) Microbes Infect. Inst. Pasteur , vol.13 , pp. 33-41
    • Yu, J.1    Niu, C.2    Wang, D.3    Li, M.4    Teo, W.5    Sun, G.6    Wang, J.7    Liu, J.8    Gao, Q.9
  • 74
    • 78651007240 scopus 로고
    • The effects of biochemical mutation on the virulence of Bacterium typhosum: the virulence of mutants
    • Bacon GA, Burrows TW, Yates M. 1950. The effects of biochemical mutation on the virulence of Bacterium typhosum: the virulence of mutants. Br. J. Exp. Pathol. 31:714-724.
    • (1950) Br. J. Exp. Pathol. , vol.31 , pp. 714-724
    • Bacon, G.A.1    Burrows, T.W.2    Yates, M.3

* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.