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Volumn 47, Issue 8, 2009, Pages 845-854

Characterization of a secreted aspartyl protease of the fungal pathogen Paracoccidioides brasiliensis

Author keywords

Gelatinolitic activity; N glycosylation; Paracoccidioides brasiliensis; Secreted aspartyl protease

Indexed keywords

ASPARTIC PROTEINASE; POLYCLONAL ANTIBODY; PROTEOME; RECOMBINANT ENZYME; RNA; TUNICAMYCIN; COMPLEMENTARY DNA; ENZYME PRECURSOR; FUNGAL PROTEIN; GELATIN; RECOMBINANT PROTEIN;

EID: 73649107910     PISSN: 13693786     EISSN: 14602709     Source Type: Journal    
DOI: 10.3109/13693780802695512     Document Type: Article
Times cited : (32)

References (39)
  • 1
    • 0027484850 scopus 로고
    • Host-parasite relationship in paracoccidioidomycosis
    • Franco M, Peracoli MT, Soares A, et al. Host-parasite relationship in paracoccidioidomycosis. Curr Top Med Mycol 1993; 5: 115-149.
    • (1993) Curr Top Med Mycol , vol.5 , pp. 115-149
    • Franco, M.1    Peracoli, M.T.2    Soares, A.3
  • 2
    • 0023209825 scopus 로고
    • Evolution in the structure and function of aspartic proteases
    • Tang J, Wong RN. Evolution in the structure and function of aspartic proteases. J Cell Biochem 1987; 33: 53-63.
    • (1987) J Cell Biochem , vol.33 , pp. 53-63
    • Tang, J.1    Wong, R.N.2
  • 3
    • 0025290527 scopus 로고
    • The structure and function of the aspartic proteinases
    • Davies DR. The structure and function of the aspartic proteinases. Annu Rev Biophys Chem 1990; 19: 189-215.
    • (1990) Annu Rev Biophys Chem , vol.19 , pp. 189-215
    • Davies, D.R.1
  • 4
    • 0029004315 scopus 로고
    • Families of aspartic peptidases and those of unknown catalytic mechanism
    • Rawling N, Barret AJ. Families of aspartic peptidases and those of unknown catalytic mechanism. Methods Enzymol 1995; 248: 105-120.
    • (1995) Methods Enzymol , vol.248 , pp. 105-120
    • Rawling, N.1    Barret, A.J.2
  • 5
    • 0141789642 scopus 로고    scopus 로고
    • Candida albicans secreted aspartyl proteinases in virulence and pathogenesis
    • Naglik JR, Challacombe SJ, Hube B. Candida albicans secreted aspartyl proteinases in virulence and pathogenesis. Microbiol Mol Biol Rev 2003; 67: 400-428.
    • (2003) Microbiol Mol Biol Rev , vol.67 , pp. 400-428
    • Naglik, J.R.1    Challacombe, S.J.2    Hube, B.3
  • 6
    • 34547887623 scopus 로고    scopus 로고
    • Differential expression of Candida albicans secreted aspartyl proteinase in human vulvovaginal candidiasis
    • Lian CH, Liu WD. Differential expression of Candida albicans secreted aspartyl proteinase in human vulvovaginal candidiasis. Mycoses 2007; 50: 383-390.
    • (2007) Mycoses , vol.50 , pp. 383-390
    • Lian, C.H.1    Liu, W.D.2
  • 7
    • 38349187889 scopus 로고    scopus 로고
    • Azole antifungals induce up-regulation of SAP4, SAP5 and SAP6 secreted proteinase genes in filamentous Candida albicans cells in vitro and in vivo
    • Barelle CJ, Duncan VM, Brown AJ, Gow NA, Odds FC. Azole antifungals induce up-regulation of SAP4, SAP5 and SAP6 secreted proteinase genes in filamentous Candida albicans cells in vitro and in vivo. J Antimicrob Chemother 2008; 61: 315-322.
    • (2008) J Antimicrob Chemother , vol.61 , pp. 315-322
    • Barelle, C.J.1    Duncan, V.M.2    Brown, A.J.3    Gow, N.A.4    Odds, F.C.5
  • 8
    • 0029125381 scopus 로고
    • Molecular cloning of the cDNA and gene for an elastinolytic aspartic proteinase from Aspergillus fumigatus and evidence of its secretion by the fungus during invasion of the host lung
    • Lee JD, Kolattukudy PE. Molecular cloning of the cDNA and gene for an elastinolytic aspartic proteinase from Aspergillus fumigatus and evidence of its secretion by the fungus during invasion of the host lung. Infect Immun 1995; 63: 3796-3803.
    • (1995) Infect Immun , vol.63 , pp. 3796-3803
    • Lee, J.D.1    Kolattukudy, P.E.2
  • 9
    • 29644437768 scopus 로고    scopus 로고
    • A recombinant aspartyl protease of Coccidioides posadasii induces protection against pulmonary coccidioidiomycosis in mice
    • Tarcha EJ, Basrur V, Hung C, Gardner MJ, Cole GT. A recombinant aspartyl protease of Coccidioides posadasii induces protection against pulmonary coccidioidiomycosis in mice. Infect Immun 2006; 74: 516-527.
    • (2006) Infect Immun , vol.74 , pp. 516-527
    • Tarcha, E.J.1    Basrur, V.2    Hung, C.3    Gardner, M.J.4    Cole, G.T.5
  • 10
    • 33645572564 scopus 로고    scopus 로고
    • Transcriptome overview of Paracoccidioides brasiliensis proteases
    • Parente JA, Costa M, Pereira M, Soares CM. Transcriptome overview of Paracoccidioides brasiliensis proteases. Genet Mol Res 2005; 4: 358-371.
    • (2005) Genet Mol Res , vol.4 , pp. 358-371
    • Parente, J.A.1    Costa, M.2    Pereira, M.3    Soares, C.M.4
  • 11
    • 0029015199 scopus 로고
    • Characterization of an exocellular serine-thiol proteinase activity in Paracoccidioides brasiliensis
    • Carmona AK, Puccia R, Oliveira MC, et al. Characterization of an exocellular serine-thiol proteinase activity in Paracoccidioides brasiliensis. Biochem J 1995; 309: 209-214.
    • (1995) Biochem J , vol.309 , pp. 209-214
    • Carmona, A.K.1    Puccia, R.2    Oliveira, M.C.3
  • 12
    • 33746431354 scopus 로고    scopus 로고
    • Exocellular proteolytic activity of Paracoccidioides brasiliensis : CCCleavage of components associated with the basement membrane
    • Puccia R, Carmona AK, Gesztesi JL, Juliano L, Travassos LR. Exocellular proteolytic activity of Paracoccidioides brasiliensis : cleavage of components associated with the basement membrane. Med Mycol 1998; 36: 345-348.
    • (1998) Med Mycol , vol.36 , pp. 345-348
    • Puccia, R.1    Carmona, A.K.2    Gesztesi, J.L.3    Juliano, L.4    Travassos, L.R.5
  • 13
    • 31344480419 scopus 로고    scopus 로고
    • Modulation of the exocellular serine-thiol proteinase activity of Paracoccidioides brasiliensis by neutral polysaccharides
    • Matsuo AL, Tersariol II, Kobata SI, et al. Modulation of the exocellular serine-thiol proteinase activity of Paracoccidioides brasiliensis by neutral polysaccharides. Microbes Infect 2006; 8: 84-91.
    • (2006) Microbes Infect , vol.8 , pp. 84-91
    • Matsuo, A.L.1    Tersariol, I.I.2    Kobata, S.I.3
  • 14
    • 34247550086 scopus 로고    scopus 로고
    • The transcriptome analysis of early morphogenesis in Paracoccidioides brasiliensis mycelium reveals novel and induced genes potentially associated to the dimorphic process
    • Bastos KP, Bailao AM, Borges CL, et al. The transcriptome analysis of early morphogenesis in Paracoccidioides brasiliensis mycelium reveals novel and induced genes potentially associated to the dimorphic process. BMC Microbiol 2007; 7: 29.
    • (2007) BMC Microbiol , vol.7 , pp. 29
    • Bastos, K.P.1    Bailao, A.M.2    Borges, C.L.3
  • 15
    • 0036138208 scopus 로고    scopus 로고
    • Serum stimulates growth of and proteinase secretion by Aspergillus fumigatus
    • Gifford AHT, Klippenstein JR, Moore MM. Serum stimulates growth of and proteinase secretion by Aspergillus fumigatus. Infect Immun 2002; 70: 19-26.
    • (2002) Infect Immun , vol.70 , pp. 19-26
    • Gifford, A.H.T.1    Klippenstein, J.R.2    Moore, M.M.3
  • 18
    • 0030801002 scopus 로고    scopus 로고
    • Gapped BLAST and PSI-BLAST: A new generation of protein database search programs
    • Altschul SF, Madden TL, Schaffer AA, et al. Gapped BLAST and PSI-BLAST: a new generation of protein database search programs. Nucleic Acids Res 1997; 25: 3389-3402.
    • (1997) Nucleic Acids Res , vol.25 , pp. 3389-3402
    • Altschul, S.F.1    Madden, T.L.2    Schaffer, A.A.3
  • 19
    • 84928586383 scopus 로고    scopus 로고
    • National Center for Biotechnology Information [updated 9 May 2008] Available from : http://www.ncbi.nlm.nih.gov
    • NCBI ( http://www.ncbi.nlm.nih.gov/ ). National Center for Biotechnology Information [updated 9 May 2008]. Available from : http://www.ncbi.nlm.nih.gov
  • 20
    • 84928585719 scopus 로고    scopus 로고
    • Motif Scan, ExPASy (Expert Protein Analysis System) Proteomics Server [ updated 21 April 2008]. Available from : http://ca.expasy.org/
    • MotifScan ( http://hits.isb-sib.ch/cgi-bin/PFSCAN ). ExPASy (Expert Protein Analysis System)Proteomics Server [updated 21 April 2008]. Available from : http://ca.expasy.org/
  • 21
    • 84928583807 scopus 로고    scopus 로고
    • Scan Prosite, ExPASy (Expert Protein Analysis System) Proteomics Server [ updated 21 April 2008]. Available from : http://ca.expasy.org/
    • ScanProsite ( http://ca.expasy.org/tools/scanprosite/ ). ExPASy (Expert Protein Analysis System)Proteomics Server [updated 21 April 2008]. Available from : http://ca.expasy.org/
  • 22
    • 84928591324 scopus 로고    scopus 로고
    • Signal P 3.0, ExPASy (Expert Protein Analysis System) Proteomics Server [updated 21 April 2008] Available from : http://ca.expasy.org/
    • SignalP 3.0 ( http://www.cbs.dtu.dk/services/SignalP/ ). ExPASy (Expert Protein Analysis System)Proteomics Server [updated 21 April 2008]. Available from : http://ca.expasy.org/
  • 23
    • 84928582895 scopus 로고    scopus 로고
    • The PSORT II Prediction site [updated 24 November 1999]
    • PSORTII Prediction ( http://psort.ims.u-tokyo.ac.jp/form2.html ). The PSORT II Prediction site [updated 24 November 1999]
  • 24
    • 0031574072 scopus 로고    scopus 로고
    • The Clustal X windows interface: Flexible strategies for multiple sequence alignment aided by quantity analysis tools
    • Thompson JD, Gibson TJ, Plewniak F, Jeanmougin F, Higgins DG. The Clustal X windows interface: flexible strategies for multiple sequence alignment aided by quantity analysis tools. Nucleic Acids Res 1997; 25: 4876-4882.
    • (1997) Nucleic Acids Res , vol.25 , pp. 4876-4882
    • Thompson, J.D.1    Gibson, T.J.2    Plewniak, F.3    Jeanmougin, F.4    Higgins, D.G.5
  • 25
    • 0004262043 scopus 로고    scopus 로고
    • Molecular cloning
    • Sambrook J, Russel DW (eds). 2nd edn. New York : Cold Spring Harbor Laboratory Press
    • Sambrook J, Russel DW (eds). Molecular Cloning. A Laboratory Manual. 2nd edn. New York : Cold Spring Harbor Laboratory Press, 2001.
    • (2001) A Laboratory Manual
  • 26
    • 0036130164 scopus 로고    scopus 로고
    • Heterologous expression, purification and immunological reactivity of a recombinant HSP60 from Paracoccidioides brasiliensis
    • Cunha DA, Zancope-Oliveira RM, Felipe MSS, et al. Heterologous expression, purification and immunological reactivity of a recombinant HSP60 from Paracoccidioides brasiliensis. Clin Diagn Lab Immunol 2002; 9: 374-377.
    • (2002) Clin Diagn Lab Immunol , vol.9 , pp. 374-377
    • Cunha, D.A.1    Zancope-Oliveira, R.M.2    Felipe, M.S.S.3
  • 27
    • 0034969626 scopus 로고    scopus 로고
    • Two-dimensional electrophoresis and characterization of antigens from Paracoccidioides brasiliensis
    • Fonseca CA, Jesuino RS, Felipe MSS, et al. Two-dimensional electrophoresis and characterization of antigens from Paracoccidioides brasiliensis. Microbes Infect 2001; 3: 535-542.
    • (2001) Microbes Infect , vol.3 , pp. 535-542
    • Fonseca, C.A.1    Jesuino, R.S.2    Felipe, M.S.S.3
  • 28
    • 0038631572 scopus 로고    scopus 로고
    • Sequential fractionation and two-dimensional gel analysis unravels the complexity of the dimorphic fungus Candida albicans cell wall proteome
    • Pitarch A, Sanchez M, Nombela C, Gil C. Sequential fractionation and two-dimensional gel analysis unravels the complexity of the dimorphic fungus Candida albicans cell wall proteome. Mol Cell Proteomics 2002; 1: 967-982.
    • (2002) Mol Cell Proteomics , vol.1 , pp. 967-982
    • Pitarch, A.1    Sanchez, M.2    Nombela, C.3    Gil, C.4
  • 29
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970; 227: 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 30
    • 0018854046 scopus 로고
    • Electrophoretic analysis of plasminogen activators in polyacrylamide gels containing sodium dodecyl sulfate and copolymerized substrates
    • Heussen C, Dowdle EB. Electrophoretic analysis of plasminogen activators in polyacrylamide gels containing sodium dodecyl sulfate and copolymerized substrates. Anal Biochem 1980; 102: 196-202.
    • (1980) Anal Biochem , vol.102 , pp. 196-202
    • Heussen, C.1    Dowdle, E.B.2
  • 31
    • 84928586134 scopus 로고    scopus 로고
    • [updated 27 June 2008] Available from : http://www.broad.mit.edu/
    • Broad Institute - Paracoccidioides brasiliensis Database ( http://www. broad.mit.edu/annotation/genome/paracoccidioides-brasiliensis/ MultiHome.html ) [updated 27 June 2008] Available from : http:// www.broad.mit.edu/
    • Paracoccidioides Brasiliensis Database
  • 32
    • 0031023724 scopus 로고    scopus 로고
    • The glycosylation of the aspartic proteinases from barley ( Hordeum vulgare L.) and cardoon ( Cynara cardunculus L.)
    • Costa J, Ashford DA, Nimtz M, Bento I, et al. The glycosylation of the aspartic proteinases from barley ( Hordeum vulgare L.) and cardoon ( Cynara cardunculus L.). Eur J Biochem 1997; 243: 695-700.
    • (1997) Eur J Biochem , vol.243 , pp. 695-700
    • Costa, J.1    Ashford, D.A.2    Nimtz, M.3    Bento, I.4
  • 33
    • 0032530681 scopus 로고    scopus 로고
    • Secretion and pH-dependent self-processing of the pro-form of the Yarrowia lypolytica acid extracellular protease
    • McEwen RK, Young TW. Secretion and pH-dependent self-processing of the pro-form of the Yarrowia lypolytica acid extracellular protease. Yeast 1998; 15: 1115-1125.
    • (1998) Yeast , vol.15 , pp. 1115-1125
    • McEwen, R.K.1    Young, T.W.2
  • 34
    • 34250617570 scopus 로고    scopus 로고
    • A family of glycosylphosphatidylinositol- linked aspartyl proteases is required for virulence of Candida glabrata
    • Kaur R, Ma B, Cormack BP. A family of glycosylphosphatidylinositol- linked aspartyl proteases is required for virulence of Candida glabrata. Proc Natl Acad Sci USA 2007; 104: 7628-7633.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 7628-7633
    • Kaur, R.1    Ma, B.2    Cormack, B.P.3
  • 35
    • 33644861572 scopus 로고    scopus 로고
    • Glycosylphosphatidylinositolanchored proteases of Candida albicans target proteins necessary for both cellular processes and host-pathogen interactions
    • Albrecht A, Felk A, Pichova I, et al. Glycosylphosphatidylinositolanchored proteases of Candida albicans target proteins necessary for both cellular processes and host-pathogen interactions. J Biol Chem 2006; 281: 688-694.
    • (2006) J Biol Chem , vol.281 , pp. 688-694
    • Albrecht, A.1    Felk, A.2    Pichova, I.3
  • 36
    • 0018805958 scopus 로고
    • Evolution in the structure and function of carboxyl proteases
    • Tang J. Evolution in the structure and function of carboxyl proteases. Mol Cell Biochem 1979; 26: 93-109.
    • (1979) Mol Cell Biochem , vol.26 , pp. 93-109
    • Tang, J.1
  • 37
    • 0022753540 scopus 로고
    • PEP4 gene of Saccharomyces cerevisiae encodes proteinase A, a vacuolar enzyme required for processing of vacuolar precursors
    • Ammerer G, Hunter CP, Rothman JH, et al. PEP4 gene of Saccharomyces cerevisiae encodes proteinase A, a vacuolar enzyme required for processing of vacuolar precursors. Mol Cell Biol 1986; 6: 2490-2499.
    • (1986) Mol Cell Biol , vol.6 , pp. 2490-2499
    • Ammerer, G.1    Hunter, C.P.2    Rothman, J.H.3
  • 38
    • 0022755757 scopus 로고
    • The PEP4 gene encodes an aspartyl protease implicated in the posttranslational regulation of Saccharomyces cerevisiae vacuolar hydrolases
    • Woolford CA, Daniels LB, Park FJ, et al. The PEP4 gene encodes an aspartyl protease implicated in the posttranslational regulation of Saccharomyces cerevisiae vacuolar hydrolases. Mol Cell Biol 1986; 6: 2500-2510.
    • (1986) Mol Cell Biol , vol.6 , pp. 2500-2510
    • Woolford, C.A.1    Daniels, L.B.2    Park, F.J.3
  • 39
    • 33847154277 scopus 로고    scopus 로고
    • Aspartic protease activities of schistosomes cleave mammalian hemoglobin in a hostspecific manner
    • Koehler JW, Morales ME, Shelby BD, Brindley PJ. Aspartic protease activities of schistosomes cleave mammalian hemoglobin in a hostspecific manner. Mem Inst Oswaldo Cruz 2007; 102: 83-85.
    • (2007) Mem Inst Oswaldo Cruz , vol.102 , pp. 83-85
    • Koehler, J.W.1    Morales, M.E.2    Shelby, B.D.3    Brindley, P.J.4


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