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Volumn 33, Issue 2, 2009, Pages 143-148

Localisation of Bgl2p upon antifungal drug treatment in Candida albicans

Author keywords

Bgl2p; Candida albicans; Cell wall proteins; Glucanosyltransferase

Indexed keywords

ANTIFUNGAL AGENT; CELL MEMBRANE PROTEIN; MICAFUNGIN;

EID: 58149181472     PISSN: 09248579     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ijantimicag.2008.08.021     Document Type: Article
Times cited : (5)

References (35)
  • 1
    • 0023493828 scopus 로고
    • Cell envelope of Candida albicans
    • Shepherd M.G. Cell envelope of Candida albicans. Crit Rev Microbiol 15 (1987) 7-25
    • (1987) Crit Rev Microbiol , vol.15 , pp. 7-25
    • Shepherd, M.G.1
  • 2
    • 0000708358 scopus 로고
    • Cell walls
    • Rose A.H., and Harrison J.S. (Eds), Academic Press, London, UK
    • Fleet G.H. Cell walls. In: Rose A.H., and Harrison J.S. (Eds). The yeasts vol. 4 (1991), Academic Press, London, UK
    • (1991) The yeasts , vol.4
    • Fleet, G.H.1
  • 3
    • 20944436932 scopus 로고    scopus 로고
    • Characterization of two Candida albicans surface mannoprotein adhesins that bind immobilized saliva components
    • Jeng H.W., Holmes A.R., and Cannon D. Characterization of two Candida albicans surface mannoprotein adhesins that bind immobilized saliva components. Med Mycol 43 (2005) 209-217
    • (2005) Med Mycol , vol.43 , pp. 209-217
    • Jeng, H.W.1    Holmes, A.R.2    Cannon, D.3
  • 5
    • 0032962171 scopus 로고    scopus 로고
    • The contribution of cell wall proteins to the organization of the yeast cell wall
    • Kapteyn J.C., Van Den Ende H., and Klis F.M. The contribution of cell wall proteins to the organization of the yeast cell wall. Biochim Biophys Acta 1426 (1999) 373-383
    • (1999) Biochim Biophys Acta , vol.1426 , pp. 373-383
    • Kapteyn, J.C.1    Van Den Ende, H.2    Klis, F.M.3
  • 6
    • 0036090545 scopus 로고    scopus 로고
    • Identification of major glucan-associated cell wall proteins of Candida albicans and their role in fluconazole resistance
    • Angiolella L., Micocci M.M., D'Alessio S., Girolamo A., Maras B., and Cassone A. Identification of major glucan-associated cell wall proteins of Candida albicans and their role in fluconazole resistance. Antimicrob Agents Chemother 46 (2002) 1688-1694
    • (2002) Antimicrob Agents Chemother , vol.46 , pp. 1688-1694
    • Angiolella, L.1    Micocci, M.M.2    D'Alessio, S.3    Girolamo, A.4    Maras, B.5    Cassone, A.6
  • 7
    • 0024109658 scopus 로고
    • Yeast beta-glucanases: a complex system of secreted enzymes
    • Nombela C., Molina M., Cenamor R., and Sanchez M. Yeast beta-glucanases: a complex system of secreted enzymes. Microbiol Sci 5 (1988) 328-332
    • (1988) Microbiol Sci , vol.5 , pp. 328-332
    • Nombela, C.1    Molina, M.2    Cenamor, R.3    Sanchez, M.4
  • 8
    • 4143102523 scopus 로고    scopus 로고
    • Organization and construction of the yeast cell wall
    • Sturgeon R. (Ed), Elsevier Science, Amsterdam, The Netherlands
    • De Nobel H., and Kliss F.M. Organization and construction of the yeast cell wall. In: Sturgeon R. (Ed). Advances in macromolecular carbohydrate research vol. 2 (2003), Elsevier Science, Amsterdam, The Netherlands
    • (2003) Advances in macromolecular carbohydrate research , vol.2
    • De Nobel, H.1    Kliss, F.M.2
  • 9
    • 0033178562 scopus 로고    scopus 로고
    • Hydrolase and transferase activities of the beta-1,3-exoglucanase of Candida albicans
    • Stubbs H.J., Brusch D.J., Emerson J.B., and Sullivan P.A. Hydrolase and transferase activities of the beta-1,3-exoglucanase of Candida albicans. Eur J Biochem 263 (1999) 889-895
    • (1999) Eur J Biochem , vol.263 , pp. 889-895
    • Stubbs, H.J.1    Brusch, D.J.2    Emerson, J.B.3    Sullivan, P.A.4
  • 10
    • 0030043268 scopus 로고    scopus 로고
    • Identification of glucan-associated enolase as a main cell wall protein of Candida albicans and an indirect target of lipopeptide antimycotics
    • Angiolella L., Facchin M., Stringaro A., Maras B., Simonetti N., and Cassone A. Identification of glucan-associated enolase as a main cell wall protein of Candida albicans and an indirect target of lipopeptide antimycotics. J Infect Dis 173 (1996) 684-690
    • (1996) J Infect Dis , vol.173 , pp. 684-690
    • Angiolella, L.1    Facchin, M.2    Stringaro, A.3    Maras, B.4    Simonetti, N.5    Cassone, A.6
  • 11
    • 0031052529 scopus 로고    scopus 로고
    • Phenotype in Candida albicans of a disruption of the BGL2 gene encoding a 1,3-beta-glucosyltransferase
    • Sarthy A., McGonial T., Coen M., Frost D.J., Meulbroek J.A., and Goldman R.C. Phenotype in Candida albicans of a disruption of the BGL2 gene encoding a 1,3-beta-glucosyltransferase. Microbiology 143 (1997) 367-376
    • (1997) Microbiology , vol.143 , pp. 367-376
    • Sarthy, A.1    McGonial, T.2    Coen, M.3    Frost, D.J.4    Meulbroek, J.A.5    Goldman, R.C.6
  • 12
    • 0025876127 scopus 로고
    • A secreted beta-glucan-branching enzyme from Candida albicans
    • Hartland R.P., Emerson G.W., and Sullivan P.A. A secreted beta-glucan-branching enzyme from Candida albicans. Proc Biol Sci 246 (1991) 155-160
    • (1991) Proc Biol Sci , vol.246 , pp. 155-160
    • Hartland, R.P.1    Emerson, G.W.2    Sullivan, P.A.3
  • 13
    • 0028985247 scopus 로고
    • Kinetics of beta-1,3 glucan interaction at the donor and acceptor sites of the fungal glucosyltransferase encoded by the BGL2 gene
    • Goldman R.C., Sullivan P.A., Zakula D., and Capobianco J.O. Kinetics of beta-1,3 glucan interaction at the donor and acceptor sites of the fungal glucosyltransferase encoded by the BGL2 gene. Eur J Biochem 227 (1995) 372-378
    • (1995) Eur J Biochem , vol.227 , pp. 372-378
    • Goldman, R.C.1    Sullivan, P.A.2    Zakula, D.3    Capobianco, J.O.4
  • 14
  • 18
    • 0015620349 scopus 로고
    • A technique for ultracryotomy of cell suspensions and tissues
    • Tokuyasu K.T. A technique for ultracryotomy of cell suspensions and tissues. J Cell Biol 57 (1973) 551-565
    • (1973) J Cell Biol , vol.57 , pp. 551-565
    • Tokuyasu, K.T.1
  • 19
    • 0031789968 scopus 로고    scopus 로고
    • A 1,3-beta-glucanosyltransferase isolated from the cell wall of Aspergillus fumigatus is a homologue of the yeast Bgl2p
    • Mouyna I., Hartland R.P., Fontaine T., Diaquin M., Simenel C., Delepierre M., et al. A 1,3-beta-glucanosyltransferase isolated from the cell wall of Aspergillus fumigatus is a homologue of the yeast Bgl2p. Microbiology 144 (1998) 3171-3180
    • (1998) Microbiology , vol.144 , pp. 3171-3180
    • Mouyna, I.1    Hartland, R.P.2    Fontaine, T.3    Diaquin, M.4    Simenel, C.5    Delepierre, M.6
  • 20
    • 0027409809 scopus 로고
    • Purification and characterization of the Saccharomyces cerevisiae BGL2 gene product, a cell wall endo-beta-1,3-glucanase
    • Mrsa V., Klebl F., and Tanner W. Purification and characterization of the Saccharomyces cerevisiae BGL2 gene product, a cell wall endo-beta-1,3-glucanase. J Bacteriol 175 (1993) 2102-2106
    • (1993) J Bacteriol , vol.175 , pp. 2102-2106
    • Mrsa, V.1    Klebl, F.2    Tanner, W.3
  • 21
    • 0031689604 scopus 로고    scopus 로고
    • New potential cell wall glucanases of Saccharomyces cerevisiae and their involvement in mating
    • Cappellaro C., Mrsa V., and Tanner W. New potential cell wall glucanases of Saccharomyces cerevisiae and their involvement in mating. J Bacteriol 180 (1998) 5030-5037
    • (1998) J Bacteriol , vol.180 , pp. 5030-5037
    • Cappellaro, C.1    Mrsa, V.2    Tanner, W.3
  • 22
    • 0033950964 scopus 로고    scopus 로고
    • The cell wall architecture of Candida albicans wild-type cells and cell wall-defective mutants
    • Kapteyn J.C., Hoyer L.L., Hecht J.E., Muller W.H., Andel A., Verkleij A.J., et al. The cell wall architecture of Candida albicans wild-type cells and cell wall-defective mutants. Mol Microbiol 35 (2000) 601-611
    • (2000) Mol Microbiol , vol.35 , pp. 601-611
    • Kapteyn, J.C.1    Hoyer, L.L.2    Hecht, J.E.3    Muller, W.H.4    Andel, A.5    Verkleij, A.J.6
  • 23
    • 0041877649 scopus 로고    scopus 로고
    • A study of the yeast cell wall composition and structure in response to growth conditions and mode of cultivation
    • Aguilar-Uscanga B., and Francois J.M. A study of the yeast cell wall composition and structure in response to growth conditions and mode of cultivation. Lett Appl Microbiol 37 (2003) 268-274
    • (2003) Lett Appl Microbiol , vol.37 , pp. 268-274
    • Aguilar-Uscanga, B.1    Francois, J.M.2
  • 24
    • 4143087024 scopus 로고    scopus 로고
    • Proteomic analysis of Candida albicans cell walls reveals covalently bound carbohydrate-active enzymes and adhesins
    • De Groot W.J., de Boet A.D., Cunningham J., Dekker H.L., de Jong L., Hellingwerf K.J., et al. Proteomic analysis of Candida albicans cell walls reveals covalently bound carbohydrate-active enzymes and adhesins. Eukaryot Cell 3 (2004) 955-965
    • (2004) Eukaryot Cell , vol.3 , pp. 955-965
    • De Groot, W.J.1    de Boet, A.D.2    Cunningham, J.3    Dekker, H.L.4    de Jong, L.5    Hellingwerf, K.J.6
  • 25
    • 33645671077 scopus 로고    scopus 로고
    • Proteomic analysis of Candida albicans yeast and hyphal cell wall and associated proteins
    • Ebanks R.O., Chisholm K., McKinnon S., Whiteway M., and Pinto D.M. Proteomic analysis of Candida albicans yeast and hyphal cell wall and associated proteins. Proteomics 6 (2006) 2147-2156
    • (2006) Proteomics , vol.6 , pp. 2147-2156
    • Ebanks, R.O.1    Chisholm, K.2    McKinnon, S.3    Whiteway, M.4    Pinto, D.M.5
  • 26
    • 33845204237 scopus 로고    scopus 로고
    • A proteomic based approach for the identification of Candida albicans protein components present in a subunit vaccine that protects against disseminated candidiasis
    • Thomas D.P., Viudes A., Monteagudo C., Lazzell A.L., Saville S.P., and Lopez-Ribot J.L. A proteomic based approach for the identification of Candida albicans protein components present in a subunit vaccine that protects against disseminated candidiasis. Proteomics 6 (2006) 6033-6041
    • (2006) Proteomics , vol.6 , pp. 6033-6041
    • Thomas, D.P.1    Viudes, A.2    Monteagudo, C.3    Lazzell, A.L.4    Saville, S.P.5    Lopez-Ribot, J.L.6
  • 27
    • 0035663218 scopus 로고    scopus 로고
    • The yeast cell-wall salvage pathway
    • Popolo L., Gualtieri T., and Ragni E. The yeast cell-wall salvage pathway. Med Mycol 39 (2001) 111-121
    • (2001) Med Mycol , vol.39 , pp. 111-121
    • Popolo, L.1    Gualtieri, T.2    Ragni, E.3
  • 28
    • 0038504070 scopus 로고    scopus 로고
    • Genome-wide analysis of the response to cell wall mutations in the yeast Saccharomyces cerevisiae
    • Lagorce A., Hauser N.C., Labourdette D., Rodriguez C., Martin-Yken H., Arroyo J., et al. Genome-wide analysis of the response to cell wall mutations in the yeast Saccharomyces cerevisiae. J Biol Chem 278 (2003) 20345-20357
    • (2003) J Biol Chem , vol.278 , pp. 20345-20357
    • Lagorce, A.1    Hauser, N.C.2    Labourdette, D.3    Rodriguez, C.4    Martin-Yken, H.5    Arroyo, J.6
  • 29
    • 2442477661 scopus 로고    scopus 로고
    • The global transcriptional response to transient cell wall damage in Saccharomyces cerevisiae and its regulation by the cell integrity signaling pathway
    • Garcia R., Bermejo C., Grau C., Perez R., Rodriguez-Pena J.M., Francois J., et al. The global transcriptional response to transient cell wall damage in Saccharomyces cerevisiae and its regulation by the cell integrity signaling pathway. J Biol Chem 279 (2004) 15183-15195
    • (2004) J Biol Chem , vol.279 , pp. 15183-15195
    • Garcia, R.1    Bermejo, C.2    Grau, C.3    Perez, R.4    Rodriguez-Pena, J.M.5    Francois, J.6
  • 30
    • 2942536765 scopus 로고    scopus 로고
    • Sed1p and Srl1p are required to compensate for cell wall instability in Saccharomyces cerevisiae mutants defective in multiple GPI-anchored mannoproteins
    • Hagen I., Ecker M., Lagorce A., Francois J.M., Sestak S., Rachel R., et al. Sed1p and Srl1p are required to compensate for cell wall instability in Saccharomyces cerevisiae mutants defective in multiple GPI-anchored mannoproteins. Mol Microbiol 52 (2004) 1413-1425
    • (2004) Mol Microbiol , vol.52 , pp. 1413-1425
    • Hagen, I.1    Ecker, M.2    Lagorce, A.3    Francois, J.M.4    Sestak, S.5    Rachel, R.6
  • 31
    • 0037161196 scopus 로고    scopus 로고
    • Correct GPI-anchor synthesis is required for the incorporation of endoglucanase/glucanosyltransferase Bgl2p into the Saccharomyces cerevisiae cell wall
    • Kalebina T.S., Laurinavichiute D.K., Packeiser A.N., Morenkov O.S., Ter-Avanesyan M.D., and Kulaev I. Correct GPI-anchor synthesis is required for the incorporation of endoglucanase/glucanosyltransferase Bgl2p into the Saccharomyces cerevisiae cell wall. FEMS Microbiol Lett 210 (2002) 81-85
    • (2002) FEMS Microbiol Lett , vol.210 , pp. 81-85
    • Kalebina, T.S.1    Laurinavichiute, D.K.2    Packeiser, A.N.3    Morenkov, O.S.4    Ter-Avanesyan, M.D.5    Kulaev, I.6
  • 32
    • 0031774198 scopus 로고    scopus 로고
    • Serodiagnosis of histoplasmosis, paracoccidioidomycosis and penicilliosis marneffei; current status and future trends
    • Hamilton A.J. Serodiagnosis of histoplasmosis, paracoccidioidomycosis and penicilliosis marneffei; current status and future trends. Med Mycol 36 (1998) 351-384
    • (1998) Med Mycol , vol.36 , pp. 351-384
    • Hamilton, A.J.1
  • 33
    • 31644437049 scopus 로고    scopus 로고
    • Decoding serological response to Candida cell wall immunome into novel diagnostic, prognostic, and therapeutic candidates for systemic candidiasis by proteomic and bioinformatic analyses
    • Pitarch A., Jimenez A., Nombela C., and Gil C. Decoding serological response to Candida cell wall immunome into novel diagnostic, prognostic, and therapeutic candidates for systemic candidiasis by proteomic and bioinformatic analyses. Mol Cell Proteomics 5 (2006) 79-96
    • (2006) Mol Cell Proteomics , vol.5 , pp. 79-96
    • Pitarch, A.1    Jimenez, A.2    Nombela, C.3    Gil, C.4
  • 34
    • 33845641402 scopus 로고    scopus 로고
    • Human domain antibodies against virulence traits of Candida albicans inhibit fungus adherence to vaginal epithelium and protect against experimental vaginal candidiasis
    • De Bernardis F., Liu H., O'Mahony R., La Valle R., Bartollino S., Sandini S., et al. Human domain antibodies against virulence traits of Candida albicans inhibit fungus adherence to vaginal epithelium and protect against experimental vaginal candidiasis. J Infect Dis 195 (2007) 149-157
    • (2007) J Infect Dis , vol.195 , pp. 149-157
    • De Bernardis, F.1    Liu, H.2    O'Mahony, R.3    La Valle, R.4    Bartollino, S.5    Sandini, S.6
  • 35
    • 33646371696 scopus 로고    scopus 로고
    • The anti-Candida vaccine based on the recombinant N-terminal domain of Als1p is broadly active against disseminated candidiasis
    • Ibrahim A.S., Spelberg B.J., Avanesian V., Fu Y., and Edwards J.E. The anti-Candida vaccine based on the recombinant N-terminal domain of Als1p is broadly active against disseminated candidiasis. Infect Immun 74 (2006) 3039-3041
    • (2006) Infect Immun , vol.74 , pp. 3039-3041
    • Ibrahim, A.S.1    Spelberg, B.J.2    Avanesian, V.3    Fu, Y.4    Edwards, J.E.5


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