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Volumn 94, Issue , 2014, Pages 79-84

Production of a defensin-like antifungal protein NFAP from Neosartorya fischeri in Pichia pastoris and its antifungal activity against filamentous fungal isolates from human infections

Author keywords

Antimicrobial susceptibility; Ascomycetes; Clinical fungal isolates; Neosartorya fischeri antifungal protein; Pichia pastoris; Zygomycetes

Indexed keywords

ASCOMYCOTA; ASPERGILLUS; FUNGI; FUSARIUM; NEOSARTORYA FISCHERI; NEOSARTORYA FISCHERI NRRL 181; PICHIA PASTORIS; ZYGOMYCETES;

EID: 84890417273     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.pep.2013.11.003     Document Type: Article
Times cited : (30)

References (30)
  • 1
    • 4043071183 scopus 로고    scopus 로고
    • Small, basic antifungal proteins secreted from filamentous ascomycetes: A comparative study regarding, expression, structure, function and potential application
    • F. Marx Small, basic antifungal proteins secreted from filamentous ascomycetes: a comparative study regarding expression, structure, function and potential application Appl. Microbiol. Biotechnol. 65 2004 133 142 (Pubitemid 39066257)
    • (2004) Applied Microbiology and Biotechnology , vol.65 , Issue.2 , pp. 133-142
    • Marx, F.1
  • 2
    • 38349097003 scopus 로고    scopus 로고
    • A small protein that fights fungi: AFP as a new promising antifungal agent of biotechnological value
    • V. Meyer A small protein that fights fungi: AFP as a new promising antifungal agent of biotechnological value Appl. Microbiol. Biotechnol. 78 2008 17 28
    • (2008) Appl. Microbiol. Biotechnol. , vol.78 , pp. 17-28
    • Meyer, V.1
  • 4
    • 38949210655 scopus 로고    scopus 로고
    • The Penicillium chrysogenum antifungal protein PAF, a promising tool for the development of new antifungal therapies and fungal cell biology studies
    • DOI 10.1007/s00018-007-7364-8
    • F. Marx, U. Binder, É. Leiter, and I. Pócsi The Penicillium chrysogenum antifungal protein PAF, a promising tool for the development of new antifungal therapies and fungal cell biology studies Cell. Mol. Life Sci. 65 2008 445 454 (Pubitemid 351214653)
    • (2008) Cellular and Molecular Life Sciences , vol.65 , Issue.3 , pp. 445-454
    • Marx, F.1    Binder, U.2    Leiter, E.3    Pocsi, I.4
  • 6
    • 0242308193 scopus 로고    scopus 로고
    • Activity of the Antifungal Protein from Aspergillus giganteus Against Botrytis cinerea
    • A.B. Moreno, Á.M. del Pozo, M. Borja, and B.S. Segudo Activity of the antifungal protein from Aspergillus giganteus against Botrytis cinerea Phytopathology 93 2003 1344 1353 (Pubitemid 37332216)
    • (2003) Phytopathology , vol.93 , Issue.11 , pp. 1344-1353
    • Moreno, A.B.1    Martinez Del Pozo, A.2    Borja, M.3    San Segundo, B.4
  • 7
    • 34247140262 scopus 로고    scopus 로고
    • Interactions between statins and Penicillium chrysogenum antifungal protein (PAF) to inhibit the germination of sporangiospores of different sensitive Zygomycetes
    • DOI 10.1111/j.1574-6968.2007.00661.x
    • L. Galgóczy, T. Papp, G. Lukács, É. Leiter, I. Pócsi, and C. Vágvölgyi Interactions between statins and Penicillium chrysogenum antifungal protein (PAF) to inhibit the germination of sporangiospores of different sensitive Zygomycetes FEMS Microbiol. Lett. 270 2007 109 115 (Pubitemid 46597345)
    • (2007) FEMS Microbiology Letters , vol.270 , Issue.1 , pp. 109-115
    • Galgoczy, L.1    Papp, T.2    Lukacs, G.3    Leiter, E.4    Pocsi, I.5    Vagvolgyi, C.6
  • 8
    • 50949124517 scopus 로고    scopus 로고
    • In vitro activity of Penicillium chrysogenum antifungal protein (PAF) and its combination with fluconazole against different dermatophytes
    • L. Galgóczy, T. Papp, I. Pócsi, N. Hegedus, and C. Vágvölgyi In vitro activity of Penicillium chrysogenum antifungal protein (PAF) and its combination with fluconazole against different dermatophytes Anton. Leeuw. Int. J. G. 94 2008 463 470
    • (2008) Anton. Leeuw. Int. J. G. , vol.94 , pp. 463-470
    • Galgóczy, L.1    Papp, T.2    Pócsi, I.3    Hegedus, N.4    Vágvölgyi, C.5
  • 9
    • 80051547994 scopus 로고    scopus 로고
    • Isolation and characterization of Neosartorya fischeri antifungal protein
    • NFAP
    • L. Kovács, M. Virágh, M. Takó, T. Papp, C. Vágvölgyi, and L. Galgóczy Isolation and characterization of Neosartorya fischeri antifungal protein NFAP Peptides 32 2011 1724 1731
    • (2011) Peptides , vol.32 , pp. 1724-1731
    • Kovács, L.1    Virágh, M.2    Takó, M.3    Papp, T.4    Vágvölgyi, C.5    Galgóczy, L.6
  • 10
    • 84873671620 scopus 로고    scopus 로고
    • Investigation of the antimicrobial effect of Neosartorya fischeri antifungal protein (NFAP) after heterologous expression in Aspergillus nidulans
    • L. Galgóczy, L. Kovács, Z. Karácsony, M. Virágh, Z. Hamari, and C. Vágvölgyi Investigation of the antimicrobial effect of Neosartorya fischeri antifungal protein (NFAP) after heterologous expression in Aspergillus nidulans Microbiology - SGM 159 2013 411 419
    • (2013) Microbiology - SGM , vol.159 , pp. 411-419
    • Galgóczy, L.1    Kovács, L.2    Karácsony, Z.3    Virágh, M.4    Hamari, Z.5    Vágvölgyi, C.6
  • 12
    • 0028983813 scopus 로고
    • Improvement of an "in-Gel" digestion procedure for the micropreparation of internal protein fragments for amino acid sequencing
    • U. Hellman, C. Wernstedt, J. Góñez, and C.H. Heldin Improvement of an "In-Gel" digestion procedure for the micropreparation of internal protein fragments for amino acid sequencing Anal. Biochem. 224 1995 451 455
    • (1995) Anal. Biochem. , vol.224 , pp. 451-455
    • Hellman, U.1    Wernstedt, C.2    Góñez, J.3    Heldin, C.H.4
  • 14
    • 84890352226 scopus 로고    scopus 로고
    • Reference method for broth dilution antifungal susceptibility testing of filamentous fungi
    • Clinical and Laboratory Standards Institute Wayne
    • Clinical and Laboratory Standards Institute, Reference method for broth dilution antifungal susceptibility testing of filamentous fungi, in: Approved Standard CLSI Document M38-A2, Clinical and Laboratory Standards Institute, Wayne, 2008.
    • (2008) Approved Standard CLSI Document M38-A2, Clinical and Laboratory Standards Institute
  • 15
    • 1542373564 scopus 로고    scopus 로고
    • Antifungal proteins: Targets, mechanisms and prospective applications
    • DOI 10.1007/s00018-003-3231-4
    • T. Theis, and U. Sthal Antifungal proteins: targets, mechanisms and prospective applications Cell. Mol. Life Sci. 61 2004 437 455 (Pubitemid 38316580)
    • (2004) Cellular and Molecular Life Sciences , vol.61 , Issue.4 , pp. 437-455
    • Theis, T.1    Stahl, U.2
  • 16
    • 34247137266 scopus 로고    scopus 로고
    • Antimicrobial peptides and plant disease control
    • DOI 10.1111/j.1574-6968.2007.00683.x
    • E. Montesinos Antimicrobial peptides and plant disease control FEMS Microbiol. Lett. 270 2007 1 11 (Pubitemid 46597355)
    • (2007) FEMS Microbiology Letters , vol.270 , Issue.1 , pp. 1-11
    • Montesinos, E.1
  • 20
    • 84884290168 scopus 로고    scopus 로고
    • Synthesis of PAF, an antifungal protein from P. Chrysogenum by native chemical ligation: Disulfide pattern and fold recovered in oxidative refolding
    • G. Váradi, K.G. Tóth, Z. Kele, L. Galgóczy, Á. Fizil, and G. Batta Synthesis of PAF, an antifungal protein from P. chrysogenum by native chemical ligation: disulfide pattern and fold recovered in oxidative refolding Chem. Eur. J. 19 2013 12684 12692
    • (2013) Chem. Eur. J. , vol.19 , pp. 12684-12692
    • Váradi, G.1    Tóth, K.G.2    Kele, Z.3    Galgóczy, L.4    Fizil, Á.5    Batta, G.6
  • 21
    • 17844386088 scopus 로고    scopus 로고
    • Sensitivity of different Zygomycetes to the Penicillium chrysogenum antifungal protein (PAF)
    • DOI 10.1002/jobm.200410512
    • L. Galgóczy, T. Papp, É. Leiter, F. Marx, I. Pócsi, and C. Vágvölgyi Sensitivity of different Zygomycetes to the Penicillium chrysogenum antifungal protein (PAF) J. Basic Microbiol. 45 2005 136 141 (Pubitemid 40589308)
    • (2005) Journal of Basic Microbiology , vol.45 , Issue.2 , pp. 136-141
    • Galgoczy, L.1    Papp, T.2    Leiter, E.3    Marx, F.4    Pocsi, I.5    Vagvolgyi, C.6
  • 23
    • 0034610432 scopus 로고    scopus 로고
    • P. Nalgiovense carries a gene which is homologous to the paf gene of P. Chrysogenum which codes for an antifungal peptide
    • R. Geisen P. nalgiovense carries a gene which is homologous to the paf gene of P. chrysogenum which codes for an antifungal peptide Int. J. Food Microbiol. 62 2000 95 101
    • (2000) Int. J. Food Microbiol. , vol.62 , pp. 95-101
    • Geisen, R.1
  • 25
    • 0037310294 scopus 로고    scopus 로고
    • The antifungal protein from Aspergillus giganteus causes membrane permeabilization
    • DOI 10.1128/AAC.47.2.588-593.2003
    • T. Theis, M. Wedde, V. Meyer, and U. Stahl The antifungal protein from Aspergillus giganteus causes membrane permeabilization Antimicrob. Agents Chemother. 47 2003 588 593 (Pubitemid 36158087)
    • (2003) Antimicrobial Agents and Chemotherapy , vol.47 , Issue.2 , pp. 588-593
    • Theis, T.1    Wedde, M.2    Meyer, V.3    Stahl, U.4
  • 26
    • 54049121110 scopus 로고    scopus 로고
    • First isolation of a novel thermostable antifungal peptide secreted by Aspergillus clavatus
    • H. Skouri-Gargour, and A. Gargouri First isolation of a novel thermostable antifungal peptide secreted by Aspergillus clavatus Peptides 29 2008 1871 1877
    • (2008) Peptides , vol.29 , pp. 1871-1877
    • Skouri-Gargour, H.1    Gargouri, A.2
  • 27
    • 77956480024 scopus 로고    scopus 로고
    • A highly thermostable antimicrobial peptide from Aspergillus clavatus ES1: Biochemical and molecular characterization
    • M. Hajji, K. Jellouli, N. Hmidet, R. Balti, A. Sellami-Kamoun, and M. Nasri A highly thermostable antimicrobial peptide from Aspergillus clavatus ES1: biochemical and molecular characterization J. Ind. Microbiol. Biotechnol. 37 2010 805 813
    • (2010) J. Ind. Microbiol. Biotechnol. , vol.37 , pp. 805-813
    • Hajji, M.1    Jellouli, K.2    Hmidet, N.3    Balti, R.4    Sellami-Kamoun, A.5    Nasri, M.6
  • 29
    • 84871405851 scopus 로고    scopus 로고
    • Antifungal peptides homologous to the Penicillium chrysogenum antifungal protein (PAF) are widespread among Fusaria
    • L. Galgóczy, M. Virágh, L. Kovács, B. Tóth, T. Papp, and C. Vágvölgyi Antifungal peptides homologous to the Penicillium chrysogenum antifungal protein (PAF) are widespread among Fusaria Peptides 39 2013 131 137
    • (2013) Peptides , vol.39 , pp. 131-137
    • Galgóczy, L.1    Virágh, M.2    Kovács, L.3    Tóth, B.4    Papp, T.5    Vágvölgyi, C.6
  • 30
    • 84890379152 scopus 로고    scopus 로고
    • Antifungal resistance: Aspergillus
    • D.L. Mayers, Humana Press-Springer New York (Chapter 65)
    • P.H. Chandrasekar, and E.K. Manavathu Antifungal resistance: Aspergillus D.L. Mayers, Antimicrobial Drug Resistance 2009 Humana Press-Springer New York 953 965 (Chapter 65)
    • (2009) Antimicrobial Drug Resistance , pp. 953-965
    • Chandrasekar, P.H.1    Manavathu, E.K.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.