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Volumn 5, Issue 1, 2015, Pages

Production of a modified peptide clavanin in Pichia pastoris: cloning, expression, purification and in vitro activities

Author keywords

Antimicrobial peptide; Clavanin; Heterologous expression; Pichia pastoris

Indexed keywords

CHLORAMPHENICOL; CLAVANIN MODIFIED PEPTIDE; PLASMID VECTOR; POLYPEPTIDE ANTIBIOTIC AGENT; UNCLASSIFIED DRUG;

EID: 84938589968     PISSN: None     EISSN: 21910855     Source Type: Journal    
DOI: 10.1186/s13568-015-0129-0     Document Type: Article
Times cited : (21)

References (38)
  • 1
    • 79952698383 scopus 로고    scopus 로고
    • Industrial-scale manufacturing of pharmaceutical-grade bioactive peptides
    • COI: 1:CAS:528:DC%2BC3MXjs1Wgtrg%3D, PID: 21238564
    • Agyei D, Danquah MK (2011) Industrial-scale manufacturing of pharmaceutical-grade bioactive peptides. Biotechnol Adv 29(3):272–277
    • (2011) Biotechnol Adv , vol.29 , Issue.3 , pp. 272-277
    • Agyei, D.1    Danquah, M.K.2
  • 2
    • 84903814380 scopus 로고    scopus 로고
    • Protein expression in Pichia pastoris: recent achievements and perspectives for heterologous protein production
    • COI: 1:CAS:528:DC%2BC2cXmsVCgtLk%3D, PID: 24743983
    • Ahmad M, Hirz M, Pichler H, Schwab H (2014) Protein expression in Pichia pastoris: recent achievements and perspectives for heterologous protein production. Appl Microbiol Biotechnol 98(2):5301–5317
    • (2014) Appl Microbiol Biotechnol , vol.98 , Issue.2 , pp. 5301-5317
    • Ahmad, M.1    Hirz, M.2    Pichler, H.3    Schwab, H.4
  • 3
    • 0033775891 scopus 로고    scopus 로고
    • Physiological functions of thioredoxin and thioredoxin reductase
    • PID: 11012661
    • Arnér ES, Holgren A (2000) Physiological functions of thioredoxin and thioredoxin reductase. Eur J Biochem 267(20):6102–6109
    • (2000) Eur J Biochem , vol.267 , Issue.20 , pp. 6102-6109
    • Arnér, E.S.1    Holgren, A.2
  • 4
    • 77952279826 scopus 로고    scopus 로고
    • Use of the yeast Pichia pastoris as an expression host for secretion of enterocin L50, a leaderless two-peptide (L50A and L50B) bacteriocin from Enterococcus faecium L50
    • COI: 1:CAS:528:DC%2BC3cXmsF2lurk%3D, PID: 20348300
    • Basanta A, Gómez-Sala B, Sánchez J, Diep DB, Herranz C, Hernández PE et al (2010) Use of the yeast Pichia pastoris as an expression host for secretion of enterocin L50, a leaderless two-peptide (L50A and L50B) bacteriocin from Enterococcus faecium L50. Appl Environ Microbiol 76(10):3314–33124
    • (2010) Appl Environ Microbiol , vol.76 , Issue.10 , pp. 3314-33124
    • Basanta, A.1    Gómez-Sala, B.2    Sánchez, J.3    Diep, D.B.4    Herranz, C.5    Hernández, P.E.6
  • 5
    • 84988074679 scopus 로고
    • Improved silver staining of plant-proteins, RNA and DNA in polyacrylamide gels
    • COI: 1:CAS:528:DyaL2sXhsFagtLc%3D
    • Blum H, Beier H, Gross HJ (1987) Improved silver staining of plant-proteins, RNA and DNA in polyacrylamide gels. Electrophoresis 8(2):93–99
    • (1987) Electrophoresis , vol.8 , Issue.2 , pp. 93-99
    • Blum, H.1    Beier, H.2    Gross, H.J.3
  • 6
    • 57649089450 scopus 로고    scopus 로고
    • Screening of fusion partners for high yield expression and purification of bioactive viscotoxins
    • COI: 1:CAS:528:DC%2BD1cXhsFansrrN, PID: 18983922
    • Bogomolovas J, Simon B, Sattler M, Stier G (2009) Screening of fusion partners for high yield expression and purification of bioactive viscotoxins. Protein Expr Purif 64(1):16–23
    • (2009) Protein Expr Purif , vol.64 , Issue.1 , pp. 16-23
    • Bogomolovas, J.1    Simon, B.2    Sattler, M.3    Stier, G.4
  • 7
    • 0141650651 scopus 로고    scopus 로고
    • Production of the active antifungal Pisum sativum defensin 1 (Psd1) in Pichia pastoris: overcoming the inefficiency of the STE13 protease
    • COI: 1:CAS:528:DC%2BD3sXntVGkt7w%3D, PID: 12963348
    • Cabral KM, Almeida MS, Valente AP, Almeida FC, Kurtenbach E (2003) Production of the active antifungal Pisum sativum defensin 1 (Psd1) in Pichia pastoris: overcoming the inefficiency of the STE13 protease. Protein Expr Purif 31(1):115–122
    • (2003) Protein Expr Purif , vol.31 , Issue.1 , pp. 115-122
    • Cabral, K.M.1    Almeida, M.S.2    Valente, A.P.3    Almeida, F.C.4    Kurtenbach, E.5
  • 9
    • 0021983928 scopus 로고
    • Isolation of alcohol oxidase and two other methanol regulatable genes from the yeast Pichia pastoris
    • COI: 1:CAS:528:DyaL2MXktVWmsbs%3D, PID: 3889590
    • Ellis SB, Brust PF, Koutz PJ, Waters AF, Harpold MM, Gingeras TR (1985) Isolation of alcohol oxidase and two other methanol regulatable genes from the yeast Pichia pastoris. Mol Cell Biol 5(5):1111–1121
    • (1985) Mol Cell Biol , vol.5 , Issue.5 , pp. 1111-1121
    • Ellis, S.B.1    Brust, P.F.2    Koutz, P.J.3    Waters, A.F.4    Harpold, M.M.5    Gingeras, T.R.6
  • 10
    • 33746744319 scopus 로고    scopus 로고
    • Enhancement of soluble protein expression through the use of fusion tags
    • COI: 1:CAS:528:DC%2BD28XotFWlur4%3D, PID: 16781139
    • Esposito D, Chatterjee DK (2006) Enhancement of soluble protein expression through the use of fusion tags. Curr Opin Biotechnol 17(4):353–358
    • (2006) Curr Opin Biotechnol , vol.17 , Issue.4 , pp. 353-358
    • Esposito, D.1    Chatterjee, D.K.2
  • 11
    • 84867265844 scopus 로고    scopus 로고
    • Secretion and activity of antimicrobial peptide cecropin D expressed in Pichia pastoris
    • COI: 1:CAS:528:DC%2BC38XhvVKgtLvP, PID: 23226775
    • Guo C, Huang Y, Zheng H, Tang L, He J, Xiang L et al (2012) Secretion and activity of antimicrobial peptide cecropin D expressed in Pichia pastoris. Exp Ther Med 4(6):1063–1068
    • (2012) Exp Ther Med , vol.4 , Issue.6 , pp. 1063-1068
    • Guo, C.1    Huang, Y.2    Zheng, H.3    Tang, L.4    He, J.5    Xiang, L.6
  • 12
    • 33845637789 scopus 로고    scopus 로고
    • Recombinant expression of human cathelicidin (hCAP18/LL-37) in Pichia pastoris
    • COI: 1:CAS:528:DC%2BD28Xht12gs7fL, PID: 17028774
    • Hong IP, Lee SJ, Kim YS, Choi SG (2007) Recombinant expression of human cathelicidin (hCAP18/LL-37) in Pichia pastoris. Biotechnol Lett 29(1):73–78
    • (2007) Biotechnol Lett , vol.29 , Issue.1 , pp. 73-78
    • Hong, I.P.1    Lee, S.J.2    Kim, Y.S.3    Choi, S.G.4
  • 13
    • 84900811958 scopus 로고    scopus 로고
    • Use of synthetic genes for cloning, production and functional expression of the bacteriocins enterocin A and bacteriocin E 50-52 by Pichia pastoris and Kluyveromyces lactis
    • COI: 1:CAS:528:DC%2BC2cXitFOqs7o%3D, PID: 24510220
    • Jimenez JJ, Borrero J, Gutiez L, Arbulu S, Herranz C, Cintas LM et al (2014) Use of synthetic genes for cloning, production and functional expression of the bacteriocins enterocin A and bacteriocin E 50-52 by Pichia pastoris and Kluyveromyces lactis. Mol Biotechnol 56:571–583
    • (2014) Mol Biotechnol , vol.56 , pp. 571-583
    • Jimenez, J.J.1    Borrero, J.2    Gutiez, L.3    Arbulu, S.4    Herranz, C.5    Cintas, L.M.6
  • 14
    • 67849084834 scopus 로고    scopus 로고
    • PDC1, a corn defensin peptide expressed in Escherichia coli and Pichia pastoris inhibits growth of Fusarium graminearum
    • COI: 1:CAS:528:DC%2BD1MXpt1Kiurg%3D, PID: 19505517
    • Kant P, Liu WZ, Pauls KP (2009) PDC1, a corn defensin peptide expressed in Escherichia coli and Pichia pastoris inhibits growth of Fusarium graminearum. Peptides 30(9):1593–1599
    • (2009) Peptides , vol.30 , Issue.9 , pp. 1593-1599
    • Kant, P.1    Liu, W.Z.2    Pauls, K.P.3
  • 15
    • 68349084675 scopus 로고    scopus 로고
    • Antibacterial activity of recombinant hCAP18/LL37 protein secreted from Pichia pastoris
    • COI: 1:CAS:528:DC%2BD1MXnslemsrg%3D, PID: 19557354
    • Kim SJ, Quan R, Lee SJ, Lee HK, Choi JK (2009) Antibacterial activity of recombinant hCAP18/LL37 protein secreted from Pichia pastoris. J Microbiol 47(3):358–362
    • (2009) J Microbiol , vol.47 , Issue.3 , pp. 358-362
    • Kim, S.J.1    Quan, R.2    Lee, S.J.3    Lee, H.K.4    Choi, J.K.5
  • 16
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • COI: 1:CAS:528:DC%2BD3MXlsFags7s%3D, PID: 5432063
    • Laemmli UK (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227(5259):680–685
    • (1970) Nature , vol.227 , Issue.5259 , pp. 680-685
    • Laemmli, U.K.1
  • 17
    • 70149103663 scopus 로고    scopus 로고
    • Carrier proteins for fusion expression of antimicrobial peptides in Escherichia coli
    • COI: 1:CAS:528:DC%2BD1MXot12ks7w%3D, PID: 19575694
    • Li Y (2009) Carrier proteins for fusion expression of antimicrobial peptides in Escherichia coli. Biotechnol Appl Biochem 54(1):1–9
    • (2009) Biotechnol Appl Biochem , vol.54 , Issue.1 , pp. 1-9
    • Li, Y.1
  • 19
    • 84899582719 scopus 로고    scopus 로고
    • Current scenario of peptide-based drugs: the key roles of cationic antitumor and antiviral peptides
    • PID: 24198814
    • Mulder KCL, Lima LA, Miranda VJ, Dias SC, Franco OL (2013a) Current scenario of peptide-based drugs: the key roles of cationic antitumor and antiviral peptides. Front Microbiol 4:321
    • (2013) Front Microbiol , vol.4 , pp. 321
    • Mulder, K.C.L.1    Lima, L.A.2    Miranda, V.J.3    Dias, S.C.4    Franco, O.L.5
  • 20
    • 84888216625 scopus 로고    scopus 로고
    • Critical Aspects to be considered prior to Large-Scale Production of peptides
    • COI: 1:CAS:528:DC%2BC3sXhslWhsbvF, PID: 23968346
    • Mulder KCL, Viana AAB, Xavier X, Parachin NS (2013b) Critical Aspects to be considered prior to Large-Scale Production of peptides. Curr Protein Pept Sci 14:556–567
    • (2013) Curr Protein Pept Sci , vol.14 , pp. 556-567
    • Mulder, K.C.L.1    Viana, A.A.B.2    Xavier, X.3    Parachin, N.S.4
  • 21
    • 84869098810 scopus 로고    scopus 로고
    • Expression systems for heterologous production of antimicrobial peptides
    • COI: 1:CAS:528:DC%2BC38XhslKqsL%2FP, PID: 23022589
    • Parachin NS, Mulder KC, Viana AA, Dias SC, Franco OL (2012) Expression systems for heterologous production of antimicrobial peptides. Peptides 38(2):446–456
    • (2012) Peptides , vol.38 , Issue.2 , pp. 446-456
    • Parachin, N.S.1    Mulder, K.C.2    Viana, A.A.3    Dias, S.C.4    Franco, O.L.5
  • 23
    • 84869227893 scopus 로고    scopus 로고
    • Exploring the pharmacological potential of promiscuous host-defense peptides: from natural screenings to biotechnological applications
    • PID: 22125552
    • Silva ON, Mulder KC, Barbosa AE, Otero-Gonzalez AJ, Lopez-Abarrategui C, Rezende TM et al (2011) Exploring the pharmacological potential of promiscuous host-defense peptides: from natural screenings to biotechnological applications. Front Microbiol 2:232
    • (2011) Front Microbiol , vol.2 , pp. 232
    • Silva, O.N.1    Mulder, K.C.2    Barbosa, A.E.3    Otero-Gonzalez, A.J.4    Lopez-Abarrategui, C.5    Rezende, T.M.6
  • 24
    • 84938661491 scopus 로고    scopus 로고
    • Patent: Antimicrobial, insecticide and antitumor synthetic molecule, composition, use and microorganism inhibition method. INPI
    • Silva ON, Migliolo L, Dias SC, Rezende TMB, Franco, OL (2011b) Patent: Antimicrobial, insecticide and antitumor synthetic molecule, composition, use and microorganism inhibition method. INPI, Brazil Patent Number 0000221109717908
    • (2011) Brazil Patent
    • Silva, O.N.1    Migliolo, L.2    Dias, S.C.3    Rezende, T.M.B.4    Franco, O.L.5
  • 26
    • 17844363007 scopus 로고    scopus 로고
    • cDNA cloning, functional expression and antifungal activities of a dimeric plant defensin SPE10 from Pachyrrhizus erosus seeds
    • COI: 1:CAS:528:DC%2BD2MXjtV2hu78%3D, PID: 15821865
    • Song X, Wang J, Wu F, Li X, Teng M, Gong W (2005) cDNA cloning, functional expression and antifungal activities of a dimeric plant defensin SPE10 from Pachyrrhizus erosus seeds. Plant Mol Biol 57(1):13–20
    • (2005) Plant Mol Biol , vol.57 , Issue.1 , pp. 13-20
    • Song, X.1    Wang, J.2    Wu, F.3    Li, X.4    Teng, M.5    Gong, W.6
  • 27
    • 84858706292 scopus 로고    scopus 로고
    • Expression, purification, and antibacterial activity of bovine lactoferrampin–lactoferricin in Pichia pastoris
    • COI: 1:CAS:528:DC%2BC38XhslyntLw%3D
    • Tang XS, Tang ZR, Wang SP, Feng ZM, Zhou D, Li TJ et al (2012) Expression, purification, and antibacterial activity of bovine lactoferrampin–lactoferricin in Pichia pastoris. Appl Biochem Biotech 166(3):640–651
    • (2012) Appl Biochem Biotech , vol.166 , Issue.3 , pp. 640-651
    • Tang, X.S.1    Tang, Z.R.2    Wang, S.P.3    Feng, Z.M.4    Zhou, D.5    Li, T.J.6
  • 28
    • 0026739991 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications
    • Towbin H, Staehelin T, Gordo J (1979) Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Biotechnol Adv 24:145–149
    • (1979) Biotechnol Adv , vol.24 , pp. 145-149
    • Towbin, H.1    Staehelin, T.2    Gordo, J.3
  • 29
    • 0035967521 scopus 로고    scopus 로고
    • Membrane activity of the peptide antibiotic clavanin and the importance of its glycine residues
    • PID: 11371202
    • van Kan EJ, van der Bent A, Demel RA, de Kruijff B (2001) Membrane activity of the peptide antibiotic clavanin and the importance of its glycine residues. Biochemistry 40(21):6398–6405
    • (2001) Biochemistry , vol.40 , Issue.21 , pp. 6398-6405
    • van Kan, E.J.1    van der Bent, A.2    Demel, R.A.3    de Kruijff, B.4
  • 30
    • 0037129944 scopus 로고    scopus 로고
    • Clavanin permeabilizes target membranes via two distinctly different pH-dependent mechanisms
    • PID: 12056883
    • van Kan EJ, Demel RA, Breukink E, van der Bent A, de Kruijff B (2002) Clavanin permeabilizes target membranes via two distinctly different pH-dependent mechanisms. Biochemistry 41(24):7529–7539
    • (2002) Biochemistry , vol.41 , Issue.24 , pp. 7529-7539
    • van Kan, E.J.1    Demel, R.A.2    Breukink, E.3    van der Bent, A.4    de Kruijff, B.5
  • 32
    • 0141679312 scopus 로고    scopus 로고
    • The peptide antibiotic clavanin A interacts strongly and specifically with lipid bilayers
    • PID: 14503887
    • van Kan EJ, Ganchev DN, Snel MM, Chupin V, van der Bent A, de Kruijff B (2003b) The peptide antibiotic clavanin A interacts strongly and specifically with lipid bilayers. Biochemistry 42(38):11366–11372
    • (2003) Biochemistry , vol.42 , Issue.38 , pp. 11366-11372
    • van Kan, E.J.1    Ganchev, D.N.2    Snel, M.M.3    Chupin, V.4    van der Bent, A.5    de Kruijff, B.6
  • 34
    • 84890417273 scopus 로고    scopus 로고
    • 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
    • COI: 1:CAS:528:DC%2BC3sXhvFyksLbJ, PID: 24269762
    • Viragh M, Voros D, Kele Z, Kovacs L, Fizil A, Lakatos G et al (2014) 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. Protein Expr Purif 94:79–84
    • (2014) Protein Expr Purif , vol.94 , pp. 79-84
    • Viragh, M.1    Voros, D.2    Kele, Z.3    Kovacs, L.4    Fizil, A.5    Lakatos, G.6
  • 35
    • 0031579445 scopus 로고    scopus 로고
    • Isolation of the Pichia pastoris glyceraldehyde-3-phosphate dehydrogenase gene and regulation and use of its promoter
    • COI: 1:CAS:528:DyaK2sXlslOjug%3D%3D, PID: 9047342
    • Waterham HR, Digan ME, Koutz PJ, Lair SV, Cregg JM (1997) Isolation of the Pichia pastoris glyceraldehyde-3-phosphate dehydrogenase gene and regulation and use of its promoter. Gene 186(1):37–44
    • (1997) Gene , vol.186 , Issue.1 , pp. 37-44
    • Waterham, H.R.1    Digan, M.E.2    Koutz, P.J.3    Lair, S.V.4    Cregg, J.M.5
  • 36
    • 77953612696 scopus 로고    scopus 로고
    • Effective and stable porcine interferon-alpha production by Pichia pastoris fed-batch cultivation with multi-variables clustering and analysis
    • COI: 1:CAS:528:DC%2BC3cXksFWmtLg%3D, PID: 19649659
    • Yu R, Dong S, Zhu Y, Jin H, Gao M, Duan Z et al (2010) Effective and stable porcine interferon-alpha production by Pichia pastoris fed-batch cultivation with multi-variables clustering and analysis. Bioprocess Biosyst Eng 33(4):473–483
    • (2010) Bioprocess Biosyst Eng , vol.33 , Issue.4 , pp. 473-483
    • Yu, R.1    Dong, S.2    Zhu, Y.3    Jin, H.4    Gao, M.5    Duan, Z.6
  • 37
    • 67651100721 scopus 로고    scopus 로고
    • Recent advances on the GAP promoter derived expression system of Pichia pastoris
    • COI: 1:CAS:528:DC%2BD1MXmtlOnsLo%3D, PID: 18781398
    • Zhang AL, Luo JX, Zhang TY, Pan YW, Tan YH, Fu CY et al (2009) Recent advances on the GAP promoter derived expression system of Pichia pastoris. Mol Biol Rep 36(6):1611–1619
    • (2009) Mol Biol Rep , vol.36 , Issue.6 , pp. 1611-1619
    • Zhang, A.L.1    Luo, J.X.2    Zhang, T.Y.3    Pan, Y.W.4    Tan, Y.H.5    Fu, C.Y.6
  • 38
    • 84857555225 scopus 로고    scopus 로고
    • Production of bioactive sheep beta-defensin-1 in Pichia pastoris
    • PID: 21643707
    • Zhao P, Cao G (2012) Production of bioactive sheep beta-defensin-1 in Pichia pastoris. J Ind Microbiol Biotechnol 39(1):11–17
    • (2012) J Ind Microbiol Biotechnol , vol.39 , Issue.1 , pp. 11-17
    • Zhao, P.1    Cao, G.2


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