메뉴 건너뛰기




Volumn 89, Issue 1, 2013, Pages 33-43

Bacterial expression and antibiotic activities of recombinant variants of human β-defensins on pathogenic bacteria and M. tuberculosis

Author keywords

Antimicrobial peptides; Human defensins; Mycobacterium tuberculosis; Peptide yields; Protein expression

Indexed keywords

BETA DEFENSIN; PEPTIDE; RECOMBINANT PROTEIN;

EID: 84875451768     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.pep.2013.02.007     Document Type: Article
Times cited : (57)

References (56)
  • 4
    • 0036467390 scopus 로고    scopus 로고
    • Defensins of vertebrate animals
    • R.I. Lehrer, and T. Ganz Defensins of vertebrate animals Curr. Opin. Immunol. 14 2002 96 102
    • (2002) Curr. Opin. Immunol. , vol.14 , pp. 96-102
    • Lehrer, R.I.1    Ganz, T.2
  • 5
    • 0037165196 scopus 로고    scopus 로고
    • Antimicrobial peptides of multicellular organisms
    • M. Zasloff Antimicrobial peptides of multicellular organisms Nature 415 2002 389 395
    • (2002) Nature , vol.415 , pp. 389-395
    • Zasloff, M.1
  • 7
    • 60249087859 scopus 로고    scopus 로고
    • In vitro bactericidal activity of recombinant human β-defensin-3 against pathogenic bacterial strains in human tooth root canal
    • W. Song, Y. Shi, M. Xiao, H. Lu, T. Qu, P. Li, Gang Wu, and Y. Tian In vitro bactericidal activity of recombinant human β-defensin-3 against pathogenic bacterial strains in human tooth root canal Int. J. Antimicrob. Agent 33 2009 237 243
    • (2009) Int. J. Antimicrob. Agent , vol.33 , pp. 237-243
    • Song, W.1    Shi, Y.2    Xiao, M.3    Lu, H.4    Qu, T.5    Li, P.6    Wu, G.7    Tian, Y.8
  • 9
    • 0042905861 scopus 로고    scopus 로고
    • The role of antimicrobial peptides in innate immunity
    • T. Ganz The role of antimicrobial peptides in innate immunity Integr. Comp. Biol. 43 2003 300 304
    • (2003) Integr. Comp. Biol. , vol.43 , pp. 300-304
    • Ganz, T.1
  • 10
    • 22244480342 scopus 로고    scopus 로고
    • Structure-activity relation of human β-defensin 3: Influence of disulfide bonds and cysteine substitution on antimicrobial activity and cytotoxicity
    • E. Klüver, S. Schulz-Maronde, S. Scheid, B. Meyer, W.-G. Forssmann, and K. Adermann Structure-activity relation of human β-defensin 3: influence of disulfide bonds and cysteine substitution on antimicrobial activity and cytotoxicity Biochemistry 44 2005 9804 9816
    • (2005) Biochemistry , vol.44 , pp. 9804-9816
    • Klüver, E.1    Schulz-Maronde, S.2    Scheid, S.3    Meyer, B.4    Forssmann, W.-G.5    Adermann, K.6
  • 13
    • 0035937107 scopus 로고    scopus 로고
    • Isolation and characterization of human β-defensin-3, a novel human inducible peptide antibiotic
    • J. Harder, J. Bartels, E. Christophers, and J.-M. Schröder Isolation and characterization of human β-defensin-3, a novel human inducible peptide antibiotic J. Biol. Chem. 276 2001 5707 5713
    • (2001) J. Biol. Chem. , vol.276 , pp. 5707-5713
    • Harder, J.1    Bartels, J.2    Christophers, E.3    Schröder, J.-M.4
  • 19
    • 0035992072 scopus 로고    scopus 로고
    • Resazurin microtiter assay plate: Simple and inexpensive method for detection of drug resistance in Mycobacterium tuberculosis
    • J.C. Palomino, A. Martin, M. Camacho, H. Guerra, J. Swings, and F. Portaels Resazurin microtiter assay plate: simple and inexpensive method for detection of drug resistance in Mycobacterium tuberculosis Antimicrob. Agent Chemother. 46 2002 2720 2722
    • (2002) Antimicrob. Agent Chemother. , vol.46 , pp. 2720-2722
    • Palomino, J.C.1    Martin, A.2    Camacho, M.3    Guerra, H.4    Swings, J.5    Portaels, F.6
  • 20
    • 78751577575 scopus 로고    scopus 로고
    • Amino acid substitutions in an alpha-helical antimicrobial arachnid peptide affect its chemical properties and biological activity towards pathogenic bacteria but improves its therapeutic index
    • A. Rodríguez, E. Villegas, H. Satake, L.D. Possani, and G. Corzo Amino acid substitutions in an alpha-helical antimicrobial arachnid peptide affect its chemical properties and biological activity towards pathogenic bacteria but improves its therapeutic index Amino Acids 40 2011 61 68
    • (2011) Amino Acids , vol.40 , pp. 61-68
    • Rodríguez, A.1    Villegas, E.2    Satake, H.3    Possani, L.D.4    Corzo, G.5
  • 21
    • 59249083736 scopus 로고    scopus 로고
    • Expression, purification and structural studies of a short antimicrobial peptide
    • M. Zorko, B. Japel, I. Hafner-Bratkovič, and R. Jerala Expression, purification and structural studies of a short antimicrobial peptide Biochem. Biophys. Acta 1788 2009 314 323
    • (2009) Biochem. Biophys. Acta , vol.1788 , pp. 314-323
    • Zorko, M.1    Japel, B.2    Hafner-Bratkovič, I.3    Jerala, R.4
  • 22
    • 80054062747 scopus 로고    scopus 로고
    • Recombinant production of antimicrobial peptides in Escherichia coli: A review
    • Y. Li Recombinant production of antimicrobial peptides in Escherichia coli: a review Protein Expr. Purif. 80 2011 260 267
    • (2011) Protein Expr. Purif. , vol.80 , pp. 260-267
    • Li, Y.1
  • 23
    • 0028804911 scopus 로고
    • Effects of rare codon clusters on high-level expression of heterologous proteins in Escherichia coli
    • J.F. Kane Effects of rare codon clusters on high-level expression of heterologous proteins in Escherichia coli Curr. Opin. Biotechnol. 6 1995 494 500
    • (1995) Curr. Opin. Biotechnol. , vol.6 , pp. 494-500
    • Kane, J.F.1
  • 25
    • 0023143242 scopus 로고
    • Factors affecting the expression of foreign proteins in Escherichia coli
    • B.R. Glick, and G.K. Whitney Factors affecting the expression of foreign proteins in Escherichia coli J. Ind. Microbiol. 1 1987 277 282
    • (1987) J. Ind. Microbiol. , vol.1 , pp. 277-282
    • Glick, B.R.1    Whitney, G.K.2
  • 26
    • 3142662719 scopus 로고    scopus 로고
    • Preferential codons enhancing the expression level of human β-defensin-2 in recombinant Escherichia coli
    • L. Peng, Z. Xu, X. Fang, F. Wang, S. Yang, and P. Cen Preferential codons enhancing the expression level of human β-defensin-2 in recombinant Escherichia coli Protein Pept. Lett. 11 2004 339 344
    • (2004) Protein Pept. Lett. , vol.11 , pp. 339-344
    • Peng, L.1    Xu, Z.2    Fang, X.3    Wang, F.4    Yang, S.5    Cen, P.6
  • 27
    • 4344559551 scopus 로고    scopus 로고
    • High-level epression of soluble human β-defensin-2 in Escherichia coli
    • L. Peng, Z. Xu, X. Fang, F. Wang, and P. Cen High-level epression of soluble human β-defensin-2 in Escherichia coli Process Biochem. 39 2004 2199 2205
    • (2004) Process Biochem. , vol.39 , pp. 2199-2205
    • Peng, L.1    Xu, Z.2    Fang, X.3    Wang, F.4    Cen, P.5
  • 28
    • 33646059875 scopus 로고    scopus 로고
    • High-level expression of a soluble functional antimicrobial peptide, human β-defensin 2, in Escherichia coli
    • Z. Xu, L. Peng, Z. Zhong, X. Fang, and P. Cen High-level expression of a soluble functional antimicrobial peptide, human β-defensin 2, in Escherichia coli Biotechnol. Prog. 22 2006 382 386
    • (2006) Biotechnol. Prog. , vol.22 , pp. 382-386
    • Xu, Z.1    Peng, L.2    Zhong, Z.3    Fang, X.4    Cen, P.5
  • 29
    • 33746744319 scopus 로고    scopus 로고
    • Enhancement of soluble protein expression through the use of fusion tags
    • D. Esposito, and D.K. Chatterjee Enhancement of soluble protein expression through the use of fusion tags Curr. Opin. Biotechnol. 17 2006 353 358
    • (2006) Curr. Opin. Biotechnol. , vol.17 , pp. 353-358
    • Esposito, D.1    Chatterjee, D.K.2
  • 30
    • 3543116141 scopus 로고    scopus 로고
    • High-level expression and purification of a recombinant hBD-1fused to LMM protein in Escherichia coli
    • I. Cipáková, E. Hostinová, J. Gasperík, and V. Velebny High-level expression and purification of a recombinant hBD-1fused to LMM protein in Escherichia coli Protein Expr. Purif. 37 2004 207 212
    • (2004) Protein Expr. Purif. , vol.37 , pp. 207-212
    • Cipáková, I.1    Hostinová, E.2    Gasperík, J.3    Velebny, V.4
  • 31
    • 33747735624 scopus 로고    scopus 로고
    • High-level production of bioactive human β-defensin-4 in Escherichia coli by soluble fusion expression
    • Z. Xu, Z. Zhong, L. Huang, L. Peng, F. Wang, and P. Cen High-level production of bioactive human β-defensin-4 in Escherichia coli by soluble fusion expression Appl. Microbiol. Biotechnol. 72 2006 471 479
    • (2006) Appl. Microbiol. Biotechnol. , vol.72 , pp. 471-479
    • Xu, Z.1    Zhong, Z.2    Huang, L.3    Peng, L.4    Wang, F.5    Cen, P.6
  • 33
    • 4444343822 scopus 로고    scopus 로고
    • Fusion expression of human β-defensin-2 from multiple joined genes in Escherichia coli
    • F. Wang, X. Fang, Z. Xu, L. Peng, and P. Cen Fusion expression of human β-defensin-2 from multiple joined genes in Escherichia coli Prep. Biochem. Biotechnol. 34 2004 215 225
    • (2004) Prep. Biochem. Biotechnol. , vol.34 , pp. 215-225
    • Wang, F.1    Fang, X.2    Xu, Z.3    Peng, L.4    Cen, P.5
  • 34
    • 34248631715 scopus 로고    scopus 로고
    • Soluble expression of active human β-defensin-3 in Escherichia coli and its effects on the growth of host cells
    • L.G. Si, X.C. Liu, Y.Y. Lu, G.Y. Wang, and W.M. Li Soluble expression of active human β-defensin-3 in Escherichia coli and its effects on the growth of host cells Chin. Med. J. 120 2007 708 713
    • (2007) Chin. Med. J. , vol.120 , pp. 708-713
    • Si, L.G.1    Liu, X.C.2    Lu, Y.Y.3    Wang, G.Y.4    Li, W.M.5
  • 35
    • 33747757981 scopus 로고    scopus 로고
    • Expression and purifcation of recombinant human alpha-defensins in Escherichia coli
    • M. Pazgier, and J. Lubkowski Expression and purifcation of recombinant human alpha-defensins in Escherichia coli Protein Expr. Purif. 49 2006 1 8
    • (2006) Protein Expr. Purif. , vol.49 , pp. 1-8
    • Pazgier, M.1    Lubkowski, J.2
  • 36
    • 0027445909 scopus 로고
    • Recombinant dna procedures for producing small antimicrobial cationic peptides in bacteria
    • K.L. Piers, M.H. Brown, and R.E.W. Hancock Recombinant dna procedures for producing small antimicrobial cationic peptides in bacteria Gene 134 1993 7 13
    • (1993) Gene , vol.134 , pp. 7-13
    • Piers, K.L.1    Brown, M.H.2    Hancock, R.E.W.3
  • 38
    • 0032577940 scopus 로고    scopus 로고
    • Determinants of recombinant production of antimicrobial cationic peptides and creation of peptide variants in bacteria
    • L. Zhang, T. Falla, M. Wu, S. Fidai, J. Burian, W. Kay, and R.E.W. Hancock Determinants of recombinant production of antimicrobial cationic peptides and creation of peptide variants in bacteria Biochem. Biophys. Res. Commun. 247 1998 674 680
    • (1998) Biochem. Biophys. Res. Commun. , vol.247 , pp. 674-680
    • Zhang, L.1    Falla, T.2    Wu, M.3    Fidai, S.4    Burian, J.5    Kay, W.6    Hancock, R.E.W.7
  • 39
    • 67149086754 scopus 로고    scopus 로고
    • Direct expression of antimicrobial peptides in an intact form by a translationally coupled two-cistron expression system
    • S.A. Jang, B.H. Sung, J.H. Cho, and S.C. Kim1 Direct expression of antimicrobial peptides in an intact form by a translationally coupled two-cistron expression system Appl. Environ. Microbiol. 75 2009 3980 3986
    • (2009) Appl. Environ. Microbiol. , vol.75 , pp. 3980-3986
    • Jang, S.A.1    Sung, B.H.2    Cho, J.H.3    Kim, S.C.4
  • 40
    • 78751582328 scopus 로고    scopus 로고
    • Expression systems of human β-defensins: Vectors, purification and biological activities
    • L.L. Corrales-Garcia, L.D. Possani, and G. Corzo Expression systems of human β-defensins: vectors, purification and biological activities Amino Acids 40 2011 5 13
    • (2011) Amino Acids , vol.40 , pp. 5-13
    • Corrales-Garcia, L.L.1    Possani, L.D.2    Corzo, G.3
  • 41
    • 78149268666 scopus 로고    scopus 로고
    • Disperse distribution of cationic amino acids on hydrophilic surface of helical wheel enhances antimicrobial peptide activity
    • Y.S. Kim, and H.J. Cha Disperse distribution of cationic amino acids on hydrophilic surface of helical wheel enhances antimicrobial peptide activity Biotechnol. Bioeng. 107 2010 216 223
    • (2010) Biotechnol. Bioeng. , vol.107 , pp. 216-223
    • Kim, Y.S.1    Cha, H.J.2
  • 42
    • 79953237054 scopus 로고    scopus 로고
    • Peptide promiscuity: An evolutionary concept for plant defense
    • O.L. Franco Peptide promiscuity: an evolutionary concept for plant defense Fed. Eur. Biochem. Soc. 585 2011 995 1000
    • (2011) Fed. Eur. Biochem. Soc. , vol.585 , pp. 995-1000
    • Franco, O.L.1
  • 44
    • 0034283216 scopus 로고    scopus 로고
    • The role of cationic antimicrobial peptides in innate host defences
    • R.E.W. Hancock, and G. Diamond The role of cationic antimicrobial peptides in innate host defences Trends Microbiol. 8 2000 402 410
    • (2000) Trends Microbiol. , vol.8 , pp. 402-410
    • Hancock, R.E.W.1    Diamond, G.2
  • 46
    • 33646460123 scopus 로고    scopus 로고
    • Production of bioactive human β-defensin-3 in Escherichia coli by soluble fusion expression
    • L. Huang, J. Wang, Z. Zhong, L. Peng, H. Chen, Z. Xu, and P. Cen Production of bioactive human β-defensin-3 in Escherichia coli by soluble fusion expression Biotechnol. Lett. 28 2006 627 632
    • (2006) Biotechnol. Lett. , vol.28 , pp. 627-632
    • Huang, L.1    Wang, J.2    Zhong, Z.3    Peng, L.4    Chen, H.5    Xu, Z.6    Cen, P.7
  • 48
    • 77956689158 scopus 로고    scopus 로고
    • Interaction of cationic antimicrobial peptides with phospholipid vesicles and their antibacterial activity
    • H.T. Chou, H.W. Wen, T.Y. Kuo, C.C. Lin, and W.J. Chen Interaction of cationic antimicrobial peptides with phospholipid vesicles and their antibacterial activity Peptides 31 2010 1811 1820
    • (2010) Peptides , vol.31 , pp. 1811-1820
    • Chou, H.T.1    Wen, H.W.2    Kuo, T.Y.3    Lin, C.C.4    Chen, W.J.5
  • 49
    • 0042808526 scopus 로고    scopus 로고
    • Engineering disulfide bridges to dissect antimicrobial and chemotactic activities of human β-defensin 3
    • Z. Wu, D.M. Hoover, D. Yang, C. Boulègue, F. Santamaria, J.J. Oppenheim, J. Lubkowski, and W. Lu Engineering disulfide bridges to dissect antimicrobial and chemotactic activities of human β-defensin 3 PNAS 100 2003 8880 8885
    • (2003) PNAS , vol.100 , pp. 8880-8885
    • Wu, Z.1    Hoover, D.M.2    Yang, D.3    Boulègue, C.4    Santamaria, F.5    Oppenheim, J.J.6    Lubkowski, J.7    Lu, W.8
  • 50
    • 10344240423 scopus 로고    scopus 로고
    • Structure-activity relationships in defensin dimers: A novel link between β-defensin tertiary structure and antimicrobial activity
    • D.J. Campopiano, D.J. Clarke, N.C. Polfer, P.E. Barran, R.J. Langley, J.R.W. Govan, A. Maxwell, and J.R. Dorin Structure-activity relationships in defensin dimers: a novel link between β-defensin tertiary structure and antimicrobial activity J. Biol. Chem. 279 2004 48671 48679
    • (2004) J. Biol. Chem. , vol.279 , pp. 48671-48679
    • Campopiano, D.J.1    Clarke, D.J.2    Polfer, N.C.3    Barran, P.E.4    Langley, R.J.5    Govan, J.R.W.6    Maxwell, A.7    Dorin, J.R.8
  • 51
    • 33746347680 scopus 로고    scopus 로고
    • Tandem repeat mhbd2 gene enhance the soluble fusion expression of hBD2 in Escherichia coli
    • Z. Zhong, Z. Xu, L. Peng, L. Huang, X. Fang, and P. Cen Tandem repeat mhbd2 gene enhance the soluble fusion expression of hBD2 in Escherichia coli Appl. Microbiol. Biotechnol. 71 2006 661 667
    • (2006) Appl. Microbiol. Biotechnol. , vol.71 , pp. 661-667
    • Zhong, Z.1    Xu, Z.2    Peng, L.3    Huang, L.4    Fang, X.5    Cen, P.6
  • 55
    • 0029761216 scopus 로고    scopus 로고
    • In vitro activities of fourteen antimicrobial agents against drug susceptible and resistant clinical isolates of Mycobacterium tuberculosis and comparative intracellular activities against the virulent H37Rv strain in human macrophages
    • N. Rastogi, V. Labrousse, and K.S. Goh In vitro activities of fourteen antimicrobial agents against drug susceptible and resistant clinical isolates of Mycobacterium tuberculosis and comparative intracellular activities against the virulent H37Rv strain in human macrophages Curr. Microbiol. 33 1996 167 175
    • (1996) Curr. Microbiol. , vol.33 , pp. 167-175
    • Rastogi, N.1    Labrousse, V.2    Goh, K.S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.