메뉴 건너뛰기




Volumn 78, Issue 1, 2008, Pages 123-130

High-level expression of an antimicrobial peptide histonin as a natural form by multimerization and furin-mediated cleavage

Author keywords

Antimicrobial peptide; Furin; Fusion; Histonin; Multimerization

Indexed keywords

ANTIMICROBIAL PEPTIDE; MULTIMERIZATION; PROTEOLYTIC DEGRADATION;

EID: 38349084056     PISSN: 01757598     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00253-007-1273-5     Document Type: Article
Times cited : (44)

References (33)
  • 1
    • 3543116141 scopus 로고    scopus 로고
    • High-level expression and purification of a recombinant hBD-1 fused to LMM protein in Escherichia coli
    • Cipakova I, Hostinova E, Gasperik J, Velebny V (2004) High-level expression and purification of a recombinant hBD-1 fused to LMM protein in Escherichia coli. Protein Expr Purif 37:207-212
    • (2004) Protein Expr Purif , vol.37 , pp. 207-212
    • Cipakova, I.1    Hostinova, E.2    Gasperik, J.3    Velebny, V.4
  • 3
    • 33749006591 scopus 로고    scopus 로고
    • The human beta-defensin-3, an antibacterial peptide with multiple biological functions
    • Dhople V, Krukemeyer A, Ramamoorthy A (2006) The human beta-defensin-3, an antibacterial peptide with multiple biological functions. Biochim Biophys Acta 1758:1499-1512
    • (2006) Biochim Biophys Acta , vol.1758 , pp. 1499-1512
    • Dhople, V.1    Krukemeyer, A.2    Ramamoorthy, A.3
  • 4
    • 33748935159 scopus 로고    scopus 로고
    • LL-37, the only human member of the cathelicidin family of antimicrobial peptides
    • Dürr UH, Sudheendra US, Ramamoorthy A (2006) LL-37, the only human member of the cathelicidin family of antimicrobial peptides. Biochim Biophys Acta 1758:1408-1425
    • (2006) Biochim Biophys Acta , vol.1758 , pp. 1408-1425
    • Dürr, U.H.1    Sudheendra, U.S.2    Ramamoorthy, A.3
  • 5
    • 33845699790 scopus 로고    scopus 로고
    • Antimicrobial and host-defense peptides as new anti-infective therapeutic strategies
    • Hancock RE, Sahl HG (2006) Antimicrobial and host-defense peptides as new anti-infective therapeutic strategies. Nat Biotechnol 24:1551-1557
    • (2006) Nat Biotechnol , vol.24 , pp. 1551-1557
    • Hancock, R.E.1    Sahl, H.G.2
  • 6
    • 34247868094 scopus 로고    scopus 로고
    • Recombinant production of antimicrobial peptides in heterologous microbial systems
    • Ingham AB, Moore RJ (2007) Recombinant production of antimicrobial peptides in heterologous microbial systems. Biotechnol Appl Biochem 47:1-9
    • (2007) Biotechnol Appl Biochem , vol.47 , pp. 1-9
    • Ingham, A.B.1    Moore, R.J.2
  • 7
    • 0029026714 scopus 로고
    • The stability of Escherichia coli lacZ mRNA depends upon the simultaneity of its synthesis and translation
    • Iost I, Dreyfus M (1995) The stability of Escherichia coli lacZ mRNA depends upon the simultaneity of its synthesis and translation. EMBO J 14:3252-3261
    • (1995) EMBO J , vol.14 , pp. 3252-3261
    • Iost, I.1    Dreyfus, M.2
  • 9
    • 33747718706 scopus 로고    scopus 로고
    • Expression of the cationic antimicrobial peptide lactoferricin fused with the anionic peptide in Escherichia coli
    • Kim HK, Chun DS, Kim JS, Yun CH, Lee JH, Hong SK, Kang DK (2006) Expression of the cationic antimicrobial peptide lactoferricin fused with the anionic peptide in Escherichia coli. Appl Microbiol Biotechnol 72:330-338
    • (2006) Appl Microbiol Biotechnol , vol.72 , pp. 330-338
    • Kim, H.K.1    Chun, D.S.2    Kim, J.S.3    Yun, C.H.4    Lee, J.H.5    Hong, S.K.6    Kang, D.K.7
  • 10
    • 0032006495 scopus 로고    scopus 로고
    • Acidic peptide-mediated expression of the antimicrobial peptide buforin II as tandem repeats in Escherichia coli
    • Lee JH, Minn I, Park CB, Kim SC (1998) Acidic peptide-mediated expression of the antimicrobial peptide buforin II as tandem repeats in Escherichia coli. Protein Expr Purif 12:53-60
    • (1998) Protein Expr Purif , vol.12 , pp. 53-60
    • Lee, J.H.1    Minn, I.2    Park, C.B.3    Kim, S.C.4
  • 11
    • 0034597709 scopus 로고    scopus 로고
    • High-level expression of antimicrobial peptide mediated by a fusion partner reinforcing formation of inclusion bodies
    • Lee JH, Kim JH, Hwang SW, Lee WJ, Yoon HK, Lee HS, Hong SS (2000) High-level expression of antimicrobial peptide mediated by a fusion partner reinforcing formation of inclusion bodies. Biochem Biophys Res Commun 277:575-580
    • (2000) Biochem Biophys Res Commun , vol.277 , pp. 575-580
    • Lee, J.H.1    Kim, J.H.2    Hwang, S.W.3    Lee, W.J.4    Yoon, H.K.5    Lee, H.S.6    Hong, S.S.7
  • 12
    • 0036256531 scopus 로고    scopus 로고
    • Enhanced expression of tandem multimers of the antimicrobial peptide buforin II in Escherichia coli by the DEAD-box protein and trxB mutant
    • Lee JH, Kim MS, Cho JH, Kim SC (2002) Enhanced expression of tandem multimers of the antimicrobial peptide buforin II in Escherichia coli by the DEAD-box protein and trxB mutant. Appl Microbiol Biotechnol 58:790-796
    • (2002) Appl Microbiol Biotechnol , vol.58 , pp. 790-796
    • Lee, J.H.1    Kim, M.S.2    Cho, J.H.3    Kim, S.C.4
  • 13
    • 11844287624 scopus 로고    scopus 로고
    • High level expression, purification, and characterization of the shrimp antimicrobial peptide, Ch-penaeidin, in Pichia pastoris
    • Li L, Wang JX, Zhao XF, Kang CJ, Liu N, Xiang JH, Li FH, Sueda S, Kondo H (2005) High level expression, purification, and characterization of the shrimp antimicrobial peptide, Ch-penaeidin, in Pichia pastoris. Protein Expr Purif 39:144-151
    • (2005) Protein Expr Purif , vol.39 , pp. 144-151
    • Li, L.1    Wang, J.X.2    Zhao, X.F.3    Kang, C.J.4    Liu, N.5    Xiang, J.H.6    Li, F.H.7    Sueda, S.8    Kondo, H.9
  • 14
    • 33750446295 scopus 로고    scopus 로고
    • Ultrashort antibacterial and antifungal lipopeptides
    • Makovitzki A, Avrahami D, Shai Y (2006) Ultrashort antibacterial and antifungal lipopeptides. Proc Natl Acad Sci U S A 103:15997-16002
    • (2006) Proc Natl Acad Sci U S a , vol.103 , pp. 15997-16002
    • Makovitzki, A.1    Avrahami, D.2    Shai, Y.3
  • 15
    • 28444457793 scopus 로고    scopus 로고
    • Membrane thinning due to antimicrobial peptide binding: An atomic force microscopy study of MSI-78 in lipid bilayers
    • Mecke A, Lee DK, Ramamoorthy A, Orr BG, Banaszak Holl MM (2005) Membrane thinning due to antimicrobial peptide binding: an atomic force microscopy study of MSI-78 in lipid bilayers. Biophys J 89:4043-4050
    • (2005) Biophys J , vol.89 , pp. 4043-4050
    • Mecke, A.1    Lee, D.K.2    Ramamoorthy, A.3    Orr, B.G.4    Banaszak Holl, M.M.5
  • 16
    • 20744456789 scopus 로고
    • Solid phase peptide synthesis, I, the synthesis of a tetrapeptide
    • Merrifield RB (1963) Solid phase peptide synthesis, I, the synthesis of a tetrapeptide. J Am Chem Soc 85:2149-2154
    • (1963) J Am Chem Soc , vol.85 , pp. 2149-2154
    • Merrifield, R.B.1
  • 17
    • 0026775916 scopus 로고
    • Human furin is a calcium-dependent serine endoprotease that recognizes the sequence Arg-X-X-Arg and efficiently cleaves anthrax toxin protective antigen
    • Molloy SS, Bresnahan PA, Leppla SH, Klimpel KR, Thomas G (1992) Human furin is a calcium-dependent serine endoprotease that recognizes the sequence Arg-X-X-Arg and efficiently cleaves anthrax toxin protective antigen. J Biol Chem 267:16396-16402
    • (1992) J Biol Chem , vol.267 , pp. 16396-16402
    • Molloy, S.S.1    Bresnahan, P.A.2    Leppla, S.H.3    Klimpel, K.R.4    Thomas, G.5
  • 18
    • 34247117757 scopus 로고    scopus 로고
    • Cationic host defence peptides: Innate immune regulatory peptides as a novel approach for treating infections
    • Mookherjee N, Hancock RE (2007) Cationic host defence peptides: innate immune regulatory peptides as a novel approach for treating infections. Cell Mol Life Sci 64:922-933
    • (2007) Cell Mol Life Sci , vol.64 , pp. 922-933
    • Mookherjee, N.1    Hancock, R.E.2
  • 19
    • 33748948233 scopus 로고    scopus 로고
    • Expression and purification of a recombinant LL-37 from Escherichia coli
    • Moon JY, Henzler-Wildman KA, Ramamoorthy A (2006) Expression and purification of a recombinant LL-37 from Escherichia coli. Biochim Biophys Acta 1758:1351-1358
    • (2006) Biochim Biophys Acta , vol.1758 , pp. 1351-1358
    • Moon, J.Y.1    Henzler-Wildman, K.A.2    Ramamoorthy, A.3
  • 20
    • 11844252589 scopus 로고    scopus 로고
    • Expression of SMAP-29 cathelicidin-like peptide in bacterial cells by intein-mediated system
    • Morassutti C, Amicis FD, Bandiera A, Marchetti S (2005) Expression of SMAP-29 cathelicidin-like peptide in bacterial cells by intein-mediated system. Protein Expr Purif 39:160-168
    • (2005) Protein Expr Purif , vol.39 , pp. 160-168
    • Morassutti, C.1    Amicis, F.D.2    Bandiera, A.3    Marchetti, S.4
  • 22
    • 0001439249 scopus 로고    scopus 로고
    • Structure-activity analysis of buforin II, a histone H2A-derived antimicrobial peptide: The proline hinge is responsible for the cell-penetrating ability of buforin II
    • Park CB, Yi KS, Matsuzaki K, Kim MS, Kim SC (2000) Structure-activity analysis of buforin II, a histone H2A-derived antimicrobial peptide: the proline hinge is responsible for the cell-penetrating ability of buforin II. Proc Natl Acad Sci U S A 97:8245-8250
    • (2000) Proc Natl Acad Sci U S a , vol.97 , pp. 8245-8250
    • Park, C.B.1    Yi, K.S.2    Matsuzaki, K.3    Kim, M.S.4    Kim, S.C.5
  • 23
    • 1842639632 scopus 로고    scopus 로고
    • Helix stability confers salt resistance upon helical antimicrobial peptides
    • Park IY, Cho JH, Kim KS, Kim YB, Kim MS, Kim SC (2004) Helix stability confers salt resistance upon helical antimicrobial peptides. J Biol Chem 279:13896-13901
    • (2004) J Biol Chem , vol.279 , pp. 13896-13901
    • Park, I.Y.1    Cho, J.H.2    Kim, K.S.3    Kim, Y.B.4    Kim, M.S.5    Kim, S.C.6
  • 24
    • 33646474970 scopus 로고    scopus 로고
    • Structures of the dimeric and monomeric variants of magainin antimicrobial peptides (MSI-78 and MSI-594) in micelles and bilayers, determined by NMR spectroscopy
    • Porcelli F, Buck-Koehntop BA, Thennarasu S, Ramamoorthy A, Veglia G (2006) Structures of the dimeric and monomeric variants of magainin antimicrobial peptides (MSI-78 and MSI-594) in micelles and bilayers, determined by NMR spectroscopy. Biochemistry 45:5793-5799
    • (2006) Biochemistry , vol.45 , pp. 5793-5799
    • Porcelli, F.1    Buck-Koehntop, B.A.2    Thennarasu, S.3    Ramamoorthy, A.4    Veglia, G.5
  • 25
    • 33745747109 scopus 로고    scopus 로고
    • Solid-state NMR investigation of the membrane-disrupting mechanism of antimicrobial peptides MSI-78 and MSI-594 derived from magainin 2 and melittin
    • Ramamoorthy A, Thennarasu S, Lee DK, Tan A, Maloy L (2006) Solid-state NMR investigation of the membrane-disrupting mechanism of antimicrobial peptides MSI-78 and MSI-594 derived from magainin 2 and melittin. Biophys J 91:206-216
    • (2006) Biophys J , vol.91 , pp. 206-216
    • Ramamoorthy, A.1    Thennarasu, S.2    Lee, D.K.3    Tan, A.4    Maloy, L.5
  • 29
    • 33746141286 scopus 로고    scopus 로고
    • Design of a peptibody consisting of the antimicrobial peptide dhvar5 and a llama variable heavy-chain antibody fragment
    • Szynol A, de Haard JJ, Veerman EC, de Soet JJ, van Nieuw Amerongen AV (2006) Design of a peptibody consisting of the antimicrobial peptide dhvar5 and a llama variable heavy-chain antibody fragment. Chem Biol Drug Des 67:425-431
    • (2006) Chem Biol Drug des , vol.67 , pp. 425-431
    • Szynol, A.1    De Haard, J.J.2    Veerman, E.C.3    De Soet, J.J.4    Van Nieuw Amerongen, A.V.5
  • 30
    • 0029983494 scopus 로고    scopus 로고
    • Expression of soluble cloned porcine pepsinogen a in Escherichia coli
    • Tanaka T, Yada RY (1996) Expression of soluble cloned porcine pepsinogen A in Escherichia coli. Biochem J 315:443-446
    • (1996) Biochem J , vol.315 , pp. 443-446
    • Tanaka, T.1    Yada, R.Y.2
  • 31
    • 25144438913 scopus 로고    scopus 로고
    • Facilitation of expression and purification of an antimicrobial peptide by fusion with baculoviral polyhedrin in Escherichia coli
    • Wei Q, Kim YS, Seo JH, Jang WS, Lee IH, Cha HJ (2005) Facilitation of expression and purification of an antimicrobial peptide by fusion with baculoviral polyhedrin in Escherichia coli. Appl Environ Microbiol 71:5038-5043
    • (2005) Appl Environ Microbiol , vol.71 , pp. 5038-5043
    • Wei, Q.1    Kim, Y.S.2    Seo, J.H.3    Jang, W.S.4    Lee, I.H.5    Cha, H.J.6
  • 32
    • 33947369797 scopus 로고    scopus 로고
    • Expression and purification of a recombinant antibacterial peptide, cecropin, from Escherichia coli
    • Xu X, Jin F, Yu X, Ji S, Wang J, Cheng H, Wang C, Zhang W (2007) Expression and purification of a recombinant antibacterial peptide, cecropin, from Escherichia coli. Protein Expr Purif 53:293-301
    • (2007) Protein Expr Purif , vol.53 , pp. 293-301
    • Xu, X.1    Jin, F.2    Yu, X.3    Ji, S.4    Wang, J.5    Cheng, H.6    Wang, C.7    Zhang, W.8
  • 33
    • 0037165196 scopus 로고    scopus 로고
    • Antimicrobial peptides of multicellular organisms
    • Zasloff M (2002) Antimicrobial peptides of multicellular organisms. Nature 415:389-395
    • (2002) Nature , vol.415 , pp. 389-395
    • Zasloff, M.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.