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Volumn 81, Issue 2, 2012, Pages 201-210

A novel protocol for the production of recombinant LL-37 expressed as a thioredoxin fusion protein

Author keywords

Antimicrobial peptide; LL 37; Oligomerization; Thioredoxin fusion protein; Thrombin cleavage

Indexed keywords

ANTIINFECTIVE AGENT; CATHELICIDIN; CATHELICIDIN ANTIMICROBIAL PEPTIDE; HYBRID PROTEIN; THIOREDOXIN; THROMBIN;

EID: 82155186247     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.pep.2011.10.011     Document Type: Article
Times cited : (20)

References (28)
  • 1
    • 0035877995 scopus 로고    scopus 로고
    • Human cathelicidin, hCAP-18, is processed to the antimicrobial peptide LL-37 by extracellular cleavage with proteinase 3
    • O.E. Sørensen, P. Follin, A.H. Johnsen, J. Calafat, G.S. Tjabringa, P.S. Hiemstra, and N. Borregaard Human cathelicidin, hCAP-18, is processed to the antimicrobial peptide LL-37 by extracellular cleavage with proteinase 3 Blood 97 2001 3951 3959
    • (2001) Blood , vol.97 , pp. 3951-3959
    • Sørensen, O.E.1    Follin, P.2    Johnsen, A.H.3    Calafat, J.4    Tjabringa, G.S.5    Hiemstra, P.S.6    Borregaard, N.7
  • 2
    • 33748935159 scopus 로고    scopus 로고
    • LL-37, the only human member of the cathelicidin family of antimicrobial peptides
    • DOI 10.1016/j.bbamem.2006.03.030, PII S000527360600126X
    • U.H. Dürr, U.S. Sudheendra, and A. Ramamoorthy LL-37, the only human member of the cathelicidin family of antimicrobial peptides Biochim. Biophys. Acta 1758 2006 1408 1425 (Pubitemid 44436081)
    • (2006) Biochimica et Biophysica Acta - Biomembranes , vol.1758 , Issue.9 , pp. 1408-1425
    • Durr, U.H.N.1    Sudheendra, U.S.2    Ramamoorthy, A.3
  • 4
    • 58149263244 scopus 로고    scopus 로고
    • The roles of cathelicidin LL-37 in immune defences and novel clinical applications
    • A. Nijnik, and R.E. Hancock The roles of cathelicidin LL-37 in immune defences and novel clinical applications Curr. Opin. Hematol. 16 2009 41 47
    • (2009) Curr. Opin. Hematol. , vol.16 , pp. 41-47
    • Nijnik, A.1    Hancock, R.E.2
  • 5
    • 77955654919 scopus 로고    scopus 로고
    • The human cathelicidin hCAP18/LL-37: A multifunctional peptide involved in mycobacterial infections
    • P. Méndez-Samperio The human cathelicidin hCAP18/LL-37: a multifunctional peptide involved in mycobacterial infections Peptides 31 2010 1791 1798
    • (2010) Peptides , vol.31 , pp. 1791-1798
    • Méndez-Samperio, P.1
  • 8
    • 84858859622 scopus 로고    scopus 로고
    • Circulating LL-37 is a biomarker for eczema severity in children
    • (in press), doi: 10.1111/j.1468-3083.2011.04083.x
    • T. Leung, K. Ching, A. Kong, G. Wong, J. Chan, K. Hon, Circulating LL-37 is a biomarker for eczema severity in children, J. Eur. Acad. Dermatol. Venereol. (in press), doi: 10.1111/j.1468-3083.2011.04083.x.
    • J. Eur. Acad. Dermatol. Venereol.
    • Leung, T.1    Ching, K.2    Kong, A.3    Wong, G.4    Chan, J.5    Hon, K.6
  • 9
    • 34247868094 scopus 로고    scopus 로고
    • Recombinant production of antimicrobial peptides in heterologous microbial systems
    • DOI 10.1042/BA20060207
    • A.B. Ingham, and R.J. Moore Recombinant production of antimicrobial peptides in heterologous microbial systems Biotechnol. Appl. Biochem. 47 2007 1 9 (Pubitemid 46762266)
    • (2007) Biotechnology and Applied Biochemistry , vol.47 , Issue.1 , pp. 1-9
    • Ingham, A.B.1    Moore, R.J.2
  • 10
    • 56649106249 scopus 로고    scopus 로고
    • RAPD: A database of recombinantly-produced antimicrobial peptides
    • Y. Li, and Z. Chen RAPD: a database of recombinantly-produced antimicrobial peptides FEMS Microbiol. Lett. 289 2008 126 129
    • (2008) FEMS Microbiol. Lett. , vol.289 , pp. 126-129
    • Li, Y.1    Chen, Z.2
  • 11
    • 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
  • 12
    • 70149103663 scopus 로고    scopus 로고
    • Carrier proteins for fusion expression of antimicrobial peptides in Escherichia coli
    • Y. Li Carrier proteins for fusion expression of antimicrobial peptides in Escherichia coli Biotechnol. Appl. Biochem. 54 2009 1 9
    • (2009) Biotechnol. Appl. Biochem. , vol.54 , pp. 1-9
    • Li, Y.1
  • 14
    • 33748948233 scopus 로고    scopus 로고
    • Expression and purification of a recombinant LL-37 from Escherichia coli
    • DOI 10.1016/j.bbamem.2006.02.003, PII S0005273606000502
    • J.Y. Moon, K.A. Henzler-Wildman, and A. Ramamoorthy Expression and purification of a recombinant LL-37 from Escherichia coli Biochim. Biophys. Acta 1758 2006 1351 1358 (Pubitemid 44436070)
    • (2006) Biochimica et Biophysica Acta - Biomembranes , vol.1758 , Issue.9 , pp. 1351-1358
    • Moon, J.-Y.1    Henzler-Wildman, K.A.2    Ramamoorthy, A.3
  • 15
    • 3543119574 scopus 로고    scopus 로고
    • Expression of bioactive recombinant GSLL-39, a variant of human antimicrobial peptide LL-37, in Escherichia coli
    • DOI 10.1016/j.pep.2004.06.007, PII S1046592804001937
    • Y.H. Yang, G.G. Zheng, G. Li, X.J. Zhang, Z.Y. Cao, Q. Rao, and K.F. Wu Expression of bioactive recombinant GSLL-39, a variant of human antimicrobial peptide LL-37, in Escherichia coli Protein Expr. Purif. 37 2004 229 235 (Pubitemid 39027265)
    • (2004) Protein Expression and Purification , vol.37 , Issue.1 , pp. 229-235
    • Yang, Y.-H.1    Zheng, G.-G.2    Li, G.3    Zhang, X.-J.4    Cao, Z.-Y.5    Rao, Q.6    Wu, K.-F.7
  • 16
    • 33646726320 scopus 로고    scopus 로고
    • Cloning, expression, isotope labeling, and purification of human antimicrobial peptide LL-37 in Escherichia coli for NMR studies
    • DOI 10.1016/j.pep.2005.10.022, PII S1046592805003803
    • Y. Li, X. Li, and G. Wang Cloning, expression, isotope labeling, and purification of human antimicrobial peptide LL-37 in Escherichia coli for NMR studies Protein Expr. Purif. 47 2006 498 505 (Pubitemid 43744452)
    • (2006) Protein Expression and Purification , vol.47 , Issue.2 , pp. 498-505
    • Li, Y.1    Li, X.2    Wang, G.3
  • 17
    • 34247370223 scopus 로고    scopus 로고
    • A novel method for purifying recombinant human host defense cathelicidin LL-37 by utilizing its inherent property of aggregation
    • DOI 10.1016/j.pep.2007.02.003, PII S1046592807000332
    • Y. Li, X. Li, H. Li, O. Lockridge, and G. Wang A novel method for purifying recombinant human host defense cathelicidin LL-37 by utilizing its inherent property of aggregation Protein Expr. Purif. 54 2007 157 165 (Pubitemid 46636313)
    • (2007) Protein Expression and Purification , vol.54 , Issue.1 , pp. 157-165
    • Li, Y.1    Li, X.2    Li, H.3    Lockridge, O.4    Wang, G.5
  • 20
    • 77049123683 scopus 로고    scopus 로고
    • Escherichia coli expression and purification of LL37 fused to a family III carbohydrate-binding module from Clostridium thermocellum
    • R. Ramos, L. Domingues, and M. Gama Escherichia coli expression and purification of LL37 fused to a family III carbohydrate-binding module from Clostridium thermocellum Protein Expr. Purif. 71 2010 1 7
    • (2010) Protein Expr. Purif. , vol.71 , pp. 1-7
    • Ramos, R.1    Domingues, L.2    Gama, M.3
  • 24
    • 0027445909 scopus 로고
    • Recombinant DNA procedures for producing small antimicrobial cationic peptides in bacteria
    • K.L. Piers, M.H. Brown, and R.E. 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.3
  • 25
    • 2942592015 scopus 로고    scopus 로고
    • Novel expression system for large-scale production and purification of recombinant class IIa bacteriocins and its application to piscicolin 126
    • DOI 10.1128/AEM.70.6.3292-3297.2004
    • G.M. Gibbs, B.E. Davidson, and A.J. Hillier Novel expression system for large-scale production and purification of recombinant class IIa bacteriocins and its application to piscicolin 126 Appl. Environ. Microbiol. 70 2004 3292 3297 (Pubitemid 38745870)
    • (2004) Applied and Environmental Microbiology , vol.70 , Issue.6 , pp. 3292-3297
    • Gibbs, G.M.1    Davidson, B.E.2    Hillier, A.J.3
  • 26
    • 38349008371 scopus 로고    scopus 로고
    • Production of active pediocin PA-1 in Escherichia coli using a thioredoxin gene fusion expression approach: Cloning, expression, purification, and characterization
    • L. Beaulieu, D. Tolkatchev, J.F. Jetté, D. Groleau, and M. Subirade Production of active pediocin PA-1 in Escherichia coli using a thioredoxin gene fusion expression approach: cloning, expression, purification, and characterization Can. J. Microbiol. 53 2007 1246 1258
    • (2007) Can. J. Microbiol. , vol.53 , pp. 1246-1258
    • Beaulieu, L.1    Tolkatchev, D.2    Jetté, J.F.3    Groleau, D.4    Subirade, M.5
  • 28
    • 34248395017 scopus 로고    scopus 로고
    • High-level production of a novel antimicrobial peptide perinerin in Escherichia coli by fusion expression
    • DOI 10.1007/s00284-006-0466-y
    • Q.F. Zhou, X.G. Luo, L. Ye, and T. Xi High-level production of a novel antimicrobial peptide perinerin in Escherichia coli by fusion expression Curr. Microbiol. 54 2007 366 370 (Pubitemid 46733871)
    • (2007) Current Microbiology , vol.54 , Issue.5 , pp. 366-370
    • Zhou, Q.-F.1    Luo, X.-G.2    Ye, L.3    Xi, T.4


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