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Volumn 16, Issue 1, 2017, Pages

Gene design, fusion technology and TEV cleavage conditions influence the purification of oxidized disulphide-rich venom peptides in Escherichia coli

Author keywords

Disulphide rich peptides; Escherichia coli (E. coli); Fusion protein; Gene design; High throughput expression; Periplasm; Recombinant expression; Venom peptides

Indexed keywords

CYSTEINE; DISULFIDE; DITHIOTHREITOL; HYBRID PROTEIN; PEPTIDE; PROLINE; PROTEINASE; TEV PROTEASE; VENOM;

EID: 85009962354     PISSN: None     EISSN: 14752859     Source Type: Journal    
DOI: 10.1186/s12934-016-0618-0     Document Type: Article
Times cited : (29)

References (32)
  • 1
    • 66949176303 scopus 로고    scopus 로고
    • Venomics as a drug discovery platform
    • Escoubas P, King GF. Venomics as a drug discovery platform. Expert Rev Proteom. 2009;6:221-4.
    • (2009) Expert Rev Proteom. , vol.6 , pp. 221-224
    • Escoubas, P.1    King, G.F.2
  • 2
    • 0242331757 scopus 로고    scopus 로고
    • Therapeutic potential of venom peptides
    • Lewis RJ, Garcia ML. Therapeutic potential of venom peptides. Nat Rev Drug Discov. 2003;2:790-802.
    • (2003) Nat Rev Drug Discov , vol.2 , pp. 790-802
    • Lewis, R.J.1    Garcia, M.L.2
  • 5
    • 0000908762 scopus 로고    scopus 로고
    • Analysis and predictions from Escherichia coli sequences
    • In: Neidhart FC, Curtiss RI, Ingraham J, Lin E, Brooks Low K, editors. Escherichia coli Salmonella typhimurium: cellular and molecular biology. Washington DC: ASM Press
    • Henaut A, Danchin A. Analysis and predictions from Escherichia coli sequences. In: Neidhart FC, Curtiss RI, Ingraham J, Lin E, Brooks Low K, editors. Escherichia coli Salmonella typhimurium: cellular and molecular biology. Washington DC: ASM Press; 1996. p. 2047.
    • (1996) , pp. 2047
    • Henaut, A.1    Danchin, A.2
  • 6
    • 0242298579 scopus 로고    scopus 로고
    • The effective number of codons for individual amino acids: some codons are more optimal than others
    • Fuglsang A. The effective number of codons for individual amino acids: some codons are more optimal than others. Gene. 2003;320:185-90.
    • (2003) Gene , vol.320 , pp. 185-190
    • Fuglsang, A.1
  • 8
    • 84905263603 scopus 로고    scopus 로고
    • High throughput quantitative expression screening and purification applied to recombinant disulfide-rich venom proteins produced in E. coli
    • Saez NJ, Nozach H, Blemont M, Vincentelli R. High throughput quantitative expression screening and purification applied to recombinant disulfide-rich venom proteins produced in E. coli. J Vis Exp. 2014;(89):e51464.
    • (2014) J Vis Exp , Issue.89
    • Saez, N.J.1    Nozach, H.2    Blemont, M.3    Vincentelli, R.4
  • 9
    • 84934435566 scopus 로고    scopus 로고
    • High-throughput expression screening and purification of recombinant proteins in E. coli
    • Saez NJ, Vincentelli R. High-throughput expression screening and purification of recombinant proteins in E. coli. Methods Mol Biol. 2014;1091:33-53.
    • (2014) Methods Mol Biol , vol.1091 , pp. 33-53
    • Saez, N.J.1    Vincentelli, R.2
  • 11
    • 84876734643 scopus 로고    scopus 로고
    • High throughput screening identifies disulfide isomerase DsbC as a very efficient partner for recombinant expression of small disulfide-rich proteins in E. coli
    • Nozach H, Fruchart-Gaillard C, Fenaille F, Beau F, Ramos OHP, Douzi B, et al. High throughput screening identifies disulfide isomerase DsbC as a very efficient partner for recombinant expression of small disulfide-rich proteins in E. coli. Microb Cell Fact. 2013;12:37.
    • (2013) Microb Cell Fact , vol.12 , pp. 37
    • Nozach, H.1    Fruchart-Gaillard, C.2    Fenaille, F.3    Beau, F.4    Ramos, O.H.P.5    Douzi, B.6
  • 12
    • 84897604263 scopus 로고    scopus 로고
    • Fusion tags for protein solubility, purification and immunogenicity in Escherichia coli: the novel Fh8 system
    • Costa SJ, Almeida A, Castro A, Domingues L. Fusion tags for protein solubility, purification and immunogenicity in Escherichia coli: the novel Fh8 system. Front Microbiol. 2014;5:63.
    • (2014) Front Microbiol. , vol.5 , pp. 63
    • Costa, S.J.1    Almeida, A.2    Castro, A.3    Domingues, L.4
  • 13
    • 0028329918 scopus 로고
    • Release of proteins and peptides from fusion proteins using a recombinant plant virus proteinase
    • Parks TD, Leuther KK, Howard ED, Johnston SA, Dougherty WG. Release of proteins and peptides from fusion proteins using a recombinant plant virus proteinase. Anal Biochem. 1994;216:413-7.
    • (1994) Anal Biochem , vol.216 , pp. 413-417
    • Parks, T.D.1    Leuther, K.K.2    Howard, E.D.3    Johnston, S.A.4    Dougherty, W.G.5
  • 14
    • 0024004266 scopus 로고
    • Biochemical and mutational analysis of a plant virus polyprotein cleavage site
    • Dougherty WG, Carrington JC, Cary SM, Parks TD. Biochemical and mutational analysis of a plant virus polyprotein cleavage site. EMBO J. 1988;7:1281-7.
    • (1988) EMBO J , vol.7 , pp. 1281-1287
    • Dougherty, W.G.1    Carrington, J.C.2    Cary, S.M.3    Parks, T.D.4
  • 15
    • 33846396124 scopus 로고    scopus 로고
    • X-ray structure and mutagenesis of the scorpion depressant toxin LqhIT2 reveals key determinants crucial for activity and anti-insect selectivity
    • Karbat I, Turkov M, Cohen L, Kahn R, Gordon D, Gurevitz M, et al. X-ray structure and mutagenesis of the scorpion depressant toxin LqhIT2 reveals key determinants crucial for activity and anti-insect selectivity. J Mol Biol. 2007;366:586-601.
    • (2007) J Mol Biol , vol.366 , pp. 586-601
    • Karbat, I.1    Turkov, M.2    Cohen, L.3    Kahn, R.4    Gordon, D.5    Gurevitz, M.6
  • 17
    • 42149130929 scopus 로고    scopus 로고
    • Chemical gene synthesis: strategies, softwares, error corrections, and applications
    • Xiong A-S, Peng R-H, Zhuang J, Gao F, Li Y, Cheng Z-M, et al. Chemical gene synthesis: strategies, softwares, error corrections, and applications. FEMS Microbiol Rev. 2008;32:522-40.
    • (2008) FEMS Microbiol Rev , vol.32 , pp. 522-540
    • Xiong, A.-S.1    Peng, R.-H.2    Zhuang, J.3    Gao, F.4    Li, Y.5    Cheng, Z.-M.6
  • 18
    • 0033676098 scopus 로고    scopus 로고
    • DNA cloning using in vitro site-specific recombination
    • Hartley JL, Temple GF, Brasch MA. DNA cloning using in vitro site-specific recombination. Genome Res. 2000;10:1788-95.
    • (2000) Genome Res , vol.10 , pp. 1788-1795
    • Hartley, J.L.1    Temple, G.F.2    Brasch, M.A.3
  • 19
    • 80053631355 scopus 로고    scopus 로고
    • High-throughput protein expression screening and purification in Escherichia coli
    • Vincentelli R, Cimino A, Geerlof A, Kubo A, Satou Y, Cambillau C. High-throughput protein expression screening and purification in Escherichia coli. Methods. 2011;55:65-72.
    • (2011) Methods , vol.55 , pp. 65-72
    • Vincentelli, R.1    Cimino, A.2    Geerlof, A.3    Kubo, A.4    Satou, Y.5    Cambillau, C.6
  • 20
    • 14844294424 scopus 로고    scopus 로고
    • Protein production by auto-induction in high density shaking cultures
    • Studier FW. Protein production by auto-induction in high density shaking cultures. Protein Expr Purif. 2005;41:207-34.
    • (2005) Protein Expr Purif , vol.41 , pp. 207-234
    • Studier, F.W.1
  • 21
    • 84877129926 scopus 로고    scopus 로고
    • Production of recombinant disulfide-rich venom peptides for structural and functional analysis via expression in the periplasm of E. coli
    • Klint JK, Senff S, Saez NJ, Seshadri R, Lau HY, Bende NS, et al. Production of recombinant disulfide-rich venom peptides for structural and functional analysis via expression in the periplasm of E. coli. PLoS ONE. 2013;8:e63865.
    • (2013) PLoS ONE , vol.8
    • Klint, J.K.1    Senff, S.2    Saez, N.J.3    Seshadri, R.4    Lau, H.Y.5    Bende, N.S.6
  • 22
    • 84939790347 scopus 로고    scopus 로고
    • Identification and characterization of ProTx-III [μ-TRTX-Tp1a], a new voltage-gated sodium channel inhibitor from venom of the tarantula thrixopelma pruriens
    • Cardoso FC, Dekan Z, Rosengren KJ, Erickson A, Vetter I, Deuis JR, et al. Identification and characterization of ProTx-III [μ-TRTX-Tp1a], a new voltage-gated sodium channel inhibitor from venom of the tarantula thrixopelma pruriens. Mol Pharmacol. 2015;88:291-303.
    • (2015) Mol Pharmacol , vol.88 , pp. 291-303
    • Cardoso, F.C.1    Dekan, Z.2    Rosengren, K.J.3    Erickson, A.4    Vetter, I.5    Deuis, J.R.6
  • 23
    • 84864381348 scopus 로고    scopus 로고
    • Functional expression in Escherichia coli of the disulfide-rich sea anemone peptide APETx2, a potent blocker of acid-sensing ion channel 3
    • Anangi R, Rash LD, Mobli M, King GF. Functional expression in Escherichia coli of the disulfide-rich sea anemone peptide APETx2, a potent blocker of acid-sensing ion channel 3. Mar Drugs. 2012;10:1605-18.
    • (2012) Mar Drugs. , vol.10 , pp. 1605-1618
    • Anangi, R.1    Rash, L.D.2    Mobli, M.3    King, G.F.4
  • 24
    • 84904173537 scopus 로고    scopus 로고
    • A distinct sodium channel voltage-sensor locus determines insect selectivity of the spider toxin Dc1a
    • Bende NS, Dziemborowicz S, Mobli M, Herzig V, Gilchrist J, Wagner J, et al. A distinct sodium channel voltage-sensor locus determines insect selectivity of the spider toxin Dc1a. Nat Commun. 2014;5:4350.
    • (2014) Nat Commun. , vol.5 , pp. 4350
    • Bende, N.S.1    Dziemborowicz, S.2    Mobli, M.3    Herzig, V.4    Gilchrist, J.5    Wagner, J.6
  • 25
    • 84923870269 scopus 로고    scopus 로고
    • The insecticidal spider toxin SFI1 is a knottin peptide that blocks the pore of insect voltage-gated sodium channels via a large b-hairpin loop
    • Bende NS, Dziemborowicz S, Herzig V, Ramanujam V, Brown GW, Bosmans F, et al. The insecticidal spider toxin SFI1 is a knottin peptide that blocks the pore of insect voltage-gated sodium channels via a large b-hairpin loop. FEBS J. 2015;282:904-20.
    • (2015) FEBS J , vol.282 , pp. 904-920
    • Bende, N.S.1    Dziemborowicz, S.2    Herzig, V.3    Ramanujam, V.4    Brown, G.W.5    Bosmans, F.6
  • 26
    • 79959554744 scopus 로고    scopus 로고
    • Functional expression of spider neurotoxic peptide Huwentoxin-I in E. coli
    • Meng E, Cai TF, Li WY, Zhang H, Liu YB, Peng K, et al. Functional expression of spider neurotoxic peptide Huwentoxin-I in E. coli. PLoS ONE. 2011;6:3-8.
    • (2011) PLoS ONE , vol.6 , pp. 3-8
    • Meng, E.1    Cai, T.F.2    Li, W.Y.3    Zhang, H.4    Liu, Y.B.5    Peng, K.6
  • 27
    • 80054777668 scopus 로고    scopus 로고
    • A dynamic pharmacophore drives the interaction between Psalmotoxin-1 and the putative drug target acid-sensing ion channel 1a
    • Saez NJ, Mobli M, Bieri M, Chassagnon IR, Malde AK, Gamsjaeger R, et al. A dynamic pharmacophore drives the interaction between Psalmotoxin-1 and the putative drug target acid-sensing ion channel 1a. Mol Pharmacol. 2011;80:796-808.
    • (2011) Mol Pharmacol , vol.80 , pp. 796-808
    • Saez, N.J.1    Mobli, M.2    Bieri, M.3    Chassagnon, I.R.4    Malde, A.K.5    Gamsjaeger, R.6
  • 28
    • 84886426830 scopus 로고    scopus 로고
    • Discovery of a selective NaV1.7 inhibitor from centipede venom with analgesic efficacy exceeding morphine in rodent pain models
    • Yang S, Xiao Y, Kang D, Liu J, Li Y, Undheim E, et al. Discovery of a selective NaV1.7 inhibitor from centipede venom with analgesic efficacy exceeding morphine in rodent pain models. Proc Natl Acad Sci USA. 2013;110:17534-9.
    • (2013) Proc Natl Acad Sci USA , vol.110 , pp. 17534-17539
    • Yang, S.1    Xiao, Y.2    Kang, D.3    Liu, J.4    Li, Y.5    Undheim, E.6
  • 29
    • 30944459888 scopus 로고    scopus 로고
    • Improved solubility of TEV protease by directed evolution
    • Van Den Berg S, Löfdahl PÅ, Härd T, Berglund H. Improved solubility of TEV protease by directed evolution. J Biotechnol. 2006;121:291-8.
    • (2006) J Biotechnol , vol.121 , pp. 291-298
    • Berg, S.1    Löfdahl, P.2    Härd, T.3    Berglund, H.4
  • 32
    • 0028907619 scopus 로고
    • Gratuitous overexpression of genes in Escherichia coli leads to growth inhibition and ribosome destruction
    • Dong H, Nilsson L, Kurland CG. Gratuitous overexpression of genes in Escherichia coli leads to growth inhibition and ribosome destruction. J Bacteriol. 1995;177:1497-504.
    • (1995) J Bacteriol , vol.177 , pp. 1497-1504
    • Dong, H.1    Nilsson, L.2    Kurland, C.G.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.