Genetic Engineering of Escherichia coli BL21 (DE3) with a codon-optimized insecticidal toxin complex gene tccZ

References

1. Mahlangu SG, Serepa-Dlamini MH. First report of bacterial endophytes from the leaves of Pellaea calomelanos in South Africa. S Afr J Sci 2018; 114:9–10 [View Article]
   [Google Scholar]
2. South African National Biodiversity Institute (SANBI) Pellaea calomelanos [homepage on the Internet]; 2022Aug30 http://pza.sanbi.org/pellaea-calomelanos
3. Mahlangu SG, Serepa-Dlamini MH. Draft genome sequence of Pantoea ananatis strain MHSD5 isolated from surface sterilized leaves of medicinal plant, Pellaea calomelanos obtained in South Africa. Data Brief 2018; 19:1727–1732 [View Article]
   [Google Scholar]
4. Ullah I, Jang E-K, Kim M-S, Shin J-H, Park G-S et al. Identification and characterization of the insecticidal toxin “makes caterpillars floppy” in Photorhabdus temperata M1021 using a cosmid library. Toxins 2014; 6:2024–2040 [View Article]
   [Google Scholar]
5. RH Bowen DJ. Novel insecticidal toxins from nematode-symbiotic bacteria. Cell Mol Life Sci 2000; 57:828–833 [View Article] [PubMed]
   [Google Scholar]
6. Yang G, Waterfield NR. The role of TcdB and TccC subunits in secretion of the Photorhabdus Tcd toxin complex. PLOS Pathog 2013; 9:e1003644 [View Article]
   [Google Scholar]
7. Chen W-J, Hsieh F-C, Hsu F-C, Tasy Y-F, Liu J-R et al. Characterization of an insecticidal toxin and pathogenicity of Pseudomonas taiwanensis against insects. PLoS Pathog 2014; 10:e1004288 [View Article]
   [Google Scholar]
8. Bowen DJ, Ensign JC. Purification and characterization of a high-molecular-weight insecticidal protein complex produced by the entomopathogenic bacterium Photorhabdus luminescens. Appl Environ Microbiol 1998; 64:3029–3035 [View Article]
   [Google Scholar]
9. ffrench-Constant RH, Bowen DJ. Novel insecticidal toxins from nematode-symbiotic bacteria. Cell Mol Life Sci 2000; 57:828–833 [View Article] [PubMed]
   [Google Scholar]
10. Wilkinson P, Paszkiewicz K, Moorhouse A, Szubert JM, Beatson S et al. New plasmids and putative virulence factors from the draft genome of an Australian clinical isolate of Photorhabdus asymbiotica. FEMS Microbiol Lett 2010; 309:136–143 [View Article] [PubMed]
    [Google Scholar]
11. Rangel LI, Henkels MD, Shaffer BT, Walker FL, Davis EW et al. Characterization of toxin complex gene clusters and insect toxicity of bacteria representing four subgroups of Pseudomonas fluorescens. PLoS One 2016; 11:e0161120 [View Article]
    [Google Scholar]
12. ffrench-Constant R, Waterfield N, Daborn P, Joyce S, Bennett H et al. Photorhabdus: towards a functional genomic analysis of a symbiont and pathogen. FEMS Microbiol Rev 2003; 26:433–456 [View Article] [PubMed]
    [Google Scholar]
13. Sergeant M, Jarrett P, Ousley M, Morgan JAW. Interactions of insecticidal toxin gene products from Xenorhabdus nematophilus PMFI296. Appl Environ Microbiol 2003; 69:3344–3349 [View Article] [PubMed]
    [Google Scholar]
14. Lang AE, Schmidt G, Schlosser A, Hey TD, Larrinua IM et al. Photorhabdus luminescens toxins ADP-ribosylate actin and RhoA to force actin clustering. Science 2010; 327:1139–1142 [View Article] [PubMed]
    [Google Scholar]
15. Kaviyapriya M, Balakrishnan N, Ramalakshmi A, Lone R. Cloning and characterization of insecticidal cry/vip genes from an indigenous Bacillus thuringiensis isolate T29 and evaluation of its toxicity to maize fall armyworm Spodoptera frugiperda. J Entomol Zool Stud 2019; 7:1314–1321
    [Google Scholar]
16. Feitelson JS, Payne J, Kim L. Bacillus thuringiensis: Insects and Beyond. Nat Biotechnol 1992; 10:271–275 [View Article]
    [Google Scholar]
17. Landsberg MJ, Jones SA, Rothnagel R, Busby JN, Marshall SDG et al. 3D structure of the Yersinia entomophaga toxin complex and implications for insecticidal activity. Proc Natl Acad Sci 2011; 108:20544–20549 [View Article]
    [Google Scholar]
18. Zhao R, Han R, Qiu X, Yan X, Cao L et al. Cloning and heterologous expression of insecticidal-protein-encoding genes from Photorhabdus luminescens TT01 in Enterobacter cloacae for termite control. Appl Environ Microbiol 2008; 74:7219–7226 [View Article]
    [Google Scholar]
19. Gatsogiannis C, Merino F, Roderer D, Balchin D, Schubert E et al. Tc toxin activation requires unfolding and refolding of a β-propeller. Nature 2018; 563:209–213 [View Article] [PubMed]
    [Google Scholar]
20. Claassens NJ, Siliakus MF, Spaans SK, Creutzburg SCA, Nijsse B et al. Improving heterologous membrane protein production in Escherichia coli by combining transcriptional tuning and codon usage algorithms. PLoS One 2017; 12:e0184355 [View Article]
    [Google Scholar]
21. Bradford MM. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 1976; 72:248–254 [View Article] [PubMed]
    [Google Scholar]
22. Wong C, Sridhara S, Bardwell JCA, Jakob U. Heating greatly speeds Coomassie blue staining and destaining. Biotechniques 2000; 28:426–428 [View Article] [PubMed]
    [Google Scholar]
23. Mossessova E, Lima CD. Ulp1-SUMO crystal structure and genetic analysis reveal conserved interactions and a regulatory element essential for cell growth in yeast. Mol Cell 2000; 5:865–876 [View Article] [PubMed]
    [Google Scholar]
24. Walls D, Loughran ST. Tagging recombinant proteins to enhance solubility and aid purification. Methods Mol Biol 2011; 681:151–175 [View Article]
    [Google Scholar]
25. Dyballa N, Metzger S. Fast and sensitive colloidal coomassie G-250 staining for proteins in polyacrylamide gels. J Vis Exp 200930 [View Article]
    [Google Scholar]
26. Novagen BugBusterTM Protein Extraction Reagent 2008
    [Google Scholar]
27. Malakhov MP, Mattern MR, Malakhova OA, Drinker M, Weeks SD et al. SUMO fusions and SUMO-specific protease for efficient expression and purification of proteins. J Struct Funct Genomics 2004; 5:75–86 [View Article]
    [Google Scholar]
28. Butt TR, Edavettal SC, Hall JP, Mattern MR. SUMO fusion technology for difficult-to-express proteins. Protein Expr Purif 2005; 43:1–9 [View Article]
    [Google Scholar]
29. Duong-Ly KC, Gabelli SB. Explanatory chapter: troubleshooting recombinant protein expression: general. Meth Enzymol 2014; 541:209–229
    [Google Scholar]
30. Young CL, Britton ZT, Robinson AS. Recombinant protein expression and purification: a comprehensive review of affinity tags and microbial applications. Biotechnol J 2012; 7:620–634 [View Article]
    [Google Scholar]
31. Dumon-Seignovert L, Cariot G, Vuillard L. The toxicity of recombinant proteins in Escherichia coli: a comparison of overexpression in BL21(DE3), C41(DE3), and C43(DE3). Protein Expr Purif 2004; 37:203–206 [View Article]
    [Google Scholar]
32. Ahmad M, Hirz M, Pichler H, Schwab H. Protein expression in Pichia pastoris: recent achievements and perspectives for heterologous protein production. Appl Microbiol Biotechnol 2014; 98:5301–5317 [View Article]
    [Google Scholar]
33. Studier FW. Stable expression clones and auto-induction for protein production in E. coli. Methods Mol Biol 2014; 1091:17–32 [View Article] [PubMed]
    [Google Scholar]
34. Jahic M, Veide A, Charoenrat T, Teeri T, Enfors S-O. Process technology for production and recovery of heterologous proteins with Pichia pastoris. Biotechnol Prog 2006; 22:1465–1473 [View Article] [PubMed]
    [Google Scholar]