Potency of the mosquitocidal Cry46Ab toxin produced using a 4AaCter-tag, which facilitates formation of protein inclusion bodies in Escherichia coli
Author:
Funder
Japan Society for the Promotion of Science
Publisher
Springer Science and Business Media LLC
Subject
Insect Science
Link
http://link.springer.com/article/10.1007/s13355-017-0529-5/fulltext.html
Reference19 articles.
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2. Akiba T, Abe Y, Kitada S, Kusaka Y, Ito A, Ichimatsu T, Katayama H, Akao T, Higuchi K, Mizuki E, Ohba M, Kanai R, Harata K (2009) Crystal structure of the parasporin-2 Bacillus thuringiensis toxin that recognizes cancer cells. J Mol Biol 386:121–133. https://doi.org/10.1016/j.jmb.2008.12.002
3. Aronson AI, Han ES, McGaughey W, Johnson D (1991) The solubility of inclusion proteins from Bacillus thuringiensis is dependent upon protoxin composition and is a factor in toxicity to insects. Appl Environ Microbiol 57:981–986
4. Bietlot HP, Vishnubhatla I, Carey PR, Pozsgay M, Kaplan H (1990) Characterization of the cysteine residues and disulphide linkages in the protein crystal of Bacillus thuringiensis. Biochem J 267:309–315
5. Chak KF, Ellar DJ (1987) Cloning and expression in Escherichia coli of an insecticidal crystal protein gene from Bacillus thuringiensis var. aizawai HD-133. J Gen Microbiol 133:2921–2931. https://doi.org/10.1099/00221287-133-10-2921
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1. Downstream processing of Cry4AaCter-induced inclusion bodies containing insect-derived antimicrobial peptides produced in Escherichia coli;Protein Expression and Purification;2019-03
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