Difference between revisions of "Part:BBa K3686010"
LeiYingJie (Talk | contribs) |
LeiYingJie (Talk | contribs) |
||
Line 10: | Line 10: | ||
[3]Vachon, V., Laprade, R., & Schwartz, J. L. (2012). Current models of the mode of action of Bacillus thuringiensis insecticidal crystal proteins: a critical review. Journal of invertebrate pathology, 111(1), 1-12.<br> | [3]Vachon, V., Laprade, R., & Schwartz, J. L. (2012). Current models of the mode of action of Bacillus thuringiensis insecticidal crystal proteins: a critical review. Journal of invertebrate pathology, 111(1), 1-12.<br> | ||
[4]Melo, A. L. D. A., Soccol, V. T., & Soccol, C. R. (2016). Bacillus thuringiensis: mechanism of action, resistance, and new applications: a review. Critical reviews in biotechnology, 36(2), 317-326<br> | [4]Melo, A. L. D. A., Soccol, V. T., & Soccol, C. R. (2016). Bacillus thuringiensis: mechanism of action, resistance, and new applications: a review. Critical reviews in biotechnology, 36(2), 317-326<br> | ||
+ | ===Source of sequence=== | ||
+ | Genome of Bacillus thuringiensis (BTH-3), full amino acid sequence submitted under GenBank accession no. EF486523. | ||
+ | ===Considerations:=== | ||
+ | Codon-optimized for expression in Escherichia coli. | ||
Revision as of 01:15, 26 October 2020
Insecticidal protein from Bacillus thuringiensis (BTH-3), complete CDs, codon-optimized
Bt toxins refers to the toxic proteins produced by insect pathogenic bacteria Bacillus thuringiensis. Each Bt toxin display unique conformations of peptide chain thus have a specificity to certain invertebrates. Where Cry7Ca1 is a differentiate of Bt toxins with a molecular mass of 129kDa, recently isolated from Bt strain BHT-13. According to the crystalline analysis, it could be inferred that this toxin displays a similar mode of action, the pre-pore forming model, like its relatives [1][2][3]. Which the lethality of this toxin against locusts have been confirmed at an LC50 (50% lethal concentration) value of 8.98 μg/ml [1].
Once ingested by insects, Cry7Ca1 undergoes a series of digestion by protease in insect gut juice. Which cleaves the protective shell and release the core toxin inside. Furthermore, the core toxin binds to the membrane-bonded protease on epithelial cells. The proteolytic degradation removes the N-terminal alpha chain, unreal the core into smaller oligomers that embed onto the cell membrane and result in cell disruption. [4]
[1]Wu, Y., Lei, C. F., Yi, D., Liu, P. M., & Gao, M. Y. (2011). Novel Bacillus thuringiensis δ-endotoxin active against Locusta migratoria manilensis. Applied and environmental microbiology, 77(10), 3227-3233.
[2]Jimenez-Juarez, N., Munoz-Garay, C., Gómez, I., Gill, S. S., Soberón, M., & Bravo, A. (2008). The pre-pore from Bacillus thuringiensis Cry1Ab toxin is necessary to induce insect death in Manduca sexta. Peptides, 29(2), <318-323..
[3]Vachon, V., Laprade, R., & Schwartz, J. L. (2012). Current models of the mode of action of Bacillus thuringiensis insecticidal crystal proteins: a critical review. Journal of invertebrate pathology, 111(1), 1-12.
[4]Melo, A. L. D. A., Soccol, V. T., & Soccol, C. R. (2016). Bacillus thuringiensis: mechanism of action, resistance, and new applications: a review. Critical reviews in biotechnology, 36(2), 317-326
Source of sequence
Genome of Bacillus thuringiensis (BTH-3), full amino acid sequence submitted under GenBank accession no. EF486523.
Considerations:
Codon-optimized for expression in Escherichia coli.
Sequence and Features
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21COMPATIBLE WITH RFC[21]
- 23COMPATIBLE WITH RFC[23]
- 25INCOMPATIBLE WITH RFC[25]Illegal NgoMIV site found at 205
Illegal NgoMIV site found at 220
Illegal NgoMIV site found at 1567
Illegal NgoMIV site found at 1828
Illegal NgoMIV site found at 1990 - 1000COMPATIBLE WITH RFC[1000]