Expression in
 Escherichia coli
 of the Native
 cyt1Aa
 from
 Bacillus thuringiensis
 subsp.
 israelensis

Sazhenskiy, Vladislav; Zaritsky, Arieh; Itsko, Mark

doi:10.1128/aem.03068-09

Cited by 8 publications

(8 citation statements)

References 19 publications

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“…This protein may be involved in post-translational processing (e.g., it may protect the nascent polypeptide from proteolysis by binding with it and allowing crystal formation) [46]. Moreover, p20 is known to increase the expression levels of other toxins such as Cyt1Aa, Cry1Ab, Cry1Ac, Cry2A, Cry3A, and truncated Cry1C proteins [34,50,51,52,53,54]. …”

Section: Other Known Crystallization Factorsmentioning

confidence: 99%

In Vivo Crystallization of Three-Domain Cry Toxins

Adalat

Saleem

Crickmore

et al. 2017

Toxins

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Bacillus thuringiensis (Bt) is the most successful, environmentally-friendly, and intensively studied microbial insecticide. The major characteristic of Bt is the production of proteinaceous crystals containing toxins with specific activity against many pests including dipteran, lepidopteran, and coleopteran insects, as well as nematodes, protozoa, flukes, and mites. These crystals allow large quantities of the protein toxins to remain stable in the environment until ingested by a susceptible host. It has been previously established that 135 kDa Cry proteins have a crystallization domain at their C-terminal end. In the absence of this domain, Cry proteins often need helper proteins or other factors for crystallization. In this review, we classify the Cry proteins based on their requirements for crystallization.

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Section: Other Known Crystallization Factorsmentioning

confidence: 99%

In Vivo Crystallization of Three-Domain Cry Toxins

Adalat

Saleem

Crickmore

et al. 2017

Toxins

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“…Previous studies reported that the P20 helper protein is required for efficient expression of Cyt1Aa and other Cry toxins (Wu and Federici, 1993; Sazhenskiy et al ., 2010). As in this work we are interested in expressing different combinations of genes and in studying the interaction among different toxins of Bti, the p20 gene was maintained in the construct.…”

Section: Resultsmentioning

confidence: 99%

“…As the 20‐kDa helper protein was previously reported to be required for efficient expression of Cyt1Aa (Wu and Federici, 1993; Sazhenskiy et al ., 2010) and other Cry toxins (Shao et al ., 2001; Diaz‐Mendoza et al ., 2012; Elleuch et al ., 2015), the cry11Aa‐p20 construct was retained for further experiments.…”

Section: Discussionmentioning

confidence: 99%

Bacillus subtilis as a host for mosquitocidal toxins production

Ursino

Albertini

Fiorentino

et al. 2020

Microbial Biotechnology

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Aedes albopictus transmits several arboviral infections. In the absence of vaccines, control of mosquito populations is the only strategy to prevent vector-borne diseases. As part of the search for novel, biological and environmentally friendly strategies for vector control, the isolation of new bacterial species with mosquitocidal activity represents a promising approach. However, new bacterial isolates may be difficult to grow and genetically manipulate. To overcome these limits, here we set up a system allowing the expression of mosquitocidal bacterial toxins in the well-known genetic background of Bacillus subtilis. As a proof of this concept, the ability of B. subtilis to express individual or combinations of toxins of Bacillus thuringiensis israelensis (Bti) was studied. Different expression systems in which toxin gene expression was driven by IPTG-inducible, auto-inducible or toxin gene-specific promoters were developed. The larvicidal activity of the resulting B. subtilis strains against second-instar Ae. albopictus larvae allowed studying the activity of individual toxins or the synergistic interaction among Cry and Cyt toxins. The expression systems here presented lay the foundation for a better improved system to be used in the future to characterize the larvicidal activity of toxin genes from new environmental isolates.

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“…Thus, the P20 appears to act as a chaperone to partially protect the host from the deleterious effects of Cyt1Aa, and although Cyt1Aa interacts with elements of the heat shock regulon, over-expression of groEL or groES does not substitute. A recent report has indicated that insecticidally active Cyt1Aa alone can be produced in E. coli using a tightly regulated promoter; however, there is still a dramatic reduction of cell viability upon induction (Sazhenskiy et al 2010). Interestingly, other structurally similar proteins can be well expressed in E. coli (Cohen et al 2008;Li et al 1996), suggesting, as expected, that sequence-specific protein interactions account for the Cyt1Aa expression defect.…”

Section: Pesticidal Protein Expression In Gram Negative Hostsmentioning

confidence: 86%

Bacillus thuringiensis Recombinant Insecticidal Protein Production

Schnepf

2012

Bacillus Thuringiensis Biotechnology

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The initial excitement of applying recombinant DNA technology to insecticidal proteins of Bacillus thuringiensis was subdued by regulatory caution about the technology and the genetic complexity of the proteins themselves. While seven biopesticide products containing recombinant proteins were eventually manufactured, expression of the proteins in Gram negative and Gram positive bacteria is predominantly for discovery and mode of action work. Regulatory studies for the registration of transgenic plants requires microbially produced insecticidal proteins in the tens of grams. Transgenic plants now dominate the production of B. thuringiensis recombinant insecticidal proteins, with expression technology yielding more than 10-fold higher levels than the earliest registered plants and worldwide use on nearly 60 million hectares.

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Expression in Escherichia coli of the Native cyt1Aa from Bacillus thuringiensis subsp. israelensis

Cited by 8 publications

References 19 publications

In Vivo Crystallization of Three-Domain Cry Toxins

In Vivo Crystallization of Three-Domain Cry Toxins

Bacillus subtilis as a host for mosquitocidal toxins production

Bacillus thuringiensis Recombinant Insecticidal Protein Production

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