Cry11Aa toxin from <i>Bacillus thuringiensis</i> binds its receptor in <i>Aedes aegypti</i> mosquito larvae through loop α‐8 of domain II

Fernández, Luisa Elena; Pérez, Cirilo; Segovia, Lorenzo; Rodrı́guez, Mario H.; Gill, Sarjeet S.; Bravo, Alejandra; Soberón, Mário

doi:10.1016/j.febslet.2005.05.032

Cited by 65 publications

(97 citation statements)

References 35 publications

(48 reference statements)

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“…These regions corresponded to the microvilli membrane from the caeca and from the posterior part of the midgut indicating that ALP colocalizes with the binding sites of Cry11Aa [7]. Our results identify domain II loop α-8 as a key determinant for the binding of Cry11Aa toxin to GPIanchored ALP [6,7] (Fig. 4).…”

Section: Random Peptide Library-identification Of An Alp Receptor Andsupporting

confidence: 51%

“…We demonstrated that the putative exposed loop α-8 of Cry11Aa toxin, located in domain II, is an important epitope involved in receptor interaction and toxicity. Four exposed loops and three putative exposed regions in domain II of Cry11A were predicted by modeling the threedimensional structure of the mosquitocidal Cry11Aa toxin [6]. Synthetic peptides corresponding to these regions were used in heterologous binding competition assays of Cry11Aa to Ae aegypti BBMV.…”

Section: Random Peptide Library-identification Of An Alp Receptor Andmentioning

confidence: 99%

“…Synthetic peptides corresponding to these regions were used in heterologous binding competition assays of Cry11Aa to Ae aegypti BBMV. We identified three regions of Cry11A toxin, corresponding to loop α-8, β4 and loop 3 that are involved in binding of this toxin to the BBMV [6]. We isolated peptide-displaying phages that bind to Cry11Aa toxin (P5.tox) or to Ae.…”

Section: Random Peptide Library-identification Of An Alp Receptor Andmentioning

confidence: 99%

“…We isolated peptide-displaying phages that bind to Cry11Aa toxin (P5.tox) or to Ae. aegypti BBMV (P1.BBMV) [6,7]. These phages interfered with the interaction of the toxin with the BBMV and attenuated the toxicity of Cry11Aa in bioassays [6,7].…”

Section: Random Peptide Library-identification Of An Alp Receptor Andmentioning

confidence: 99%

“…aegypti BBMV (P1.BBMV) [6,7]. These phages interfered with the interaction of the toxin with the BBMV and attenuated the toxicity of Cry11Aa in bioassays [6,7]. The binding of both phages was competed by loop α-8 synthetic peptide, suggesting that phage P5.tox binds the toxin by interacting with loop α-8 while P1.BBMV interacts with the receptor by using an epitope similar to this region [6,7].…”

Section: Random Peptide Library-identification Of An Alp Receptor Andmentioning

confidence: 99%

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Employing phage display to study the mode of action of Bacillus thuringiensis Cry toxins

et al. 2008

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Phage display is an in vitro method for selecting polypeptides with desired properties from a large collections of variants. The insecticidal Cry toxins produced by Bacillus thuringiensis are highly specific to different insects. Various proteins such as cadherin, aminopeptidase-N (APN) and alkaline phosphatase (ALP) have been characterized as potential Cry-receptors. We used phage display to characterize the Cry toxin-receptor interaction(s). By employing phage-libraries that display singlechain antibodies (scFv) from humans or from immunized rabbits with Cry1Ab toxin or random 12-residues peptides, we have identified the epitopes that mediate binding of lepidopteran Cry1Ab toxin with cadherin and APN receptors from Manduca sexta and the interaction of dipteran Cry11Aa toxin with the ALP receptor from Aedes aegypti. Finally we displayed in phages the Cry1Ac toxin and discuss the potential for selecting Cry variants with improved toxicity or different specificity.

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Section: Random Peptide Library-identification Of An Alp Receptor Andsupporting

confidence: 51%

Section: Random Peptide Library-identification Of An Alp Receptor Andmentioning

confidence: 99%

Section: Random Peptide Library-identification Of An Alp Receptor Andmentioning

confidence: 99%

Section: Random Peptide Library-identification Of An Alp Receptor Andmentioning

confidence: 99%

Section: Random Peptide Library-identification Of An Alp Receptor Andmentioning

confidence: 99%

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Employing phage display to study the mode of action of Bacillus thuringiensis Cry toxins

et al. 2008

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Enzyme‐linked immunosorbent assay detection and bioactivity of Cry1Ab protein fragments

Albright

Hellmich

Coats

2016

Enviro Toxic and Chemistry

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The continuing use of transgenic crops has led to an increased interest in the fate of insecticidal crystalline (Cry) proteins in the environment. Enzyme-linked immunosorbent assays (ELISAs) have emerged as the preferred detection method for Cry proteins in environmental matrices. Concerns exist that ELISAs are capable of detecting fragments of Cry proteins, which may lead to an overestimation of the concentration of these proteins in the environment. Five model systems were used to generate fragments of the Cry1Ab protein, which were then analyzed by ELISAs and bioassays. Fragments from 4 of the model systems were not detectable by ELISA and did not retain bioactivity. Fragments from the proteinase K model system were detectable by ELISA and retained bioactivity. In most cases, ELISAs appear to provide an accurate estimation of the amount of Cry proteins in the environment, as detectable fragments retained bioactivity and nondetectable fragments did not retain bioactivity. Environ Toxicol Chem 2016;35:3101-3112. © 2016 SETAC.

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Cry11Aa and Cyt1Aa exhibit different structural orders in crystal topography

Chen

Teulon

Pellequer

2023

J of Molecular Recognition

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Cry11Aa and Cyt1Aa are two pesticidal toxins produced by Bacillus thuringiensis subsp. israelensis. To improve our understanding of the nature of their oligomers in the toxic actions and synergistic effects, we performed the atomic force microscopy to probe the surfaces of their natively grown crystals, and used the L‐weight filter to enhance the structural features. By L‐weight filtering, molecular sizes of the Cry11Aa and Cyt1Aa monomers obtained are in excellent agreement with the three‐dimensional structures determined by x‐ray crystallography. Moreover, our results show that the layered feature of a structural element distinguishes the topographic characteristics of Cry11Aa and Cyt1Aa crystals, suggesting that the Cry11Aa toxin has a better chance than Cyt1Aa for multimerization and therefore cooperativeness of the toxic actions.

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Cry11Aa toxin from Bacillus thuringiensis binds its receptor in Aedes aegypti mosquito larvae through loop α‐8 of domain II

Cited by 65 publications

References 35 publications

Employing phage display to study the mode of action of Bacillus thuringiensis Cry toxins

Employing phage display to study the mode of action of Bacillus thuringiensis Cry toxins

Enzyme‐linked immunosorbent assay detection and bioactivity of Cry1Ab protein fragments

Cry11Aa and Cyt1Aa exhibit different structural orders in crystal topography

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