Exogenous peptide replacement of three loops in domain II of Cry1Ab toxin reduces its toxicity against Helicoverpa armigera (Lepidoptera: Noctuidae)

Result code in IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60077344%3A_____%2F19%3A00503978" target="_blank" >RIV/60077344:_____/19:00503978 - isvavai.cz</a>

Result on the web

<a href="https://bioone.org/journals/african-entomology/volume-27/issue-1/003.027.0066/Exogenous-Peptide-Replacement-of-Three-Loops-in-Domain-II-of/10.4001/003.027.0066.full" target="_blank" >https://bioone.org/journals/african-entomology/volume-27/issue-1/003.027.0066/Exogenous-Peptide-Replacement-of-Three-Loops-in-Domain-II-of/10.4001/003.027.0066.full</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.4001/003.027.0066" target="_blank" >10.4001/003.027.0066</a>

Result language

angličtina

Original language name

Exogenous peptide replacement of three loops in domain II of Cry1Ab toxin reduces its toxicity against Helicoverpa armigera (Lepidoptera: Noctuidae)

Original language description

To investigate the contribution of surface-exposed loops (loops 1, 2 and 3) in the toxicity of Cry1Ab against Helicoverpa armigera larvae, three loop-replaced Cry1Ab mutants were prokaryotically expressed in Escherichia coli BL21 (DE3). Proteolytic processing of Cry1Ab toxins with trypsin indicated that the replacement of each surface-exposed loop caused no damage to toxin stability. Results of in vitro binding and competition assay indicated that, similarly to the native Cry1Ab toxin, the mutants retained almost the same binding affinity and specificity with brush border membrane vesicles (BBMV) of H. armigera. Nevertheless, H. armigera larvae fed with each loop-replaced Cry1Ab mutant showed less growth inhibition in comparison with those fed with native Cry1Ab toxin. The most significant decrease in toxicity was observed from larvae fed with loop 2-replaced Cry1Ab mutant, with a c. 12-fold increase in the weight of tested larvae relative to that of larvae fed native Cry1Ab toxin. The results demonstrate that the replacement of three surface-exposed loops located in domain II of Cry1Ab toxin may result in a certain reduction in the toxicity. Relative to loop 1 and loop 3, loop 2 seem to play a more important role in generating toxicity of Cry1Ab against H. armigera larvae.

Czech name

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Czech description

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Type

J_imp - Article in a specialist periodical, which is included in the Web of Science database

CEP classification

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OECD FORD branch

40106 - Agronomy, plant breeding and plant protection; (Agricultural biotechnology to be 4.4)

Project

—

Continuities

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Publication year

2019

Confidentiality

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Name of the periodical

African Entomology

ISSN

1021-3589

e-ISSN

—

Volume of the periodical

27

Issue of the periodical within the volume

1

Country of publishing house

ZA - SOUTH AFRICA

Number of pages

9

Pages from-to

66-74

UT code for WoS article

000465610200009

EID of the result in the Scopus database

2-s2.0-85064949942