Fragments of Tenebrio molitor cadherin enhance Cry3Aa toxicity for the red flour beetle, Tribolium castaneum (Herbst)
Identifikátory výsledku
Kód výsledku v IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60077344%3A_____%2F16%3A00464839" target="_blank" >RIV/60077344:_____/16:00464839 - isvavai.cz</a>
Výsledek na webu
<a href="http://dx.doi.org/10.1111/jen.12255" target="_blank" >http://dx.doi.org/10.1111/jen.12255</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1111/jen.12255" target="_blank" >10.1111/jen.12255</a>
Alternativní jazyky
Jazyk výsledku
angličtina
Název v původním jazyce
Fragments of Tenebrio molitor cadherin enhance Cry3Aa toxicity for the red flour beetle, Tribolium castaneum (Herbst)
Popis výsledku v původním jazyce
Bacillus thuringiensis crystalline (Cry) proteins are highly toxic to a wide range of insect pests, but some species resist their action. This is true for many economically important beetles, including stored product pests, such as Tribolium castaneum. In this article, we show that the susceptibility of T.castaneum larvae to natural as well as to a recombinant Cry3Aa-type toxin, applied in the diet, is enhanced by supplementing the diet with recombinant fragments of Tenebrio molitor cadherin; Cry toxin-binding sites occur in several cadherin repeats (CR). In our study, we used the toxin-binding region CRtb, which represents a substantial part of the repeat CR12-MPED (membrane-proximal extracellular domain). CRtb and CR12-MPED consistently increased Cry3Aa toxicity. This synergistic effect occured at diverse mass ratios between the toxin and the cadherin fragments, suggesting that optimal ratios can be found. In our 6-week-long assay with T.castaneum, we achieved mortality of up to 96.6% with toxin concentration 30g/g. Cadherin fragments CR11 and CR9-11 elicited small and diverse effects that require further analysis.
Název v anglickém jazyce
Fragments of Tenebrio molitor cadherin enhance Cry3Aa toxicity for the red flour beetle, Tribolium castaneum (Herbst)
Popis výsledku anglicky
Bacillus thuringiensis crystalline (Cry) proteins are highly toxic to a wide range of insect pests, but some species resist their action. This is true for many economically important beetles, including stored product pests, such as Tribolium castaneum. In this article, we show that the susceptibility of T.castaneum larvae to natural as well as to a recombinant Cry3Aa-type toxin, applied in the diet, is enhanced by supplementing the diet with recombinant fragments of Tenebrio molitor cadherin; Cry toxin-binding sites occur in several cadherin repeats (CR). In our study, we used the toxin-binding region CRtb, which represents a substantial part of the repeat CR12-MPED (membrane-proximal extracellular domain). CRtb and CR12-MPED consistently increased Cry3Aa toxicity. This synergistic effect occured at diverse mass ratios between the toxin and the cadherin fragments, suggesting that optimal ratios can be found. In our 6-week-long assay with T.castaneum, we achieved mortality of up to 96.6% with toxin concentration 30g/g. Cadherin fragments CR11 and CR9-11 elicited small and diverse effects that require further analysis.
Klasifikace
Druh
J<sub>x</sub> - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)
CEP obor
EB - Genetika a molekulární biologie
OECD FORD obor
—
Návaznosti výsledku
Projekt
—
Návaznosti
I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace
Ostatní
Rok uplatnění
2016
Kód důvěrnosti údajů
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Údaje specifické pro druh výsledku
Název periodika
Journal of Applied Entomology
ISSN
0931-2048
e-ISSN
—
Svazek periodika
140
Číslo periodika v rámci svazku
4
Stát vydavatele periodika
DE - Spolková republika Německo
Počet stran výsledku
10
Strana od-do
277-286
Kód UT WoS článku
000374494400005
EID výsledku v databázi Scopus
2-s2.0-84937597690