A cadherin‐like protein influences B acillus thuringiensis   Cry 1 Ab toxicity in the oriental armyworm, M ythimna separata

Cadherins comprise a family of calcium‐dependent cell adhesion proteins that act in cell–cell interactions. Cadherin‐like proteins ( CADs ) in midguts of some insects act as receptors that bind some of the toxins produced by the B acillus thuringiensis ( Bt ). We cloned a CAD gene associated with la...

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Veröffentlicht in:Environmental microbiology reports 2013-06, Vol.5 (3), p.438-443
Hauptverfasser: Wang, Ling, Jiang, Xingfu, Luo, Lizhi, Stanley, David, Sappington, Thomas W., Zhang, Lei
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Sprache:eng
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Zusammenfassung:Cadherins comprise a family of calcium‐dependent cell adhesion proteins that act in cell–cell interactions. Cadherin‐like proteins ( CADs ) in midguts of some insects act as receptors that bind some of the toxins produced by the B acillus thuringiensis ( Bt ). We cloned a CAD gene associated with larval midguts prepared from M ythimna separata . The full‐length cDNA ( MsCAD1 , G en B ank Accession No. JF 951432) is 5642 bp, with an open reading frame encoding a 1757 amino acid and characteristics typical of insect CADs . Expression of MsCAD1 is predominantly in midgut tissue, with highest expression in the 3rd‐ to 6th‐instars and lowest in newly hatched larvae. Knocking‐down MsCAD1 decreased Cry 1 Ab susceptibility, indicated by reduced developmental time, increased larval weight and reduced larval mortality. We expressed MsCAD1 in E . coli and recovered the recombinant protein, rMsCAD 1, which binds Cry 1 Ab toxin. Truncation analysis and binding experiments revealed that a contiguous 209‐aa, located in CR 11 and CR 12, is the minimal Cry 1 Ab binding region. These results demonstrate that MsCAD 1 is associated with Cry 1 Ab toxicity and is one of the Cry 1 Ab receptors in this insect. The significance of this work lies in identifying MsCAD 1 as a Cry 1 Ab receptor, which helps understand the mechanism of Cry 1 Ab toxicity and of potential resistance to Bt in M . separata .
ISSN:1758-2229
1758-2229
DOI:10.1111/1758-2229.12036