Fabrick Jeff, Oppert Cris, Lorenzen Marcé D, Morris Kaley, Oppert Brenda, Jurat-Fuentes Juan Luis
United States Department of Agriculture Agricultural Research Service United States Arid-Land Agricultural Research Center, Maricopa, Arizona 85238, USA.
J Biol Chem. 2009 Jul 3;284(27):18401-10. doi: 10.1074/jbc.M109.001651. Epub 2009 May 5.
Cry toxins produced by the bacterium Bacillus thuringiensis are effective biological insecticides. Cadherin-like proteins have been reported as functional Cry1A toxin receptors in Lepidoptera. Here we present data that demonstrate that a coleopteran cadherin is a functional Cry3Aa toxin receptor. The Cry3Aa receptor cadherin was cloned from Tenebrio molitor larval midgut mRNA, and the predicted protein, TmCad1, has domain structure and a putative toxin binding region similar to those in lepidopteran cadherin B. thuringiensis receptors. A peptide containing the putative toxin binding region from TmCad1 bound specifically to Cry3Aa and promoted the formation of Cry3Aa toxin oligomers, proposed to be mediators of toxicity in lepidopterans. Injection of TmCad1-specific double-stranded RNA into T. molitor larvae resulted in knockdown of the TmCad1 transcript and conferred resistance to Cry3Aa toxicity. These data demonstrate the functional role of TmCad1 as a Cry3Aa receptor in T. molitor and reveal similarities between the mode of action of Cry toxins in Lepidoptera and Coleoptera.
苏云金芽孢杆菌产生的晶体毒素是有效的生物杀虫剂。据报道,类钙黏蛋白是鳞翅目昆虫中功能性Cry1A毒素的受体。在此,我们提供的数据表明,一种鞘翅目钙黏蛋白是功能性Cry3Aa毒素受体。从黄粉虫幼虫中肠mRNA克隆出Cry3Aa受体钙黏蛋白,预测的蛋白TmCad1具有与鳞翅目苏云金芽孢杆菌受体钙黏蛋白相似的结构域结构和假定的毒素结合区域。含有来自TmCad1假定毒素结合区域的肽特异性结合Cry3Aa,并促进Cry3Aa毒素寡聚体的形成,而毒素寡聚体被认为是鳞翅目昆虫中毒性的介质。向黄粉虫幼虫注射TmCad1特异性双链RNA导致TmCad1转录本的敲低,并赋予对Cry3Aa毒性的抗性。这些数据证明了TmCad1作为黄粉虫中Cry3Aa受体的功能作用,并揭示了鳞翅目和鞘翅目昆虫中Cry毒素作用模式的相似性。