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三结构域Cry毒素的体内结晶

In Vivo Crystallization of Three-Domain Cry Toxins.

作者信息

Adalat Rooma, Saleem Faiza, Crickmore Neil, Naz Shagufta, Shakoori Abdul Rauf

机构信息

Department of Biotechnology, Lahore College for Women University, Lahore 54590, Pakistan.

School of Life Sciences, University of Sussex, Falmer, Brighton BN1 9RH, UK.

出版信息

Toxins (Basel). 2017 Mar 9;9(3):80. doi: 10.3390/toxins9030080.

Abstract

(Bt) is the most successful, environmentally-friendly, and intensively studied microbial insecticide. The major characteristic of Bt is the production of proteinaceous crystals containing toxins with specific activity against many pests including dipteran, lepidopteran, and coleopteran insects, as well as nematodes, protozoa, flukes, and mites. These crystals allow large quantities of the protein toxins to remain stable in the environment until ingested by a susceptible host. It has been previously established that 135 kDa Cry proteins have a crystallization domain at their C-terminal end. In the absence of this domain, Cry proteins often need helper proteins or other factors for crystallization. In this review, we classify the Cry proteins based on their requirements for crystallization.

摘要

苏云金芽孢杆菌(Bt)是最成功、对环境友好且研究深入的微生物杀虫剂。Bt的主要特征是产生含毒素的蛋白质晶体,这些毒素对包括双翅目、鳞翅目和鞘翅目昆虫以及线虫、原生动物、吸虫和螨虫在内的许多害虫具有特定活性。这些晶体使大量蛋白质毒素在环境中保持稳定,直至被易感宿主摄取。先前已经确定,135 kDa的Cry蛋白在其C末端有一个结晶结构域。在没有该结构域的情况下,Cry蛋白通常需要辅助蛋白或其他因子来进行结晶。在本综述中,我们根据Cry蛋白结晶所需条件对其进行分类。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/9b9a/5371835/9b265b57a0ce/toxins-09-00080-g001.jpg

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