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首页> 外文期刊>Protein Expression and Purification >Escherichia coli expression and purification of four antimicrobial peptides fused to a family 3 carbohydrate-binding module (CBM) from Clostridium thermocellum
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Escherichia coli expression and purification of four antimicrobial peptides fused to a family 3 carbohydrate-binding module (CBM) from Clostridium thermocellum

机译：大肠杆菌表达和纯化与热纤梭菌第3族碳水化合物结合模块（CBM）融合的四种抗菌肽

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Antimicrobial Peptides (AMPs) are molecules that act in a wide range of physiological defensive mechanisms developed to counteract bacteria, fungi, parasites and viruses. Several hundreds of AMPs have been identified and characterized. These molecules are presently gaining increasing importance, as a consequence of their remarkable resistance to microorganism adaptation. Carbohydrate-binding modules (CBMs) are non-catalytic domains that anchor glycoside hydrolases into complex carbohydrates. Clostridium thermocellum produces a multi-enzyme complex of cellulases and hemicellulases, termed the cellulosome, which is organized by the scaffoldin protein CipA. Binding of the cellulosome to the plant cell wall results from the action of CipA family 3 CBM (CBM3), which presents a high affinity for crystalline cellulose. Here CipA family 3 CBM was fused to four different AMPs using recombinant DNA technology and the fusion recombinant proteins were expressed at high levels in Escherichia coli cells. CBM3 does not present antibacterial activity and does not bind to the bacterial surface. However, the four recombinant proteins retained the ability to bind cellulose, suggesting that CBM3 is a good candidate polypeptide to direct the binding of AMPs into cellulosic supports. A comprehensive characterization of the antimicrobial activity of the recombinant fusion proteins is currently under evaluation. (C) 2008 Elsevier Inc. All rights reserved.
机译：抗菌肽（AMP）是在广泛的生理防御机制中起作用的分子，这些机制可以抵抗细菌，真菌，寄生虫和病毒。已经鉴定并表征了数百个AMP。由于它们对微生物适应的显着抗性，这些分子目前正变得越来越重要。碳水化合物结合模块（CBM）是将糖苷水解酶固定在复杂碳水化合物中的非催化域。热纤梭菌产生纤维素酶和半纤维素酶的多酶复合物，称为纤维素体，由支架蛋白CipA组成。纤维素体与植物细胞壁的结合是由于CipA家族3 CBM（CBM3）的作用而产生的，它对结晶纤维素具有很高的亲和力。在这里，使用重组DNA技术将CipA家族3的CBM与四种不同的AMPs融合，融合的重组蛋白在大肠杆菌细胞中高水平表达。 CBM3不具有抗菌活性，也不与细菌表面结合。但是，这四个重组蛋白保留了结合纤维素的能力，这表明CBM3是将AMPs结合到纤维素支持物中的良好候选多肽。目前正在评估重组融合蛋白的抗菌活性的全面表征。 （C）2008 Elsevier Inc.保留所有权利。

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