Targeting the gram-negative bacteria peptidoglycan synthase MraY as a new approach for monoclonal antibody anti-bacterial activity
Targeting the gram-negative bacteria peptidoglycan synthase MraY as a new approach for monoclonal antibody anti-bacterial activity
复制标题
靶向革兰氏阴性菌肽聚糖合酶MraY作为单克隆抗体抗菌活性的新方法
DOI：
10.1080/21645515.2017.1337613
复制
发表时间：
2017-01-01
影响因子：
4.8
通讯作者：
Yu, Shenye
中科院分区：
文献类型：
--
作者：
Cao, Jun;Yi, Fei;Yu, Shenye
使用抗生素靶向细菌是控制动物和人类感染的有效方法。肽聚糖的生物合成是细菌中的一个重要过程，保守的肽聚糖合成酶MraY是一个有吸引力的药物设计靶点。然而，由于缺乏详细的MraY结构信息，尚未开发出靶向MraY的抗生素。在本研究中，从大肠杆菌MraY的2个亲水区表达为融合蛋白，并用于提高小鼠的单克隆抗体。我们证实了MraY氨基酸序列PESFSKRGTPT形成了被单克隆抗体M-H11识别的核心表位。此外，我们的研究结果表明，M-H11有效地控制大肠杆菌BL 21（DE 3）plysS感染，在体外和体内。我们的研究结果可能在寻找用于控制细菌感染的新方法方面具有重要价值。
The use of antibiotics to target bacteria is a well-validated approach for controlling infections in animals and humans. Peptidoglycan biosynthesis is a crucial process in bacteria, and the conserved peptidoglycan synthase MraY is an attractive target for drug design. However, due to the lack of detailed MraY structural information, antibiotics targeting MraY have not yet been developed. In the present study, 2 hydrophilic regions of MraY from Escherichia coli were expressed as a fusion protein and used to raise a monoclonal antibody in mice. We confirmed that the MraY amino acid sequence PESHFSKRGTPT forms the core epitope recognized by the monoclonal antibody M-H11. Furthermore, our results show that M-H11 effectively controls Escherichia coli BL21 (DE3) plysS infection, both in vitro and in vivo. Our results may be of great value in the search for novel approaches used to control bacterial infections.