Department of Food and Animal Biotechnology, Center for Agricultural Biomaterials Seoul National University, Seoul, South Korea.
FEMS Microbiol Lett. 2012 Jul;332(1):76-83. doi: 10.1111/j.1574-6968.2012.02578.x. Epub 2012 May 10.
Use of bacteriophages as biocontrol agents is a promising tool for controlling pathogenic bacteria including antibiotic-resistant bacteria. Not only bacteriophages but also endolysins, the peptidoglycan hydrolyzing enzymes encoded by bacteriophages, have high potential for applications as biocontrol agents against food-borne pathogens. In this study, a putative endolysin gene was identified in the genome of the bacteriophage BPS13, which infects Bacillus cereus. In silico analysis of this endolysin, designated LysBPS13, showed that it consists of an N-terminal catalytic domain (PGRP domain) and a C-terminal cell wall binding domain (SH3_5 domain). Further characterization of the purified LysBPS13 revealed that this endolysin is an N-acetylmuramyl-l-alanine amidase, the activity of which was not influenced by addition of EDTA. In addition, LysBPS13 demonstrated remarkable thermostability in the presence of glycerol, and it retained its lytic activity even after incubation at 100 °C for 30 min. Taken together, these results indicate that LysBPS13 can be considered a favorable candidate for a new antimicrobial agent to control B. cereus.
噬菌体作为生物防治剂的使用是控制包括抗生素耐药菌在内的病原菌的一种有前途的工具。不仅噬菌体，而且噬菌体编码的肽聚糖水解酶内溶素，也具有作为食品病原体生物防治剂的高应用潜力。在这项研究中，在感染蜡状芽孢杆菌的噬菌体 BPS13 的基因组中鉴定出一个假定的内溶素基因。对内溶素 LysBPS13 的计算机分析表明，它由一个 N 端催化结构域（PGRP 结构域）和一个 C 端细胞壁结合结构域（SH3_5 结构域）组成。对纯化的 LysBPS13 的进一步表征表明，这种内溶素是一种 N-乙酰胞壁酰-L-丙氨酰酰胺酶，其活性不受 EDTA 加入的影响。此外，LysBPS13 在甘油存在下表现出显著的热稳定性，即使在 100°C 孵育 30 分钟后，它仍保持其裂解活性。总之，这些结果表明 LysBPS13 可以被认为是一种有前途的新型抗菌剂候选物，可用于控制蜡状芽孢杆菌。
