Bovicin HJ50, a novel lantibiotic produced by Streptococcus bovis HJ50.

Bovicin HJ50, a novel lantibiotic produced by Streptococcus bovis HJ50.
复制标题

DOI:
10.1099/mic.0.26437-0
复制
发表时间:
2004
期刊:
影响因子:
1.5
通讯作者:
Haijie Xiao;Xiuzhu Chen;Meiling Chen;Shan Tang;Xin Zhao;Liandong Huan
Haijie Xiao;Xiuzhu Chen;Meiling Chen;Shan Tang;Xin Zhao;Liandong Huan
中科院分区:
生物学4区
文献类型:
--
作者:
Haijie Xiao;Xiuzhu Chen;Meiling Chen;Shan Tang;Xin Zhao;Liandong Huan

文献摘要

被引文献

相似文献

从原料乳中分离到一株细菌素产生菌,命名为牛链球菌HJ 50。与大多数乳酸菌产生的细菌素一样,bovicin HJ 50表现出较窄的抑制活性范围。对胰蛋白酶、枯草杆菌蛋白酶和蛋白酶K敏感。Bovicin HJ 50经正丙醇提取、SP Sepharose Fast Flow、Phenyl Superose和Sephadex G-50纯化。用bovicin HJ 50处理黄色微球菌NCIB 8166,显示钾以浓度依赖性方式从细胞内流出。测得bovicin HJ 50的分子量为3428.3 Da。经DTT处理的bovicin HJ 50的MS分析表明,bovicin HJ 50含有二硫键。根据牛亲和素HJ 50的N端氨基酸序列,采用巢式PCR技术克隆了其结构基因。序列分析表明,该基因编码一个58个氨基酸的前肽,由25个氨基酸的N端前导序列和33个氨基酸的C端前肽结构域组成。Bovicin HJ 50与AII型羊毛硫抗生素相似。使用含乙硫醇的反应混合物的化学修饰表明,两个Thr残基被修饰。
A bacteriocin-producing strain was isolated from raw milk and named Streptococcus bovis HJ50. Like most bacteriocins produced by lactic acid bacteria, bovicin HJ50 showed a narrow range of inhibiting activity. It was sensitive to trypsin, subtilisin and proteinase K. Bovicin HJ50 was extracted by n-propanol and purified by SP Sepharose Fast Flow, followed by Phenyl Superose and Sephadex G-50. Treatment of Micrococcus flavus NCIB8166 with bovicin HJ50 revealed potassium efflux from inside the cell in a concentration-dependent manner. The molecular mass of bovicin HJ50 was determined to be 3428.3 Da. MS analysis of DTT-treated bovicin HJ50 suggested that bovicin HJ50 contains a disulfide bridge. The structural gene of bovicin HJ50 was cloned by nested PCR based on its N-terminal amino acid sequence. Sequence analysis showed that it encodes a 58 aa prepeptide consisting of an N-terminal leader sequence of 25 aa and a C-terminal propeptide domain of 33 aa. Bovicin HJ50 shows similarity to type AII lantibiotics. Chemical modification using an ethanethiol-containing reaction mixture showed that two Thr residues are modified.