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Bovicin HJ50, a novel lantibiotic produced by Streptococcus bovis HJ50

¹ Molecular Microbiology Research Center, Institute of Microbiology, Chinese Academy of Sciences, PO Box 2714, Beijing, PR China
² State Key Laboratory of Microbial Resources, Institute of Microbiology, Chinese Academy of Sciences, PO Box 2714, Beijing, PR China
³ Department of Microbiology, University of California, Riverside, CA 92521, USA

Correspondence
Liandong Huan
huanld{at}sun.im.ac.cn

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.

The GenBank accession numbers for the 16S rDNA sequence of S. bovis HJ50 and bovA reported in this paper are AY173079 and AY271354.

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