Bacteriocin ASM1 is an O / S -diglycosylated, plasmid-encoded homologue of glycocin F

FEBS Letters

article

Patrick Main¹  Tomomi Hata²  Trevor S. Loo¹  Petr Man³  Petr Novak³  Vladimír Havlíček³  Gillian E. Norris¹  Mark L. Patchett¹ 

[1] School of Fundamental Sciences, Massey University;Department of Food and Nutritional Sciences, Ochanomizu University;Institute of Microbiology, Academy of Sciences of the Czech Republic;Maurice Wilkins Centre for Molecular Biodiscovery, University of Auckland

关键词: bacteriocin;    glycocin;    plasmid;    S-linked glycopeptide bacteriostatic;   

DOI  :  10.1002/1873-3468.13708

来源: John Wiley & Sons Ltd.

【 摘 要 】

Here, we report on the biochemical characterization of a new glycosylated bacteriocin (glycocin), ASM1, produced by Lactobacillus plantarum A-1 and analysis of the A-1 bacteriocinogenic genes. ASM1 is 43 amino acids in length with Ser18-O- and Cys43-S-linked N-acetylglucosamine moieties that are essential for its inhibitory activity. Its only close homologue, glycocin F (GccF), has five amino acid substitutions all residing in the flexible C-terminal ‘tail’ and a lower IC50 (0.9 nM) compared to that of ASM1 (1.5 nM). Asm/gcc genes share the same organization (asmH ?asmABCDE?F), and the asm genes reside on an 11 905-bp plasmid dedicated to ASM1 production. The A-1 genome also harbors a gene encoding a ‘rare’ bactofencintype bacteriocin. As more examples of prokaryote S-GlcNAcylation are discovered, the functions of this modification may be understood.

【 授权许可】

Unknown