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FEBS Lett. 2019 Dec 12. doi: 10.1002/1873-3468.13708. [Epub ahead of print]

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

Author information

1
School of Fundamental Sciences, Massey University, Palmerston North, New Zealand.
2
Department of Food and Nutritional Sciences, Ochanomizu University, Tokyo, Japan.
3
Institute of Microbiology, v.v.i., Academy of Sciences of the Czech Republic, Prague 4, Czech Republic.
4
Maurice Wilkins Centre for Molecular Biodiscovery, University of Auckland, New Zealand.

Abstract

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' bactofencin-type bacteriocin. As more examples of prokaryote S-GlcNAcylation are discovered, the functions of this modification may be understood.

KEYWORDS:

S-linked glycopeptide bacteriostatic; bacteriocin; glycocin; plasmid

PMID:
31829452
DOI:
10.1002/1873-3468.13708

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