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Microbiologyopen. 2016 Aug;5(4):700-8. doi: 10.1002/mbo3.363. Epub 2016 May 5.

A putative amino acid transporter determines sensitivity to the two-peptide bacteriocin plantaricin JK.

Author information

1
Biochemistry and Molecular Biology Section, Department of Biosciences, University of Oslo, P.O. Box 1066 Blindern, Oslo, 0316, Norway.
2
Molecular Genetics Group, Groningen Biomolecular Sciences and Biotechnology Institute, Centre for Synthetic Biology, University of Groningen, Nijenborgh 7 9747 AG, Groningen, The Netherlands.

Abstract

Lactobacillus plantarum produces a number of antimicrobial peptides (bacteriocins) that mostly target closely related bacteria. Although bacteriocins are important for the ecology of these bacteria, very little is known about how the peptides target sensitive cells. In this work, a putative membrane protein receptor of the two-peptide bacteriocin plantaricin JK was identified by comparing Illumina sequence reads from plantaricin JK-resistant mutants to a crude assembly of the sensitive wild-type Weissella viridescens genome using the polymorphism discovery tool VAAL. Ten resistant mutants harbored altogether seven independent mutations in a gene encoding an APC superfamily protein with 12 transmembrane helices. The APC superfamily transporter thus is likely to serve as a target for plantaricin JK on sensitive cells.

KEYWORDS:

Antibacterial activity; bacteriocins; membrane proteins; mode of action

PMID:
27150273
PMCID:
PMC4985602
DOI:
10.1002/mbo3.363
[Indexed for MEDLINE]
Free PMC Article

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