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

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.

Plantaricin NC8 αβ exerts potent antimicrobial activity against Staphylococcus spp. and enhances the effects of antibiotics

“…www.nature.com/scientificreports www.nature.com/scientificreports/ leading to stabilization of the peptides, and a subsequent membrane permeabilization and bacterial cell death due to alteration in intracellular pH and electric potential 11 . The role of partition-folding coupling was supported by the induced secondary structure when PLNC8 αβ interacted with a lipid bilayer as well as the absence of antimicrobial activity when scrambling the peptide sequences.…”

Identification and three‐dimensional structure of carnobacteriocin XY, a class IIb bacteriocin produced by Carnobacteria

“…By generating LcnG-resistant mutants and comparing their genomes to the genomes of sensitive strains, it was discovered that UppP, a membrane protein involved in peptidoglycan synthesis, is the receptor for LcnG [45]. In a similar fashion, the receptor for PlnJK was found to be a putative amino acid transporter [46]. This same strategy could be used to identify the receptor for CbnXY.…”

Sensitivity to the two peptide bacteriocin plantaricin EF is dependent on CorC, a membrane‐bound, magnesium/cobalt efflux protein

“…We hypothesize that PlnEF anchors to CorC and either inserts into the lipid bilayer directly or, alternatively, PlnEF inserts through CorC to cause disrupted metal homeostasis. In either case, the activity of PlnEF is distinct from the L. plantarum bacteriocin Plantaricin JK which is known to induce anion efflux and for which the cell surface receptor was identified as a protein in the APC transporter family (Oppegård et al, ). The results are similarly consistent with prior work showing the bacterial receptor for PlnEF is different from lactococcin A and other class II pediocin‐like bacteriocins known to bind to proteins in the mannose phosphotransferase system (Diep, Skaugen, Salehian, Holo, & Nes, ).…”

“…Initial success at identification of such receptors employed comparative genomics of bacteriocinsensitive and spontaneous, bacteriocin-resistant LAB strains (Kjos et al, 2014). In this way, the receptor for the pediocin-like bacteriocin leucocin A (targeting a mannose-specific phosphotransferase) (Ramnath, Beukes, Tamura, & Hastings, 2000), the leaderless bacteriocin enterocin K1 (targeting a stress response membrane-bound Zn-dependent protease) (Ovchinnikov et al, 2017), the two-peptide bacteriocins lactococcin G (targeting undecaprenyl pyrophosphate phosphatase) (Kjos et al, 2014), and plantaricin JK (targeting an uncharacterized protein in the amino acid-polyamine-organocation APC transporter protein family) were identified (Ekblad, Nissen-Meyer, & Kristensen, 2017;Oppegård, Kjos, Veening, Nissen-Meyer, & Kristensen, 2016).…”