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

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

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.

MeSH terms

  • Amino Acid Sequence
  • Bacteriocins / genetics*
  • Bacteriocins / metabolism*
  • Base Sequence
  • Drug Resistance, Bacterial / genetics*
  • Genes, Bacterial / genetics
  • Lactobacillus plantarum / metabolism*
  • Microbial Sensitivity Tests
  • Sequence Analysis, DNA
  • Weissella / drug effects*
  • Weissella / genetics*

Substances

  • Bacteriocins
  • plantaricin JK