ArticleMolecular microbiology2021
Two ABC transport systems carry out peptide uptake in Enterococcus faecalis: Their roles in growth and in uptake of sex pheromones.
Article in Molecular microbiology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 10 citations in OpenAlex.
- Pheromone cCF10 Enhances Persister Formation inMicroorganisms · 2026Article
- Insights into ecology, pathogenesis, and biofilm formation ofMicrobiology and molecular biology reviews : MMBR · 2025Review
- Structure and ligand binding in the putative anti-microbial peptide transporter protein, YejA.Microbiology (Reading, England) · 2024Article
- Pheromone cCF10 inhibits the antibiotic persistence ofFrontiers in microbiology · 2024Article
- Two Permeases Associated with the Multifunctional CtaP Cysteine Transport System in Listeria monocytogenes Play Distinct Roles in Pathogenesis.Microbiology spectrum · 2023Article
- Vancomycin-variable enterococci in sheep and cattle isolates and whole-genome sequencing analysis of isolates harboringIranian journal of veterinary research · 2023Article
- Structural Differences in Complexes between the Master Regulator PrgX, Peptide Pheromones, and Operator Binding Sites Determine the Induction State for Conjugative Transfer of pCF10.Journal of bacteriology · 2022Article
- Adaptation of the gut pathobiont Enterococcus faecalis to deoxycholate and taurocholate bile acids.Scientific reports · 2022Article
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
Abstract
Enterococcal pheromone-inducible plasmids encode a predicted OppA-family secreted lipoprotein. In the case of plasmid pCF10, the protein is PrgZ, which enhances the mating response to cCF10 pheromone. OppA proteins generally function with associated OppBCDF ABC transporters to import peptides. In this study, we analyzed the potential interactions of PrgZ with two host-encoded Opp transporters using two pheromone-inducible fluorescent reporter constructs. Based on our results, we propose renaming these loci opp1 (OG1RF_10634-10639) and opp2 (OG1RF_12366-12370). We also examined the ability of the Opp1 and Opp2 systems to mediate import in the absence of PrgZ. Cells expressing PrgZ were able to import pheromone if either opp1 or opp2 was functional, but not if both opp loci were disrupted. In the absence of PrgZ, pheromone import was dependent on a functional opp2 system, including opp2A. Comparative structural analysis of the peptide-binding pockets of PrgZ, Opp1A, Opp2A, and the related Lactococcus lactis OppA protein, suggested that the robust pheromone-binding ability of PrgZ relates to a nearly optimal fit of the hydrophobic peptide, whereas binding ability of Opp2A likely results from a more open, promiscuous peptide-binding pocket similar to L. lactis OppA.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.