ArticleProceedings of the National Academy of Sciences of the United States of America2008
RNA-dependent lipid remodeling by bacterial multiple peptide resistance factors.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 82 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
82 citing papers in PubMed, 123 citations in OpenAlex.
- Cryo-EM structures of multiple-peptide resistance factor (MprF) from Pseudomonas aeruginosa.The FEBS journal · 2026Article
- Structure of ergosteryl-aspartate synthase reveals how an entrapped tRNA is used like a prosthetic swinging arm in the synthesis of aminoacylated sterols.Nature communications · 2026Article
- Characteristics of Clostridium perfringens from sheep (Ovis aries) flocks in Northern China.Veterinary research communications · 2025Article
- Coupling tRNAGly gene redundancy with staphylococcal cell wall integrity, antibiotic susceptibility, and virulence potential.Nucleic acids research · 2025Article
- MprF fromScience advances · 2025Article
- Lysyl-Phosphatidylglycerol: A Lipid Involved in the Resistance ofAntibiotics (Basel, Switzerland) · 2025Review
- Article
- MprF-mediated immune evasion is necessary for Lactiplantibacillus plantarum resilience in the Drosophila gut during inflammation.PLoS pathogens · 2024Article
- Article
- The intricate link between membrane lipid structure and composition and membrane structural properties in bacterial membranes.Chemical science · 2024Review
- The MprF homolog LysX synthesizes lysyl-diacylglycerol contributing to antibiotic resistance and virulence.Microbiology spectrum · 2023Article
- The tRNA identity landscape for aminoacylation and beyond.Nucleic acids research · 2023Review
- Harnessing the Role of Bacterial Plasma Membrane Modifications for the Development of Sustainable Membranotropic Phytotherapeutics.Membranes · 2022Review
- LysX2 is a Mycobacterium tuberculosis membrane protein with an extracytoplasmic MprF-like domain.BMC microbiology · 2022Article
- Identification of a novel cationic glycolipid in Streptococcus agalactiae that contributes to brain entry and meningitis.PLoS biology · 2022Article
- Lipid diversity in clostridia.Biochimica et biophysica acta. Molecular and cell biology of lipids · 2021Review
- Phospholipid translocation captured in a bifunctional membrane protein MprF.Nature communications · 2021Article
- In Silico Prediction and Analysis of Unusual Lantibiotic Resistance Operons in the GenusMicroorganisms · 2021Article
- Article
- Small-Molecule Acetylation by GCN5-RelatedMicrobiology and molecular biology reviews : MMBR · 2020Review
22 more citing papers are in PubMed but not listed here.
Corrections and comments
- Commented on by
Authors and funding
2 authors at 2 institutions in 2 countries.
Funding
Abstract
Multiple peptide resistance (MprF) virulence factors control cellular permeability to cationic antibiotics by aminoacylating inner membrane lipids. It has been shown previously that one class of MprF can use Lys-tRNA(Lys) to modify phosphatidylglycerol (PG), but the mechanism of recognition and possible role of other MprFs are unknown. Here, we used an in vitro reconstituted lipid aminoacylation system to investigate the two phylogenetically distinct MprF paralogs (MprF1 and MprF2) found in the bacterial pathogen Clostridium perfringens. Although both forms of MprF aminoacylate PG, they do so with different amino acids; MprF1 is specific for Ala-tRNA(Ala), and MprF2 utilizes Lys-tRNA(Lys). This provides a mechanism by which the cell can fine tune the charge of the inner membrane by using the neutral amino acid alanine, potentially providing resistance to a broader range of antibiotics than offered by lysine modification alone. Mutation of tRNA(Ala) and tRNA(Lys) had little effect on either MprF activity, indicating that the aminoacyl moiety is the primary determinant for aminoacyl-tRNA recognition. The lack of discrimination of the tRNA is consistent with the role of MprF as a virulence factor, because species-specific differences in tRNA sequence would not present a barrier to horizontal gene transfer. Taken together, our findings reveal how the MprF proteins provide a potent virulence mechanism by which pathogens can readily acquire resistance to chemically diverse antibiotics.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.