ArticleThe Journal of biological chemistry2011
Structural basis for the interaction of lipopolysaccharide with outer membrane protein H (OprH) from Pseudomonas aeruginosa.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.
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Who cites it
44 citing papers in PubMed.
- High resolution cryo-EM structure of theJournal of structural biology: X · 2026Article
- Targeting Outer Membrane Vesicles ofJournal of microbiology and biotechnology · 2026Review
- Beyond Antibiotics: The Role of Antimicrobial Polymers in Modern Therapeutics.Pharmaceutics · 2026Review
- Solution NMR Spectroscopy for the Determination of Structures of Membrane Proteins in a Lipid Environment.Methods in molecular biology (Clifton, N.J.) · 2026Article
- The structure of the bacterial outer membrane transporter FusA enabled by addition of the native lipid lipopolysaccharide.Journal of structural biology: X · 2025Article
- Discovery of a Pseudomonas aeruginosa-specific small molecule targeting outer membrane protein OprH-LPS interaction by a multiplexed screen.Cell chemical biology · 2025Article
- Role of Divalent Ions in Membrane Models of Polymyxin-Sensitive and Resistant Gram-Negative Bacteria.Journal of chemical information and modeling · 2025Article
- Multidrug resistance in Pseudomonas aeruginosa: genetic control mechanisms and therapeutic advances.Molecular biomedicine · 2024Review
- AI analysis of super-resolution microscopy: Biological discovery in the absence of ground truth.The Journal of cell biology · 2024Review
- Antibiotic influx and efflux in Pseudomonas aeruginosa: Regulation and therapeutic implications.Microbial biotechnology · 2024Review
- Advances in Development of Novel Therapeutic Strategies against Multi-Drug ResistantAntibiotics (Basel, Switzerland) · 2024Review
- Aminoglycoside uptake, stress, and potentiation in Gram-negative bacteria: new therapies with old molecules.Microbiology and molecular biology reviews : MMBR · 2023Review
- CHARMM-GUIJournal of chemical theory and computation · 2023Review
- Membrane lipid renovation in Pseudomonas aeruginosa - implications for phage therapy?Environmental microbiology · 2022Review
- NMR measurement of biomolecular translational and rotational motion for evaluating changes of protein oligomeric state in solution.European biophysics journal : EBJ · 2022Review
- The Functional Significance of Hydrophobic Residue Distribution in Bacterial Beta-Barrel Transmembrane Proteins.Membranes · 2021Article
- Comparative analysis ofJournal of biomolecular NMR · 2021Article
- OMPdb: A Global Hub of Beta-Barrel Outer Membrane Proteins.Frontiers in bioinformatics · 2021Article
- The Building Blocks of Antimicrobial Resistance inFrontiers in cellular and infection microbiology · 2021Review
- COVID-19: Review on latest available drugs and therapies against SARS-CoV-2. Coagulation and inflammation cross-talking.Virus research · 2020Review
Corrections and comments
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Authors and funding
4 authors.
Funding
Abstract
Pseudomonas aeruginosa is a major nosocomial pathogen that infects cystic fibrosis and immunocompromised patients. The impermeability of the P. aeruginosa outer membrane contributes substantially to the notorious antibiotic resistance of this human pathogen. This impermeability is partially imparted by the outer membrane protein H (OprH). Here we have solved the structure of OprH in a lipid environment by solution NMR. The structure reveals an eight-stranded β-barrel protein with four extracellular loops of unequal size. Fast time-scale dynamics measurements show that the extracellular loops are disordered and unstructured. It was previously suggested that the function of OprH is to provide increased stability to the outer membranes of P. aeruginosa by directly interacting with lipopolysaccharide (LPS) molecules. Using in vivo and in vitro biochemical assays, we show that OprH indeed interacts with LPS in P. aeruginosa outer membranes. Based upon NMR chemical shift perturbations observed upon the addition of LPS to OprH in lipid micelles, we conclude that the interaction is predominantly electrostatic and localized to charged regions near both rims of the barrel, but also through two conspicuous tyrosines in the middle of the bilayer. These results provide the first molecular structure of OprH and offer evidence for multiple interactions between OprH and LPS that likely contribute to the antibiotic resistance of P. aeruginosa.
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