ArticleNature chemical biology2021
Dynamics of an LPS translocon induced by substrate and an antimicrobial peptide.
Article in Nature chemical biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.
What it found
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Who cites it
43 citing papers in PubMed, 68 citations in OpenAlex.
- Computational design of a soluble mimic of the outer membrane LPS transport protein LptD suitable for screening of antibiotics.Protein science : a publication of the Protein Society · 2026Article
- Design and evaluation of a bifunctional fusion polypeptide for targeted delivery of tigecycline against drug-resistant Klebsiella pneumoniae.Journal of nanobiotechnology · 2026Article
- Bacterial cell envelope-targeting antibiotics.Nature reviews. Microbiology · 2026Review
- Time-resolved transcriptomic analysis reveals envelope stress-mediated adaptation ofFrontiers in microbiology · 2026Article
- Structural snapshots of Pseudomonas aeruginosa LptBNature communications · 2025Article
- Structural basis of lipopolysaccharide assembly by the outer membrane translocon holo-complex.Nature communications · 2025Article
- Structures, Interactions, and Antimicrobial Activity of the Shortest Thanatin Peptide fromInternational journal of molecular sciences · 2025Article
- Inhibiting Lipopolysaccharide Biogenesis: The More You Know the Further You Go.Annual review of biochemistry · 2025Review
- Native MS-guided lipidomics to define endogenous lipid microenvironments of eukaryotic receptors and transporters.Nature protocols · 2025Article
- Review
- Designing Analogs of SAAP-148 with Enhanced Antimicrobial and Anti-LPS Activities.International journal of molecular sciences · 2024Article
- Dynamics design of a non-natural transcription factor responding to androst-4-ene-3,17-dione.Synthetic and systems biotechnology · 2024Article
- Thanatin: A Promising Antimicrobial Peptide Targeting the Achilles' Heel of Multidrug-Resistant Bacteria.International journal of molecular sciences · 2024Review
- Seeing is believing: Illuminating the Gram-negative outer membrane with molecular dynamics simulations.Current opinion in structural biology · 2024Review
- Detergents with Scalable Properties Identify Noncanonical Lipopolysaccharide Binding to Bacterial Inner Membrane Proteins.Journal of the American Chemical Society · 2024Article
- Structural Insights into the Lipopolysaccharide Transport (Lpt) System as a Novel Antibiotic Target.Journal of microbiology (Seoul, Korea) · 2024Review
- Real-Time Biosynthetic Reaction Monitoring Informs the Mechanism of Action of Antibiotics.Journal of the American Chemical Society · 2024Article
- Outer-Membrane Permeabilization, LPS Transport Inhibition: Activity, Interactions, and Structures of Thanatin Derived Antimicrobial Peptides.International journal of molecular sciences · 2024Article
- Structures, Interactions and Activity of the N-Terminal Truncated Variants of Antimicrobial Peptide Thanatin.Antibiotics (Basel, Switzerland) · 2024Article
- Recent Advances in Modeling Membrane β-Barrel Proteins Using Molecular Dynamics Simulations: From Their Lipid Environments to Their Assemblies.Methods in molecular biology (Clifton, N.J.) · 2024Article
Corrections and comments
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Authors and funding
10 authors at 3 institutions in 1 country.
Funding
Abstract
Lipopolysaccharide (LPS) transport to the outer membrane (OM) is a crucial step in the biogenesis of microbial surface defenses. Although many features of the translocation mechanism have been elucidated, molecular details of LPS insertion via the LPS transport (Lpt) OM protein LptDE remain elusive. Here, we integrate native MS with hydrogen-deuterium exchange MS and molecular dynamics simulations to investigate the influence of substrate and peptide binding on the conformational dynamics of LptDE. Our data reveal that LPS induces opening of the LptD β-taco domain, coupled with conformational changes on β-strands adjacent to the putative lateral exit gate. Conversely, an antimicrobial peptide, thanatin, stabilizes the β-taco, thereby preventing LPS transport. Our results illustrate that LPS insertion into the OM relies on concerted opening movements of both the β-barrel and β-taco domains of LptD, and suggest a means for developing antimicrobial therapeutics targeting this essential process in Gram-negative ESKAPE pathogens.
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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.