ArticleJournal of bacteriology2013
The Escherichia coli Lpt transenvelope protein complex for lipopolysaccharide export is assembled via conserved structurally homologous domains.
Article in Journal of bacteriology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 78 papers.
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Who cites it
78 citing papers in PubMed.
- Article
- Computational systems immunology and multi-scale modeling for the design of a Multi-Epitope Vaccine (MEV) against emerging multidrug-resistant Klebsiella michiganensis.International microbiology : the official journal of the Spanish Society for Microbiology · 2026Article
- Molecular mechanism of action of small molecule SMT-738 on bacterial lipoprotein transporter LolCDE.Nature communications · 2026Article
- The structures and functions of Salmonella outer membrane.Archives of microbiology · 2026Review
- Article
- High-Throughput Identification and Characterization of LptDE-Binding Bicycle Peptides Using Phage Display and Cryo-EM.Journal of medicinal chemistry · 2025Article
- Conformational Plasticity of LptC Regulates Lipopolysaccharide Transport by the LptBJournal of the American Chemical Society · 2025Article
- Inhibiting Lipopolysaccharide Biogenesis: The More You Know the Further You Go.Annual review of biochemistry · 2025Review
- The LptC transmembrane helix undergoes a rigid body movement upon LptBProtein science : a publication of the Protein Society · 2025Article
- Advances in Helicobacter pylori lipopolysaccharide structure and function.FEMS microbiology reviews · 2025Review
- Integrated multi-omics reveals distinct maternal and neonatal gut microbial and metabolic signatures associated with small for gestational age status.Frontiers in microbiology · 2025Article
- Article
- Thanatin: A Promising Antimicrobial Peptide Targeting the Achilles' Heel of Multidrug-Resistant Bacteria.International journal of molecular sciences · 2024Review
- Structural Insights into the Lipopolysaccharide Transport (Lpt) System as a Novel Antibiotic Target.Journal of microbiology (Seoul, Korea) · 2024Review
- Subverting the Canon: Novel Cancer-Promoting Functions and Mechanisms for snoRNAs.International journal of molecular sciences · 2024Review
- Conformational investigation of the asymmetric periplasmic domains ofApplied magnetic resonance · 2024Article
- Residues within the LptC transmembrane helix are critical for Escherichia coli LptBProtein science : a publication of the Protein Society · 2024Article
- Article
- Article
- Designing of multi-epitope peptide vaccine against Acinetobacter baumannii through combined immunoinformatics and protein interaction-based approaches.Immunologic research · 2023Article
18 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
10 authors.
Funding
Abstract
Lipopolysaccharide is a major glycolipid component in the outer leaflet of the outer membrane (OM), a peculiar permeability barrier of Gram-negative bacteria that prevents many toxic compounds from entering the cell. Lipopolysaccharide transport (Lpt) across the periplasmic space and its assembly at the Escherichia coli cell surface are carried out by a transenvelope complex of seven essential Lpt proteins spanning the inner membrane (LptBCFG), the periplasm (LptA), and the OM (LptDE), which appears to operate as a unique machinery. LptC is an essential inner membrane-anchored protein with a large periplasm-protruding domain. LptC binds the inner membrane LptBFG ABC transporter and interacts with the periplasmic protein LptA. However, its role in lipopolysaccharide transport is unclear. Here we show that LptC lacking the transmembrane region is viable and can bind the LptBFG inner membrane complex; thus, the essential LptC functions are located in the periplasmic domain. In addition, we characterize two previously described inactive single mutations at two conserved glycines (G56V and G153R, respectively) of the LptC periplasmic domain, showing that neither mutant is able to assemble the transenvelope machinery. However, while LptCG56V failed to copurify any Lpt component, LptCG153R was able to interact with the inner membrane protein complex LptBFG. Overall, our data further support the model whereby the bridge connecting the inner and outer membranes would be based on the conserved structurally homologous jellyroll domain shared by five out of the seven Lpt components.
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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.