ArticleProceedings of the National Academy of Sciences of the United States of America2009
Model of mouth-to-mouth transfer of bacterial lipoproteins through inner membrane LolC, periplasmic LolA, and outer membrane LolB.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 73 papers.
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Who cites it
73 citing papers in PubMed, 114 citations in OpenAlex.
- Mechanistic basis of LolDF-mediated lipoprotein transport in Acinetobacter.Nature communications · 2026Article
- Conformational hijacking of lipoprotein transporter LolDF enables precision antimicrobial activity against Acinetobacter baumannii.Nature communications · 2026Article
- Structure and druggable conformation of the homodimeric lipoprotein transporter of Acinetobacter baumannii.Nature communications · 2026Article
- Identification of a LolB-like protein in Porphyromonas gingivalis reveals selective LolA-LolB pairing.Scientific reports · 2026Article
- Targeting of the Gram-Negative Outer Membrane for Antibiotic Discovery and Potentiation.ACS infectious diseases · 2026Review
- Identification and characterization of the functional LolB ortholog inbioRxiv : the preprint server for biology · 2026Article
- Structural basis of outer membrane biogenesis by the TamAB translocase.Nature communications · 2026Article
- Surface protein machineries in Gram-negative bacteria.Journal of cell science · 2025Review
- Advances in Small Molecule Inhibitors Targeting the Bacterial Lipoprotein Transport System (Lol) in Gram-Negative Bacteria.Chemistry, an Asian journal · 2025Review
- Outer membrane lipoproteins: late to the party, but the center of attention.Journal of bacteriology · 2025Review
- Article
- Lipoprotein Signal Peptide as Adjuvants: Leveraging Lipobox-Driven TLR2 Activation in Modern Vaccine Design.Vaccines · 2025Review
- Deciphering the molecular basis of lipoprotein recognition and transport by LolCDE.Signal transduction and targeted therapy · 2024Article
- Dissection of an ABC transporter LolCDE function analyzed by photo-crosslinking.Journal of biochemistry · 2024Article
- Designing a multi-epitope vaccine againstFrontiers in genetics · 2024Article
- Structural and functional analysis of theFrontiers in microbiology · 2024Article
- Identification of an Essential LolD-Like Protein in Helicobacter pylori.Journal of bacteriology · 2023Article
- A comparative analysis of lipoprotein transport proteins: LolA and LolB from Vibrio cholerae and LolA from Porphyromonas gingivalis.Scientific reports · 2023Article
- Teasing apart the evolution of lipoprotein trafficking in gram-negative bacteria reveals a bifunctional LolA.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Making a chink in their armor: Current and next-generation antimicrobial strategies against the bacterial cell envelope.Advances in microbial physiology · 2023Article
13 more citing papers are in PubMed but not listed here.
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Authors and funding
2 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Outer membrane-specific lipoproteins in Escherichia coli are released from the inner membrane by an ATP-binding cassette transporter, the LolCDE complex, which causes the formation of a soluble complex with a periplasmic molecular chaperone, LolA. LolA then transports lipoproteins to the outer membrane where an outer membrane receptor, LolB, incorporates lipoproteins into the outer membrane. The molecular mechanisms underlying the Lol-dependent lipoprotein sorting have been clarified in detail. However, it remained unclear how Lol factors interact with each other to conduct very efficient lipoprotein transfer in the periplasm where ATP is not available. To address this issue, a photo-reactive phenylalanine analogue, p-benzoyl-phenylalanine, was introduced at various positions of LolA and LolB, of which the overall structures are very similar and comprise an incomplete beta-barrel with a hydrophobic cavity inside. Cells expressing LolA or LolB derivatives containing the above analogue were irradiated with UV for in vivo photo-cross-linking. These analyses revealed a hot area in the same region of LolA and LolB, through which LolA and LolB interact with each other. This area is located at the entrance of the hydrophobic cavity. Moreover, this area in LolA is involved in the interaction with a membrane subunit, LolC, whereas no cross-linking occurs between LolA and the other membrane subunit, LolE, or ATP-binding subunit LolD, despite the structural similarity between LolC and LolE. The hydrophobic cavities of LolA and LolB were both found to bind lipoproteins inside. These results indicate that the transfer of lipoproteins through Lol proteins occurs in a mouth-to-mouth manner.
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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.