ArticleThe Journal of biological chemistry2014
Roles of the protruding loop of factor B essential for the localization of lipoproteins (LolB) in the anchoring of bacterial triacylated proteins to the outer membrane.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 32 citations in OpenAlex.
- 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
- Transcriptome Analysis Reveals the Potential Mechanism of MAP34-B TargetingMicroorganisms · 2026Article
- Identification and characterization of the functional LolB ortholog inbioRxiv : the preprint server for biology · 2026Article
- The structures and functions of Salmonella outer membrane.Archives of microbiology · 2026Review
- Breaking the outer membrane barrier: structure, targets, and antimicrobial strategies for Gram-negative bacteria.Frontiers in microbiology · 2026Review
- Advances in Small Molecule Inhibitors Targeting the Bacterial Lipoprotein Transport System (Lol) in Gram-Negative Bacteria.Chemistry, an Asian journal · 2025Review
- LolA and LolB are conserved in Bacteroidota and are crucial for gliding motility and Type IX secretion.Communications biology · 2025Article
- Outer membrane lipoproteins: late to the party, but the center of attention.Journal of bacteriology · 2025Review
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- Structural and functional analysis of theFrontiers in microbiology · 2024Article
- Genetic analysis reveals a robust and hierarchical recruitment of the LolA chaperone to the LolCDE lipoprotein transporter.bioRxiv : the preprint server for biology · 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
- LolA and LolB from the plant-pathogenFrontiers in microbiology · 2023Article
- The lolB gene in Xanthomonas campestris pv. campestris is required for bacterial attachment, stress tolerance, and virulence.BMC microbiology · 2022Article
- Lipid trafficking across the Gram-negative cell envelope.The Journal of biological chemistry · 2019Review
- tRNA Methylation Is a Global Determinant of Bacterial Multi-drug Resistance.Cell systems · 2019Article
Corrections and comments
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Authors and funding
8 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The Lol system comprising five Lol proteins, LolA through LolE, sorts Escherichia coli lipoproteins to outer membranes. The LolCDE complex, an ATP binding cassette transporter in inner membranes, releases outer membrane-specific lipoproteins in an ATP-dependent manner, causing formation of the LolA-lipoprotein complex in the periplasm. LolA transports lipoproteins through the periplasm to LolB on outer membranes. LolB is itself a lipoprotein anchored to outer membranes, although the membrane anchor is functionally dispensable. LolB then localizes lipoproteins to outer membranes through largely unknown mechanisms. The crystal structure of LolB is similar to that of LolA, and it possesses a hydrophobic cavity that accommodates acyl chains of lipoproteins. To elucidate the molecular function of LolB, a periplasmic version of LolB, mLolB, was mutagenized at various conserved residues. Despite the lack of acyl chains, most defective mutants were insoluble. However, a derivative with glutamate in place of leucine 68 was soluble and unable to localize lipoproteins to outer membranes. This leucine is present in a loop protruding from mLolB into an aqueous environment, and no analogous loop is present in LolA. Thus, leucine 68 was replaced with other residues. Replacement by acidic, but not hydrophobic, residues generated for the first time mLolB derivatives that can accept but cannot localize lipoproteins to outer membranes. Moreover, deletion of the leucine with neighboring residues impaired the lipoprotein receptor activity. Based on these observations, the roles of the protruding loop of LolB in the last step of lipoprotein sorting are discussed.
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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.