ArticleCommunications biology2025
LolA and LolB are conserved in Bacteroidota and are crucial for gliding motility and Type IX secretion.
Article in Communications biology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed.
- Proteomic Profiling Reveals Intracellular Regulatory Network Disturbance Induced by QseB Deletion inMicroorganisms · 2026Article
- β-lactamase genes in clinical isolates of Capnocytophaga canimorsus and description of a novel class D β-lactamase, OXA-1422.European journal of clinical microbiology & infectious diseases : official publication of the European Society of Clinical Microbiology · 2026Article
- Identification of a LolB-like protein in Porphyromonas gingivalis reveals selective LolA-LolB pairing.Scientific reports · 2026Article
- Borrelia BBJ25 is a plasmid-encoded Omp85-family protein associated with a potential export system.Bioscience reports · 2026Article
- Identification and characterization of the functional LolB ortholog inbioRxiv : the preprint server for biology · 2026Article
- TamL is a Key Player of the Outer Membrane Homeostasis in Bacteroidota.Journal of molecular biology · 2025Article
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12 authors.
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Abstract
Lipoproteins are key outer membrane (OM) components in Gram-negative bacteria, essential for functions like membrane biogenesis and virulence. Bacteroidota, a diverse and widespread phylum, produce numerous OM lipoproteins that play vital roles in nutrient acquisition, Type IX secretion system (T9SS), and gliding motility. In Escherichia coli, lipoprotein transport to the OM is mediated by the Lol system, where LolA shuttles lipoproteins to LolB, which anchors them in the OM. However, LolB homologs were previously thought to be limited to γ- and β-proteobacteria. This study uncovers the presence of LolB in Bacteroidota and demonstrates that multiple LolA and LolB proteins co-exist in various species. Specifically, in Flavobacterium johnsoniae, LolA1 and LolB1 transport gliding motility and T9SS lipoproteins to the OM. Notably, these proteins are not interchangeable with their E. coli counterparts, indicating functional specialization. Some lipoproteins still localize to the OM in the absence of LolA and LolB, suggesting the existence of alternative transport pathways in Bacteroidota. This points to a more complex lipoprotein transport system in Bacteroidota compared to other Gram-negative bacteria. These findings reveal previously unrecognized lipoprotein transport mechanisms in Bacteroidota and suggest that this phylum has evolved unique strategies to manage the essential task of lipoprotein localization.
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