ArticleBMC microbiology2015
Characterization of the β-barrel assembly machine accessory lipoproteins from Borrelia burgdorferi.
Article in BMC microbiology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 24 citations in OpenAlex.
- Analysis of the BadR regulon in Borrelia burgdorferi.BMC microbiology · 2025Article
- Leptospira interrogans encodes a canonical BamA and three novel noNterm Omp85 outer membrane protein paralogs.Scientific reports · 2024Article
- Article
- A conserved C-terminal domain of TamB interacts with multiple BamA POTRA domains in Borreliella burgdorferi.PloS one · 2024Article
- Identification of a novel transport system in Borrelia burgdorferi that links the inner and outer membranes.Pathogens and disease · 2023Article
- Crystallization and X-ray analysis of Borrelia burgdorferi β-barrel assembly machinery A.Acta crystallographica. Section F, Structural biology communications · 2020Article
- BB0326 is responsible for the formation of periplasmic flagellar collar and assembly of the stator complex in Borrelia burgdorferi.Molecular microbiology · 2020Article
- Characterization of 6S RNA in the Lyme disease spirochete.Molecular microbiology · 2020Article
- Membrane directed expression in Escherichia coli of BBA57 and other virulence factors from the Lyme disease agent Borrelia burgdorferi.Scientific reports · 2019Article
- Protein Secretion in Spirochetes.Microbiology spectrum · 2019Article
- Deprivation of the Periplasmic Chaperone SurA Reduces Virulence and Restores Antibiotic Susceptibility of Multidrug-ResistantFrontiers in microbiology · 2019Article
- A tetratricopeptide repeat domain protein has profound effects on assembly of periplasmic flagella, morphology and motility of the lyme disease spirochete Borrelia burgdorferi.Molecular microbiology · 2018Article
- Co-immunoprecipitation for Identifying Protein-Protein Interactions in Borrelia burgdorferi.Methods in molecular biology (Clifton, N.J.) · 2018Article
- Comprehensive Spatial Analysis of the Borrelia burgdorferi Lipoproteome Reveals a Compartmentalization Bias toward the Bacterial Surface.Journal of bacteriology · 2017Article
- The TamB ortholog of Borrelia burgdorferi interacts with the β-barrel assembly machine (BAM) complex protein BamA.Molecular microbiology · 2016Article
- Consensus computational network analysis for identifying candidate outer membrane proteins from Borrelia spirochetes.BMC microbiology · 2016Article
- The Treponema pallidum Outer Membrane.Current topics in microbiology and immunologyReview
- Genetic Manipulation of Borrelia Spp.Current topics in microbiology and immunologyReview
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
backgroundLike all diderm bacteria studied to date, Borrelia burgdorferi possesses a β-barrel assembly machine (BAM) complex. The bacterial BAM complexes characterized thus far consist of an essential integral outer membrane protein designated BamA and one or more accessory proteins. The accessory proteins are typically lipid-modified proteins anchored to the inner leaflet of the outer membrane through their lipid moieties. We previously identified and characterized the B. burgdorferi BamA protein in detail and more recently identified two lipoproteins encoded by open reading frames bb0324 and bb0028 that associate with the borrelial BamA protein. The role(s) of the BAM accessory lipoproteins in B. burgdorferi is currently unknown.
resultsStructural modeling of B. burgdorferi BB0028 revealed a distinct β-propeller fold similar to the known structure for the E. coli BAM accessory lipoprotein BamB. Additionally, the structural model for BB0324 was highly similar to the known structure of BamD, which is consistent with the prior finding that BB0324 contains tetratricopeptide repeat regions similar to other BamD orthologs. Consistent with BB0028 and BB0324 being BAM accessory lipoproteins, mutants lacking expression of each protein were found to exhibit altered membrane permeability and enhanced sensitivity to various antimicrobials. Additionally, BB0028 mutants also exhibited significantly impaired in vitro growth. Finally, immunoprecipitation experiments revealed that BB0028 and BB0324 each interact specifically and independently with BamA to form the BAM complex in B. burgdorferi.
conclusionsCombined structural studies, functional assays, and co-immunoprecipitation experiments confirmed that BB0028 and BB0324 are the respective BamB and BamD orthologs in B. burgdorferi, and are important in membrane integrity and/or outer membrane protein localization. The borrelial BamB and BamD proteins both interact specifically and independently with BamA to form a tripartite BAM complex in B. burgdorferi. A working model has been developed to further analyze outer membrane biogenesis and outer membrane protein transport in this pathogenic spirochete.
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