ArticleMolecular microbiology2010
Borrelia burgdorferi locus BB0795 encodes a BamA orthologue required for growth and efficient localization of outer membrane proteins.
Article in Molecular microbiology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.
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51 citing papers in PubMed, 64 citations in OpenAlex.
- Borrelia BBJ25 is a plasmid-encoded Omp85-family protein associated with a potential export system.Bioscience reports · 2026Article
- Dissection of amino acid acquisition pathways demonstrates that amino acid starvation of Borrelia burgdorferi results in a (p)ppGpp-independent maladaptive response.Communications biology · 2025Article
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- Analysis of the BadR regulon in Borrelia burgdorferi.BMC microbiology · 2025Article
- Outer membrane lipoproteins: late to the party, but the center of attention.Journal of bacteriology · 2025Review
- Leptospira interrogans encodes a canonical BamA and three novel noNterm Omp85 outer membrane protein paralogs.Scientific reports · 2024Article
- A conserved C-terminal domain of TamB interacts with multiple BamA POTRA domains in Borreliella burgdorferi.PloS one · 2024Article
- A Borrelia burgdorferi LptD homolog is required for flipping of surface lipoproteins through the spirochetal outer membrane.Molecular microbiology · 2023Article
- Identification of a novel transport system in Borrelia burgdorferi that links the inner and outer membranes.Pathogens and disease · 2023Article
- BB0562 is a nutritional virulence determinant with lipase activity important for Borrelia burgdorferi infection and survival in fatty acid deficient environments.PLoS pathogens · 2021Article
- Article
- Genetic Manipulation ofCurrent issues in molecular biology · 2021Review
- Crystallization and X-ray analysis of Borrelia burgdorferi β-barrel assembly machinery A.Acta crystallographica. Section F, Structural biology communications · 2020Article
- Characterization of 6S RNA in the Lyme disease spirochete.Molecular microbiology · 2020Article
- Protein Secretion in Spirochetes.Microbiology spectrum · 2019Article
- Borrelia burgdorferi protein interactions critical for microbial persistence in mammals.Cellular microbiology · 2019Review
- Identification of Surface Epitopes Associated with Protection against Highly Immune-Evasive VlsE-Expressing Lyme Disease Spirochetes.Infection and immunity · 2018Article
- Lipid rafts can form in the inner and outer membranes of Borrelia burgdorferi and have different properties and associated proteins.Molecular microbiology · 2018Article
- Co-immunoprecipitation for Identifying Protein-Protein Interactions in Borrelia burgdorferi.Methods in molecular biology (Clifton, N.J.) · 2018Article
- Folding of a bacterial integral outer membrane protein is initiated in the periplasm.Nature communications · 2017Article
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2 authors at 1 institution in 1 country.
Funding
Abstract
The outer membrane (OM) of the pathogenic diderm spirochete, Borrelia burgdorferi, contains integral beta-barrel outer membrane proteins (OMPs) in addition to its numerous outer surface lipoproteins. Very few OMPs have been identified in B. burgdorferi, and the protein machinery required for OMP assembly and OM localization is currently unknown. Essential OM BamA proteins have recently been characterized in Gram-negative bacteria that are central components of an OM beta-barrel assembly machine and are required for proper localization and insertion of bacterial OMPs. In the present study, we characterized a putative B. burgdorferi BamA orthologue encoded by open reading frame bb0795. Structural model predictions and cellular localization data indicate that the B. burgdorferi BB0795 protein contains an N-terminal periplasmic domain and a C-terminal, surface-exposed beta-barrel domain. Additionally, assays with an IPTG-regulatable bb0795 mutant revealed that BB0795 is required for B. burgdorferi growth. Furthermore, depletion of BB0795 results in decreased amounts of detectable OMPs in the B. burgdorferi OM. Interestingly, a decrease in the levels of surface-exposed lipoproteins was also observed in the mutant OMs. Collectively, our structural, cellular localization and functional data are consistent with the characteristics of other BamA proteins, indicating that BB0795 is a B. burgdorferi BamA orthologue.
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