ArticleMolecular microbiology2016
The TamB ortholog of Borrelia burgdorferi interacts with the β-barrel assembly machine (BAM) complex protein BamA.
Article in Molecular microbiology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.
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Who cites it
43 citing papers in PubMed, 59 citations in OpenAlex.
- The Omp85 family protein, TamA, exhibits characteristics of a suitable drug target againstMicrobiology (Reading, England) · 2026Article
- BamA self-insertion drives inner-to-outer membrane remodelling in diderm Firmicutes.Nature communications · 2026Article
- Characterization of the OMP biogenesis machinery in Fusobacterium nucleatum.Structure (London, England : 1993) · 2025Article
- Structural insights into outer membrane protein biogenesis in pathogenic Neisseria.Structure (London, England : 1993) · 2025Article
- Surface protein machineries in Gram-negative bacteria.Journal of cell science · 2025Review
- TamL is a Key Player of the Outer Membrane Homeostasis in Bacteroidota.Journal of molecular biology · 2025Article
- Analysis of the BadR regulon in Borrelia burgdorferi.BMC microbiology · 2025Article
- Treponema denticola major surface protein (Msp): a key player in periodontal pathogenicity and immune evasion.Archives of microbiology · 2025Review
- Terrabacteria: redefining bacterial envelope diversity, biogenesis and evolution.Nature reviews. Microbiology · 2025Review
- The translocation assembly module (TAM) catalyzes the assembly of bacterial outer membrane proteins in vitro.Nature communications · 2024Article
- The translocation assembly module (TAM) catalyzes the assembly of bacterial outer membrane proteinsbioRxiv : the preprint server for biology · 2024Article
- Assessment of the hypothetical protein BB0616 in the murine infection ofInfection and immunity · 2024Article
- YdbH and YnbE form an intermembrane bridge to maintain lipid homeostasis in the outer membrane ofProceedings of the National Academy of Sciences of the United States of America · 2024Article
- The TAM, a Translocation and Assembly Module for protein assembly and potential conduit for phospholipid transfer.EMBO reports · 2024Review
- A conserved C-terminal domain of TamB interacts with multiple BamA POTRA domains in Borreliella burgdorferi.PloS one · 2024Article
- Analysis of Transmembrane β-Barrel Proteins by Native and Semi-native Polyacrylamide Gel Electrophoresis.Methods in molecular biology (Clifton, N.J.) · 2024Article
- TamAB is regulated by PhoPQ and functions in outer membrane homeostasis duringJournal of bacteriology · 2023Article
- Surveying membrane landscapes: a new look at the bacterial cell surface.Nature reviews. Microbiology · 2023Review
- 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
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
Two outer membrane protein (OMP) transport systems in diderm bacteria assist in assembly and export of OMPs. These two systems are the β-barrel assembly machine (BAM) complex and the translocation and assembly module (TAM). The BAM complex consists of the OMP component BamA along with several outer membrane associated proteins. The TAM also consists of an OMP, designated TamA, and a single inner membrane (IM) protein, TamB. Together TamA and TamB aid in the secretion of virulence-associated OMPs. In this study we characterized the hypothetical protein BB0794 in Borrelia burgdorferi. BB0794 contains a conserved DUF490 domain, which is a motif found in all TamB proteins. All spirochetes lack a TamA ortholog, but computational and physicochemical characterization of BB0794 revealed it is a TamB ortholog. Interestingly, BB0794 was observed to interact with BamA and a BB0794 regulatable mutant displayed altered cellular morphology and antibiotic sensitivity. The observation that B. burgdorferi contains a TamB ortholog that interacts with BamA and is required for proper outer membrane biogenesis not only identifies a novel role for TamB-like proteins, but also may explain why most diderms harbor a TamB-like protein while only a select group encodes TamA.
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