ArticleJournal of proteome research2011
Characterization of multiprotein complexes of the Borrelia burgdorferi outer membrane vesicles.
Article in Journal of proteome research, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.
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Who cites it
45 citing papers in PubMed, 57 citations in OpenAlex.
- Targeting of interaction between BB0323-BB0238 informs new paradigms in Lyme disease therapeutics.PLoS pathogens · 2026Article
- Peptidoglycan architecture dictates protein interactions, tissue tropism, and arthritis in the Lyme disease spirochete Borrelia burgdorferi.PLoS pathogens · 2026Article
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- A systemic approach to identify non-abundant immunogenic proteins in Lyme disease pathogens.mSystems · 2024Article
- The Interaction of Borrelia burgdorferi with Human Dendritic Cells: Functional Implications.Journal of immunology (Baltimore, Md. : 1950) · 2023Article
- Dome1-JAK-STAT signaling between parasite and host integrates vector immunity and development.Science (New York, N.Y.) · 2023Article
- Transmission Cycle of Tick-Borne Infections and Co-Infections, Animal Models and Diseases.Pathogens (Basel, Switzerland) · 2022Review
- Cross-Reactive Results in Serological Tests for Borreliosis in Patients with Active Viral Infections.Pathogens (Basel, Switzerland) · 2022Article
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- BB0562 is a nutritional virulence determinant with lipase activity important for Borrelia burgdorferi infection and survival in fatty acid deficient environments.PLoS pathogens · 2021Article
- The peptidoglycan-associated protein NapA plays an important role in the envelope integrity and in the pathogenesis of the lyme disease spirochete.PLoS pathogens · 2021Article
- Antibodies against EGF-like domains in Ixodes scapularis BM86 orthologs impact tick feeding and survival of Borrelia burgdorferi.Scientific reports · 2021Article
- Investigating BB0405 as a novel Borrelia afzelii vaccination candidate in Lyme borreliosis.Scientific reports · 2021Article
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- The Borrelia burgdorferi infection critical BBK13 protein forms large oligomers in the spirochete membrane.Biochemical and biophysical research communications · 2021Article
- Interactions Between Ticks and Lyme Disease Spirochetes.Current issues in molecular biology · 2021Article
- A Novel Laminin-Binding Protein Mediates Microbial-Endothelial Cell Interactions and Facilitates Dissemination of Lyme Disease Pathogens.The Journal of infectious diseases · 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
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Authors and funding
8 authors at 3 institutions in 1 country.
Funding
Abstract
Among bacterial cell envelopes, the Borrelia burgdorferi outer membrane (OM) is structurally unique in that the identities of many protein complexes remain unknown; however, their characterization is the first step toward our understanding of membrane protein interactions and potential functions. Here, we used two-dimensional blue native/SDS-PAGE/mass spectrometric analysis for a global characterization of protein-protein interactions as well as to identify protein complexes in OM vesicles isolated from multiple infectious sensu stricto isolates of B. burgdorferi. Although we uncovered the existence of at least 10 distinct OM complexes harboring several unique subunits, the complexome is dominated by the frequent occurrence of a limited diversity of membrane proteins, most notably P13, outer surface protein (Osp) A, -B, -C, and -D and Lp6.6. The occurrence of these complexes and specificity of subunit interaction were further supported by independent two-dimensional immunoblotting and coimmunoprecipitation assays as well as by mutagenesis studies, where targeted depletion of a subunit member (P66) selectively abolished a specific complex. Although a comparable profile of the OM complexome was detected in two major infectious isolates, such as B31 and 297, certain complexes are likely to occur in an isolate-specific manner. Further assessment of protein complexes in multiple Osp-deficient isolates showed loss of several protein complexes but revealed the existence of additional complex/subunits that are undetectable in wild-type cells. Together, these observations uncovered borrelial antigens involved in membrane protein interactions. The study also suggests that the assembly process of OM complexes is specific and that the core or stabilizing subunits vary between complexes. Further characterization of these protein complexes including elucidation of their biological significance may shed new light on the mechanism of pathogen persistence and the development of preventative measures against the infection.
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