ArticleScientific reports2021
Interaction between Borrelia miyamotoi variable major proteins Vlp15/16 and Vlp18 with plasminogen and complement.
Article in Scientific reports, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 14 citations in OpenAlex.
- Complement inhibition by a unique cluster of immunomodulatory outer surface proteins of Borrelia recurrentis.Nature communications · 2026Article
- Natural genetic variation impacts complement inhibitory activity of PFam54 orthologs of Asian Borrelia bavariensis.Scientific reports · 2026Article
- Establishment of a laboratory mouse model to studyFrontiers in immunology · 2026Article
- Combining short- and long-read sequencing unveils geographically structured diversity iniScience · 2024Article
- Multifunctional interaction of CihC/FbpC orthologs of relapsing fever spirochetes with host-derived proteins involved in adhesion, fibrinolysis, and complement evasion.Frontiers in immunology · 2024Article
- "Conformational dynamics of C1r inhibitor proteins from Lyme disease and relapsing fever spirochetes".bioRxiv : the preprint server for biology · 2023Article
- Review
- Novel approaches for the serodiagnosis of louse-borne relapsing fever.Frontiers in cellular and infection microbiology · 2022Article
- Article
- Interactions Between PathogenicFrontiers in cellular and infection microbiology · 2021Review
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Authors and funding
6 authors at 4 institutions in 3 countries.
Funding
Abstract
Borrelia miyamotoi, a relapsing fever spirochete transmitted by Ixodid ticks causes B. miyamotoi disease (BMD). To evade the human host´s immune response, relapsing fever borreliae, including B. miyamotoi, produce distinct variable major proteins. Here, we investigated Vsp1, Vlp15/16, and Vlp18 all of which are currently being evaluated as antigens for the serodiagnosis of BMD. Comparative analyses identified Vlp15/16 but not Vsp1 and Vlp18 as a plasminogen-interacting protein of B. miyamotoi. Furthermore, Vlp15/16 bound plasminogen in a dose-dependent fashion with high affinity. Binding of plasminogen to Vlp15/16 was significantly inhibited by the lysine analog tranexamic acid suggesting that the protein-protein interaction is mediated by lysine residues. By contrast, ionic strength did not have an effect on binding of plasminogen to Vlp15/16. Of relevance, plasminogen bound to the borrelial protein cleaved the chromogenic substrate S-2251 upon conversion by urokinase-type plasminogen activator (uPa), demonstrating it retained its physiological activity. Interestingly, further analyses revealed a complement inhibitory activity of Vlp15/16 and Vlp18 on the alternative pathway by a Factor H-independent mechanism. More importantly, both borrelial proteins protect serum sensitive Borrelia garinii cells from complement-mediated lysis suggesting multiple roles of these two variable major proteins in immune evasion of B. miyamotoi.
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