ArticlemBio2023
Structural Elucidation of a Protective B Cell Epitope on Outer Surface Protein C (OspC) of the Lyme Disease Spirochete, Borreliella burgdorferi.
Article in mBio, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
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Who cites it
8 citing papers in PubMed, 12 citations in OpenAlex.
- Machine learning-driven identification of virulence determinants in Borrelia burgdorferi associated with human dissemination.PLoS computational biology · 2026Article
- Monovalent and multivalent OspA mRNA-LNP vaccines elicit functional antibodies and protect against Borrelia burgdorferi in mice.NPJ vaccines · 2026Article
- Broadly conserved protective epitopes on the lyme disease vaccine antigen, OspA.PLoS pathogens · 2026Article
- An Fc-silent OspA monoclonal antibody passively protects mice from tick and intradermal Borrelia burgdorferi challenge.PloS one · 2026Article
- A type-specific B-cell epitope at the apex of outer surface protein C (OspC) of the Lyme disease spirochete,Microbiology spectrum · 2025Article
- Germline encoded residues dominate the interaction of a human monoclonal antibody with decorin binding protein A ofFrontiers in immunology · 2025Article
- Antibody-mediated immunological memory correlates with long-term Lyme veterinary vaccine protection in mice.Vaccine · 2024Article
- A Refined Human Linear B Cell Epitope Map of Outer Surface Protein C (OspC) From the Lyme Disease Spirochete,Pathogens & immunity · 2024Article
Corrections and comments
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Authors and funding
12 authors at 5 institutions in 1 country.
Funding
Abstract
Outer surface protein C (OspC) plays a pivotal role in mediating tick-to-host transmission and infectivity of the Lyme disease spirochete, Borreliella burgdorferi. OspC is a helical-rich homodimer that interacts with tick salivary proteins, as well as components of the mammalian immune system. Several decades ago, it was shown that the OspC-specific monoclonal antibody, B5, was able to passively protect mice from experimental tick-transmitted infection by B. burgdorferi strain B31. However, B5's epitope has never been elucidated, despite widespread interest in OspC as a possible Lyme disease vaccine antigen. Here, we report the crystal structure of B5 antigen-binding fragments (Fabs) in complex with recombinant OspC type A (OspC
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.