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Updated: Jun 12, 2026

Immuno-fluorescence Assay of Leptospiral Surface-exposed Proteins
Published on: July 1, 2011
BmpA is a surface-exposed outer-membrane protein of Borrelia burgdorferi
Anton V Bryksin1, Alexandra Tomova, Henry P Godfrey
1Department of Microbiology and Immunology, New York Medical College, Valhalla, NY 10595, USA.
Abstract:
BmpA is an immunodominant protein of Borrelia burgdorferi as well as an arthritogenic factor. Rabbit antirecombinant BmpA (rBmpA) antibodies were raised, characterized by assaying their cross reactivity with rBmpB, rBmpC and rBmpD, and then rendered monospecific by absorption with rBmpB. This monospecific reagent reacted only with rBmpA in dot immunobinding and detected a single 39 kDa, pI 5.0, spot on two-dimensional immunoblots. It was used to assess the BmpA cellular location. BmpA was present in both detergent-soluble and -insoluble fractions of Triton X-114 phase-partitioned borrelial cells, suggesting that it was a membrane lipoprotein. Immunoblots of proteinase K-treated intact and Triton X-100 permeabilized cells showed digestion of BmpA in intact cells, consistent with surface exposure. This exposure was confirmed by dual-label immunofluorescence microscopy of intact and permeabilized borrelial cells. Conservation and surface localization of BmpA in all B. burgdorferi sensu lato genospecies could point to its playing a key role in this organism's biology and pathobiology.
Insights
Borrelia burgdorferi
Area of Science:
- Microbiology
- Immunology
- Molecular Biology
Background:
- Borrelia burgdorferi (B. burgdorferi) is the causative agent of Lyme disease.
- BmpA is an immunodominant and arthritogenic protein of B. burgdorferi.
Purpose of the Study:
- To characterize the BmpA protein.
- To determine the cellular location of BmpA in B. burgdorferi.
Main Methods:
- Antibody production and characterization.
- Dot immunobinding and 2D immunoblots.
- Triton X-114 phase partitioning.
- Proteinase K treatment.
- Immunofluorescence microscopy.
Main Results:
- Monospecific antibodies confirmed BmpA as a single 39 kDa, pI 5.0 protein.
- BmpA was localized to both detergent-soluble and -insoluble cell fractions.
- BmpA was accessible to proteinase K digestion on intact cells, indicating surface exposure.
- Immunofluorescence confirmed surface localization of BmpA.
Conclusions:
- BmpA is a surface-exposed membrane lipoprotein in B. burgdorferi.
- The conserved surface localization suggests a critical role for BmpA in B. burgdorferi biology and pathogenesis.
- BmpA may be a potential target for diagnostic or therapeutic strategies against Lyme disease.
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