Open AccessBmpA is a surface‐exposed outer‐membrane protein of Borrelia burgdorferi
Author(s) -
Bryksin Anton V.,
Tomova Alexandra,
Godfrey Henry P.,
Cabello Felipe C.
Publication year - 2010
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.2010.02020.x
Subject(s) - borrelia burgdorferi , biology , microbiology and biotechnology , proteinase k , bacterial outer membrane , immunofluorescence , antibody , biochemistry , escherichia coli , immunology , enzyme , gene
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.