Abstract
The cloning, expression and molecular characterization of a novel polymorphic B. burgdorferi lipoprotein recognized by monoclonal antibody LA7 is described. lpLA7 shows sequence similarity with other prokaryotic lipoproteins, including the immunodominant B. burgdorferi outer surface proteins OspA, OspB, OspC and OspD.
Upon solubilization of intact B. burgdorferi with the non-ionic detergent Triton X-114, lpLA7 was extracted together with other lipoproteins into the detergent phase. Indirect immuno-labeling studies indicated that the epitope recognized by mAb LA7 is mainly localized to the periplasmic space. Two dimensional gel electrophoresis and immuno-blotting confirmed the calculated acidic pI of 5.7 for 1pLA-7. The LA7 gene is shown to be species specific and to be located on the linear chromosome of B. burgdorferi. The analysis of 40 individual spirochetal isolates by restriction fragment length polymorphism analysis revealed a considerable genotypic heterogeneity of LA7 corresponding to that previously found for OspA.
Native and recombinant lpLA-7 were recognized by immune sera from infected mice as well as some human sera and may also prove useful as an additional marker for serodiagnosis of Lyme disease.
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Wallich, R., Helmes, C., Schaible, U.E., Kramer, M.D., Simon, M.M. (1994). Biochemical and Immunological Analysis of a Polymorphic Low-Molecular-Weight Lipoprotein of Borrelia Burgdorferi . In: Axford, J.S., Rees, D.H.E. (eds) Lyme Borreliosis. NATO ASI Series, vol 260. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-2415-1_37
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DOI: https://doi.org/10.1007/978-1-4615-2415-1_37
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