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Borrelia burgdorferi, the
Lyme disease spirochete, possesses a surface protein, VlsE (variable major protein-like sequence, expressed), that undergoes antigenic variation. Unlike conserved regions of other proteins involved in antigenic variation, the most conserved invariable region of VlsE is immunodominant in
Lyme-disease patients. Physicochemical analyses of pure recombinant VlsE yielded the following results: The protein appeared oligomeric in solution, with a secondary structure dominated by alpha-helices. Thermal denaturation (pH 7) probed by calorimetry involved two transitions: oligomer-to-monomer conversion (around 40 degrees C) followed by protein unfolding (55 +/- 1 degrees C). Chemical denaturation monitored by far-UV circular dichroism (20 degrees C, pH 7) sensed only polypeptide unfolding and took place in a single transition (Delta G(U)(H(2)O) = 23 +/- 2 kJ/mol). VlsE did not adopt a native structure at pH 3; at pH 10 the stability was significantly reduced. Knowledge of biophysical properties of VlsE may aid in understanding the mechanism of VlsE antigenic variation in B. burgdorferi.