Characterization of surface antigen from Lyme disease spirochete Borrelia burgdorferi

被引:10
作者
Jones, K
Guidry, J
Wittung-Stafshede, P [1 ]
机构
[1] Tulane Univ, Mol & Cellular Biol Grad Program, New Orleans, LA 70118 USA
[2] Tulane Univ, Dept Chem, New Orleans, LA 70118 USA
关键词
lyme disease; Borrelia burgdorferi; surface antigen; circular dichroism; protein unfolding; differential scanning calorimetry;
D O I
10.1006/bbrc.2001.5983
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Borrelia burgdorferi, the Lyme disease spirochete, possesses a surface protein, VIsE (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 VIsE is immunodominant in Lyme-disease patients. Physicochemical analyses of pure recombinant VIsE yielded the following results: The protein appeared oligomeric in solution, with a secondary structure dominated by a-helices. Thermal denaturation (pH 7) probed by calorimetry involved two transitions: oligomer-to-monomer conversion (around 40 degreesC) followed by protein unfolding (55 +/- 1 degreesC). Chemical denaturation monitored by far-UV circular dichroism (20 degreesC, pH 7) sensed only polypeptide unfolding and took place in a single transition (DeltaG(U)(H2O) = 23 +/- 2 kJ/mol). VIsE did not adopt a native structure at pH 3; at pH 10 the stability was significantly reduced. Knowledge of biophysical properties of VIsE may aid in understanding the mechanism of VIsE antigenic variation in B. burgdorferi. (C) 2001 Elsevier Science
引用
收藏
页码:389 / 394
页数:6
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