| Autor: |
Jones K; Molecular and Cellular Biology Graduate Program, Tulane University, New Orleans, Louisiana, 70118-5698, Guidry J, Wittung-Stafshede P |
| Jazyk: |
angličtina |
| Zdroj: |
Biochemical and biophysical research communications [Biochem Biophys Res Commun] 2001 Nov 30; Vol. 289 (2), pp. 389-94. |
| DOI: |
10.1006/bbrc.2001.5983 |
| Abstrakt: |
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. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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