Abstract
The outer surface protein C (OspC) is one of the major host-induced antigens of Borrelia burgdorferi, the causative agent of Lyme disease. We have solved the crystal structure of recombinant OspC to a resolution of 2.5 Å. OspC, a largely α-helical protein, is a dimer with a characteristic central four-helical bundle formed by association of the two longest helices from each subunit. OspC is very different from OspA and similar to the extracellular domain of the bacterial aspartate receptor and the variant surface glycoprotein from Trypanosoma brucei. Most of the surface-exposed residues of OspC are highly variable among different OspC isolates. The membrane proximal halves of the two long α-helices are the only conserved regions that are solvent accessible. As vaccination with recombinant OspC has been shown to elicit a protective immune response in mice, these regions are candidates for peptide-based vaccines.
Original language | English (US) |
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Pages (from-to) | 10010-10015 |
Number of pages | 6 |
Journal | Journal of Biological Chemistry |
Volume | 276 |
Issue number | 13 |
DOIs | |
State | Published - Mar 30 2001 |
ASJC Scopus subject areas
- Biochemistry
- Molecular Biology
- Cell Biology