Crystal Structure of Lyme Disease Antigen Outer Surface Protein C from Borrelia burgdorferi

Christoph Eicken, Vivek Sharma, Thomas Klabunde, Rick T. Owens, Dagmar S. Pikas, Magnus Höök, James C. Sacchettini

    Research output: Contribution to journalArticlepeer-review

    80 Scopus citations

    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 languageEnglish (US)
    Pages (from-to)10010-10015
    Number of pages6
    JournalJournal of Biological Chemistry
    Volume276
    Issue number13
    DOIs
    StatePublished - Mar 30 2001

    ASJC Scopus subject areas

    • Biochemistry
    • Molecular Biology
    • Cell Biology

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