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Originally published In Press as doi:10.1074/jbc.M010062200 on January 3, 2001

J. Biol. Chem., Vol. 276, Issue 13, 10010-10015, March 30, 2001
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Crystal Structure of Lyme Disease Antigen Outer Surface Protein C from Borrelia burgdorferi*

Christoph EickenDagger §, Vivek SharmaDagger §, Thomas KlabundeDagger §, Rick T. Owens||**, Dagmar S. Pikas||, Magnus Höök||, and James C. SacchettiniDagger §Dagger Dagger

From the Dagger  Department of Biochemistry & Biophysics, Texas A&M University, College Station, Texas 77843-2128 and § The Center for Structural Biology, Albert B. Alkek Institute of Biosciences and Technology, Houston, Texas 77030-3303 and || The Center for Extracellular Matrix Biology, Texas A&M University System Health Science Center, Albert B. Alkek Institute of Biosciences and Technology, Houston, Texas 77030-3303

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 alpha -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 alpha -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.

* This work was supported by the Welch Foundation, the National Institutes of Health, and the Wenner-Gren Foundations, Sweden.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The atomic coordinates and the structure factors (code 1G5Z) have been deposited in the Protein Data Bank, Research Collaboratory for Structural Bioinformatics, Rutgers University, New Brunswick, NJ (http://www.rcsb.org/). .

Present address: Aventis Pharma Deutschland GmbH, Chemical Research-Molecular Modeling, Bldg. G838, D-65926 Frankfurt am Main, Germany.

** Present address: LifeCell Corp., One Millenium Way, Branchburg, NJ 08876.

Dagger Dagger To whom correspondence should be addressed. Tel.: 1-979-8627636; Fax: 1-979-8627638; E-mail: sacchett@tamu.edu.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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