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

• DOI: 10.1074/jbc.m010062200
• Publication Date: 2002-07-26T15:08:15Z
• Authors: Christoph Eicken; Vivek Sharma; Thomas Klabunde; Rick T. Owens; Dagmar S. Pikas; Magnus Höök; James C. Sacchettini
• Keywords: Models, Molecular; Salmonella typhimurium; Antigens, Bacterial; Aspartic Acid; Lyme Disease; 0303 health sciences; Sequence Homology, Amino Acid; Protein Conformation; Molecular Sequence Data; Electrons; Crystallography, X-Ray; Protein Structure, Secondary; Recombinant Proteins; Protein Structure, Tertiary; 3. Good health; 03 medical and health sciences; Borrelia burgdorferi Group; Animals; Amino Acid Sequence; Peptides; Dimerization; Conserved Sequence; Bacterial Outer Membrane Proteins

The outer surface protein C (OspC) is one of the major host-induced antigens Borrelia burgdorferi, causative agent Lyme disease. We have solved crystal structure recombinant OspC to a resolution 2.5 A. OspC, largely alpha-helical protein, dimer with characteristic central four-helical bundle formed by association two longest helices from each subunit. very different OspA and similar extracellular domain bacterial aspartate receptor variant glycoprotein Trypanosoma brucei. Most surface-exposed residues are highly variable among isolates. membrane proximal halves long alpha-helices only conserved regions that solvent accessible. As vaccination has been shown elicit protective immune response in mice, these candidates for peptide-based vaccines.