Crystal structure of Lyme disease antigen outer surface protein C from Borrelia burgdorferi | Academic Article individual record
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 A. 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.

author list (cited authors)
Eicken, C., Sharma, V., Klabunde, T., Owens, R. T., Pikas, D. S., Hook, M., & Sacchettini, J. C.
publication date
2001
keywords
  • Crystallography, X-Ray
  • Sequence Homology, Amino Acid
  • Bacterial Outer Membrane Proteins
  • Salmonella Typhimurium
  • Antigens, Bacterial
  • Animals
  • Borrelia Burgdorferi Group
  • Recombinant Proteins
  • Conserved Sequence
  • Trypanosoma Brucei Brucei
  • Protein Structure, Secondary
  • Protein Structure, Tertiary
  • Molecular Sequence Data
  • Aspartic Acid
  • Electrons
  • Peptides
  • Models, Molecular
  • Lyme Disease
  • Dimerization
  • Protein Conformation
  • Amino Acid Sequence
altmetric score

6.0

citation count

67