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Crystal structure of outer surface protein C (OspC) from the Lyme disease spirochete, Borrelia burgdorferi

  • D. Kumaran
  • , S. Eswaramoorthy
  • , B. J. Luft
  • , S. Koide
  • , J. J. Dunn
  • , C. L. Lawson
  • , S. Swaminathan
  • Brookhaven National Laboratory
  • University of Rochester
  • Rutgers - The State University of New Jersey, New Brunswick

Research output: Contribution to journalArticlepeer-review

100 Scopus citations

Abstract

Outer surface protein C (OspC) is a major antigen on the surface of the Lyme disease spirochete, Borrelia burgdorferi, when it is being transmitted to humans. Crystal structures of OspC have been determined for strains HB19 and B31 to 1.8 and 2.5 Å resolution, respectively. The three-dimensional structure is predominantly helical. This is in contrast to the structure of OspA, a major surface protein mainly present when spirochetes are residing in the midgut of unfed ticks, which is mostly β-sheet. The surface of OspC that would project away from the spirochete's membrane has a region of strong negative electrostatic potential which may be involved in binding to positively charged host ligands. This feature is present only on OspCs from strains known to cause invasive human disease.

Original languageEnglish
Pages (from-to)971-978
Number of pages8
JournalEMBO Journal
Volume20
Issue number5
DOIs
StatePublished - Mar 1 2001

Keywords

  • 3D structure
  • Lyme disease
  • OspC
  • X-ray diffraction

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