Journal
EMBO JOURNAL
Volume 20, Issue 5, Pages 971-978Publisher
WILEY
DOI: 10.1093/emboj/20.5.971
Keywords
Lyme disease; OspC; 3D structure; X-ray diffraction
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Funding
- NIAID NIH HHS [AI37256] Funding Source: Medline
- NINDS NIH HHS [P01-NS34092-01A2] Funding Source: Medline
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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 Angstrom 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 P-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.
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