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Crystal structure of Lyme disease antigen outer surface protein A complexed with an Fab.

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Abstract

OspA (outer surface protein A) is an abundant immunogenic lipoprotein of the
Lyme disease spirochete Borrelia burgdorferi. The crystal structure of a soluble recombinant form of OspA was solved in a complex with the Fab fragment of mouse monoclonal antibody 184.1 and refined to a resolution of 1.9 A. OspA has a repetitive antiparallel beta topology with an unusual nonglobular region of "freestanding" sheet connecting globular N- and C-terminal domains. Arrays of residues with alternating charges are a predominant feature of the folding pattern in the nonglobular region. The 184.1 epitope overlaps with a well conserved surface in the N-terminal domain, and a hydrophobic cavity buried in a positively charged cleft in the C-terminal domain is a potential binding site for an unknown ligand. An exposed variable region on the C-terminal domain of OspA is predicted to be an important factor in the worldwide effectiveness of OspA-based vaccines.

Proc Natl Acad Sci U S A. 1997 Apr 15;94(8):3584-9. Research Support, Non-U.S. Gov’t; Research Support, U.S. Gov’t, Non-P.H.S.; Research Support, U.S. Gov’t, P.H.S.

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