UPTON, NY A research team working at the U.S. Department of Energys Brookhaven National Laboratory has determined the three-dimensional structure of a key protein on the bacterium that causes Lyme disease. Called OspC, the protein is derived from two strains of the Lyme disease bacterium. This research may lead to a second-generation vaccine that would be more effective than the current one.
The current vaccine is based on another Lyme disease protein, known as OspA, which was previously deciphered at Brookhaven. Both OspA and OspC are outer surface proteins of Borrelia burgdoferi, the bacterium that causes Lyme disease. Researchers from Brookhaven Lab, Stony Brook Universitys School of Medicine, the University of Rochester Medical Center and Rutgers University will report their findings on the structure of OspC in the March 1, 2001 edition of The EMBO Journal.
Spread by the bite of an infected deer tick, Lyme disease is the most common vector-borne disease in the U.S. Between 1982 and 1996, more than 99,000 cases were reported in the nation. Early symptoms of the disease include a bulls-eye rash and flu-like symptoms. If the disease is not promptly treated with antibiotics, more serious symptoms, including joint and neurological complications, may develop.
To determine the structure of OspC, the researchers used a technique at Brookhavens National Synchrotron Light Source (NSLS) known as multiple wavelength anomalous diffraction. First, researchers grew crystals of the protein that could withstand the intense x-rays at the NSLS. To make large quantities of OspC, the team used the T7 gene-expression system, which was developed at Brookhaven.
Then the crystal was illuminated with beams of x-rays at different energies, and diffraction patterns were recorded on a detector. With the aid of powerful computers, the researchers then analyzed the diffraction patterns to gain the vital information needed to create an image of the protein
Contact: Diane Greenberg
DOE/Brookhaven National Laboratory