The antibody binds to sugars on the surface of HIV and effectively neutralizes the virus because of its unique structure, which is described in the latest issue of the journal Science.

"What we found was an unusual configuration of the antibody in which its two Fab domains -- the antigen recognition units -- are 'interdigitating' with each other," says TSRI Professor Ian Wilson, D.Phil., one of two TSRI professors who led the research. "Nothing like this has ever been seen before."

This new structure is an important step toward the goal of designing an effective vaccine against HIV, and it gives the researchers a new way to design antibodies in general.

"It may enable us to make antibodies that recognize whole new sets of molecules," says TSRI Professor Dennis Burton, Ph.D., the other TSRI professor who led the research.

The Problem of HIV and Antibodies

HIV causes AIDS by binding to, entering and ultimately, killing T helper cells, immune cells that are necessary to fight off infections by common bacteria and other pathogens. As HIV depletes the body of T helper cells, common pathogens can become potentially lethal.

The latest statistics are grim. The World Health Organization estimates that around 40 million people are living with HIV worldwide. During 2001 alone, more than four million men, women, and children succumbed to the disease, and by the end of that year, the disease had made orphans of 14 million children. In the United States, 40,000 people are infected with HIV each year.

One of the most compelling medical challenges today is to develop a vaccine that will provide complete prophylactic protection to someone who is late
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Contact: Jason Bardi
jasonb@scripps.edu
858-784-9254
Scripps Research Institute
26-Jun-2003