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Scientists explain binding action of 2 key HIV antibodies; could lead to new vaccine design

A very close and detailed study of how the most robust antibodies work to block the HIV virus as it seeks entry into healthy cells has revealed a new direction for researchers hoping to design an effective vaccine.

"Our study clearly showed that we've been overlooking a very important component of antibody function," says S. Munir Alam, Ph.D., an associate professor of medicine at Duke University Medical Center and lead author of the paper appearing in the Proceedings of the National Academy of Sciences.

Alam, a member of the Duke Human Vaccine Institute and study senior author Bing Chen, Ph.D., assistant professor of pediatrics, Harvard Medical School and Children's Hospital Boston, studied two potentially powerful antibodies against HIV, 2F5 and 4E10. Both of these are rare, broadly neutralizing antibodies, meaning that they can block a number of different strains of the HIV virus. They accomplish that by binding to the "Achilles heel" of the virus – the so-called outer coat membrane proximal region – a part of the outer protein coating next to the viral membrane that opens up and is exposed to the antibodies for just a few minutes during the process of cell fusion and infection.
 
 

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