In a finding that unlocks new doors to devising drugs and vaccines against HIV,
scientists have crystallized the core of gp120, the surface protein molecule
that the virus uses to attach itself to immune system cells.
The new model of the gp120 core's crystal structure reveals specific targets for
anti-HIV vaccines and drugs, and highlights the surprising array of defenses
that the virus uses to evade attack.
"Studying the gp120 crystal's structure can tell us a lot more about how the
virus locks on to immune system cells," says Anthony S. Fauci, M.D., director of
the National Institute of Allergy and Infectious Diseases (NIAID). "We now have
specific target sites on which to focus in developing new drugs and vaccines."
The research, funded in part by NIAID, comes from a team led by Joseph G.
Sodroski, M.D., of the Dana-Farber Cancer Institute, Harvard Medical School,
Boston, Mass., and Wayne Hendrickson, Ph.D., of Columbia University College of
Physicians and Surgeons, New York, N.Y. Their work appears in the June 18,
1998, issue of Nature and the June 19, 1998, issue of Science.
The scientists confirmed several previously known features but also found some
surprises in the crystal structure of the protein. "We discovered that a large
part of the gp120 surface is protected against attack by a dense array of
carbohydrates and by an amazing capacity to change shape," says Dr. Sodroski.
Among their findings were:
- A shape-shifting device that allows gp120 to shield itself from antibodies
until it reaches CD4 receptor sites on the immune system's T-cells - the first
step in hijacking these cells. Loop-shaped projections that stick out above the
molecule's surface hide the critical locking regions. When the virus reaches
its target, the loops collapse and move out of the way, unmasking the locking
- An icing of carbohydrate molecules that also shields the receptor-binding
regions of the gp120 surface from a
Contact: June Wyman
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