News from Argonne National Laboratory
November 14, 2013
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The first atomic-level structure of the tripartite HIV (human immunodeficiency virus) envelope protein—long considered one of the most difficult targets in structural biology and of great value for medical science—has been determined by scientists using data obtained at three synchrotron x-ray light sources including the U.S. Department of Energy (DOE) Office of Science’s Advanced Photon Source.
The structure of the human immunodeficiency virus envelope protein, shown here bound by broadly neutralizing antibodies against two distinct sites of vulnerability. (Courtesy of The Scripps Research Institute)
The new findings provide the most detailed picture yet of the acquired immune deficiency syndrome (AIDS)-causing virus’s complex envelope, including sites that future vaccines will try to mimic to elicit a protective immune response.
“Most of the prior structural studies of this envelope complex focused on individual subunits; but we’ve needed the structure of the full complex to properly define the sites of vulnerability that could be targeted, for example with a vaccine,” said Ian A. Wilson of The Scripps Research Institute (TSRI) and a senior author of the new research that included colleagues from TSRI; Weill Cornell Medical College; the Ragon Institute of MGH, MIT, and Harvard; and the Academic Medical Center (The Netherlands). The findings were published in two papers in Science Express, the early online edition of the journal Science, on October 31, 2013.
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The Advanced Photon Source at Argonne National Laboratory is one of five national synchrotron radiation light sources supported by the U.S. Department of Energy’s Office of Science to carry out applied and basic research to understand, predict, and ultimately control matter and energy at the electronic, atomic, and molecular levels, provide the foundations for new energy technologies, and support DOE missions in energy, environment, and national security.
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