Collaborating¹ scientists at The Scripps Research Institute (TSRI) and Weill Cornell Medical College have determined² the first atomic-level structure of the tripartite（三重的） HIV envelope protein -- long considered one of the most difficult targets in structural³ biology and of great value for medical science. The new findings provide the most detailed⁴ picture yet of the AIDS-causing virus's complex envelope, including sites that future vaccines⁶ will try to mimic⁷ to elicit⁸（引起） 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 vaccine⁵," said Ian A. Wilson, the Hansen Professor of Structural Biology at TSRI, and a senior author of the new research with biologists Andrew Ward⁹ and Bridget Carragher of TSRI and John Moore of Weill Cornell.

 

The findings are published in two papers in Science Express, the early online edition of the journal Science, on October 31, 2013.

 

 

HIV, the human immunodeficiency virus, currently infects about 34 million people globally, 10 percent of whom are children, according to World Health Organization estimates. Although antiviral drugs are now used to manage many HIV infections, especially in developed countries, scientists have long sought a vaccine that can prevent new infections and perhaps ultimately eradicate¹⁰ the virus from the human population.

 

However, none of the HIV vaccines tested so far has come close to providing adequate protection. This failure is due largely to the challenges posed by HIV's envelope protein, known to virologists as Env.

 

Env's structure is so complex and delicate that scientists have had great difficulty obtaining the protein in a form that is suitable for the atomic-resolution imaging necessary to understand it.

 

"It tends to fall apart, for example, even when it's on the surface of the virus, so to study it we have to engineer it to be more stable," said Ward, who is an assistant professor in TSRI's Department of Integrative Structural and Computational Biology.

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