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Researchers open door to new HIV therapy
Date:1/28/2014

rries attached CD4 receptors to the lysosome for destruction.

"The new high-resolution image reveals a cavity at the site where Nef binds to AP2, that could be a good site for drug targeting," Bonifacino said.

"This cavity on AP2 is not known to be used by any other host protein, so if we interfere with the cavity we are not going to interfere with any host cell function, only the function of Nef," he said. "This will inform better searches for inhibitors."

Hurley cautioned, however, that the research "needs more validation to prove that the cavity is a target. But we are excited because it is a potential target, and these things don't come along every day."

Taking a snapshot

UC Berkeley scientist Xuefeng "Snow" Ren obtained the high-resolution snapshot of Nef bound to AP2 by crystallizing the proteins and zapping the complex with X-rays. She calculated the 3-D structure from the resulting X-ray diffraction pattern. She is now at work crystallizing the Nef-AP2 complex bound to the CD4 receptor to look for other possible drug targets on AP2 or CD4 that could prevent Nef from trashing CD4.

Hurley and Bonifacino are primarily interested in the function of adaptors like AP2 there are at least five known adaptors in human cells that control intracellular membrane traffic.

"This work was an extension of our work on clathrin adaptors, an opportunity to do something relevant to fighting HIV that was based on the purely basic research we are doing on the sorting of proteins to lysosomes," Hurley said.


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Contact: Robert Sanders
rlsanders@berkeley.edu
510-643-6998
University of California - Berkeley
Source:Eurekalert  

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