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Scientists capture most detailed picture yet of key AIDS protein
Date:10/31/2013

ve inaccessibility of these neutralizing epitopes," Dr. Julien added. "It helps to know this for future vaccine design, but it also makes it clear why previous structure-based HIV vaccines have had so little success."

"We found that these neutralizing epitopes encompass features such as the variable loop regions and glycans that were excluded from previous studies of individual Env subunits," said Dmitry Lyumkis, first author of the electron microscopy study, who is a graduate student at TSRI participating in the NIH-funded National Resource for Automated Molecular Microscopy. "We observed, too, that neutralizing antibody binding to gp120 can be influenced by the neighboring gp120 structure within the trimer--another complication that was not apparent when we were not studying the whole trimer."

Having provided these valuable structural insights, the new Env trimer is now being put to work in vaccine development. "We and others are already injecting the trimer into animals to elicit antibodies," Dr. Ward said. "We can look at the antibodies that are generated and if necessary modify the Env trimer structure and try again. In this iterative way, we aim to refine and increase the antibody response in the animals and eventually, humans."


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Contact: Sarah Smith
sas2072@med.cornell.edu
646-317-7401
Weill Cornell Medical College
Source:Eurekalert

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