Researchers have worked on this for 20 years
Being a virus, HIV cannot replicate on its own, and needs a host cell in order to produce more copies of itself. So, when it enters a human cell, for example, it hijacks the genetic mechanisms at work inside, and makes them produce more viral agents. It therefore needs to paste a copy of its genetic material into the genome of the cell, and the way it does that is via an enzyme called integrase. What the ICL team did was grow a crystal that revealed the structure of integrase. This could help molecular biologists create drugs that are targeted at this enzyme directly, a completely new approach to treating HIV.
“It is a truly amazing story. When we started out, we knew that the project was very difficult, and that many tricks had already been tried and given up by others long ago. Therefore, we went back to square one and started by looking for a better model of HIV integrase, which could be more amenable for crystallization. Despite initially painstakingly slow progress and very many failed attempts, we did not give up and our effort was finally rewarded,” ICL Department of Medicine expert Dr. Peter Cherepanov says. He has also been the lead author of the Nature paper.
The investigation was conducted over a period of four years, during which time more than 40,000 trials were attempted. Of these trials, just seven resulted in usable crystals. These materials are absolutely essential for studying molecules. The enzyme was collected from a type of retrovirus known as the Prototype Foamy Virus (PFV). In this organism, the integration processes and functions of integrase are roughly the same as the ones in HPV, the researchers say. They add that the final data showed that the enzyme had a very different structure than the one proposed through the theoretical model. The new data will soon help inform on new drug-design efforts.
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