Structure of key HIV protein solved, offers hope to millions of HIV/AIDS patients

Views of the integrase enzyme bound to viral DNA and to the integrase inhibitors MK0518 and GS9137 (b and c).

By Liz H.

After nearly 4 years and 40,000 trials, a team of researchers from Harvard University and Imperial College London has reported the structure of the HIV enzyme integrase in a landmark study published in the January 31st issue of Nature (full article).  Integrase is a key retroviral enzyme that allows the virus to insert its DNA into the chromosomes of host cells and replicate. This discovery sheds light on how current integrase inhibitors target the enzyme and may lead to the development of more effective therapeutics.

Scientists grew a crystal of the enzyme obtained from the Prototype Foamy Virus, a model for HIV, and used a synchotron machine at the Diamond Light Source in South Oxfordshire to take a picture of the enzyme’s structure using a method known as x-ray diffraction.  These crystals were then soaked in integrase inhibitors and the drugs’ actions were also studied using x-ray diffraction.  Scientists hope that their findings will allow them to develop improved next-generation integrase inhibitors.

Over 33 million people are infected by HIV and combination antiretroviral therapy (ART) is used to slow the progression of disease (source). However, the increasing prevalence of multi-drug resistance, high cost, and side effects of therapeutics undermines the efficacy of current treatments.

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