Scientists watch how a large HIV protein activates its replication

Understanding how HIV replicates inside cells is key to developing new treatments. Group

scientists from the Salk Institute and UniversityRutgers was the first to determine the molecular structure of the pol protein of the HIV virus. It plays a key role in the later stages of HIV replication, the process by which the virus multiplies and spreads throughout the body. So scientists discovered a new vulnerability in the virus that can be affected with drugs.

The pol gene, a polyprotein, is split into threeenzymes—protease, reverse transcriptase, and integrase—that work together to assemble the mature form of the virus. The protease plays a critical role in initiating this process by cutting the molecule into other components. But previously, scientists did not know how the protease itself is released (first from the larger HIV gag-pol polyprotein, and then from HIV Pol) to perform this task. In the new paper, the scientists suggested that the protease initiates the process by self-cleaving, separating itself from the rest parts of the molecule, using reverse transcriptase and possibly integrase.

During the study, scientists usedcryogenic electron microscopy (an imaging technique) to reveal the three-dimensional structure of the pol protein molecule. This is how biologists realized that pol is a dimer, that is, it is formed by two proteins bound together. This surprised scientists - other similar viral proteins are single-protein assemblies.

Moreover, in this two-way structurethe protease component pol is loosely bound to the reverse transcriptase component. Based on the new data, scientists are studying the structures of the larger and more complex gag-po polyprotein. He is also involved in the assembly of the virus. The experts will also study the role of integrase in the assembly of the mature form of the HIV virus during replication.

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