In a new study, the scientists' method shows that the lattice that forms the main structural
When HIV particles grow from an infectedcells, viruses are retained before they become infectious. Protease, an enzyme that is embedded as half a molecule in the GagPol proteins, must bind to other similar molecules in a process called dimerization. This triggers the maturation of the virus, resulting in the appearance of infectious particles. No one knows how these semi-protease molecules find each other and dimerize, but this may be due to the rearrangement of the lattice formed by the Gag and GagPol proteins, which lie only inside the viral envelope. Gag is a major structural protein and has been shown to be sufficient for the assembly of virus-like particles. Gag molecules form a lattice hexagonal structure where the particles intertwine with themselves. The gaps between them are minimal. The new method showed that the Gag lattice is not static.
The new method is one step ahead thanks tothe use of microscopy, which traditionally provides only static information. In addition to new microscopic techniques, the scientists used a mathematical model and biochemical experiments to test lattice dynamics. Apart from the virus, the main effect of the method is that researchers can see how molecules move around the cell. The study of any biomedical structure has become more accessible.
This is the first study to show thatthe structure of the protein lattice of the virus in the envelope is dynamic. The new tool will be important to better understand the changes taking place in the lattice as new viral particles move from immaturity to dangerously infectious.
What are the molecular mechanisms that lead toinfections? This opens up a new area of research. If you can understand the process, you might be able to do something to prevent them from finding each other, such as a medicine that will stop the virus.
Ipsita Saha, graduate student researcher in the Department of Physics and Astronomy at Utah State University
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