Viruses are cellular parasites that reproduce themselves by hijacking the machinery of the cells they infect. We have significant knowledge regarding cell infection and virus reproduction of themselves within cells, but scarce is our understanding of the final stages of protein folding and virus construction. However, according to SciTechDaily, researchers at Children’s Hospital of Pittsburgh of UPMC and the University of Pittsburgh School of Medicine have published a report in Nature Microbiology revealing how the proteins of the common, normally harmless reovirus, are properly folded by the cell to produce the final viruses.
The key is the common chaperonin protein complex, TriC. A given protein can potentially fold multiple ways, but the chaperonins help proteins in the cell to fold properly. In fact, it helps fold up to 10% of all the cell’s proteins, including important proteins such as cellular cytoskeleton proteins and cell cycle regulators. TriC is highly conserved across species, indicating its importance in proper protein folding and function. This conserved structure also suggests that TriC might be a common protein for viruses to use.
The TriC helps the reovirus’s outer capsid proteins to fold such that they can assemble into virus particles capable of being released from the cell to infect new cells. Given the central role of TriC in properly folding reovirus proteins, scientists may find ways to inhibit the folding process. However, given the central importance of TriC as a chaperonin for 10% of the cell’s proteins, therapies must be conducted carefully to avoid damage to the cells themselves.
Whether new therapies can be developed or not, understanding the roles of chaperonins like TriC is an important step to understanding the virus lifecycle. The more we understand about how viruses take over the cellular structure, the closer we are to understanding how to therapeutically fight these miniscule cellular parasites.