[ad_1]
Researchers have found a new way to target influenza viruses.
There is a hitch in the sway of a protein that transmits the flu virus. Researchers at Rice University and Baylor College of Medicine believe that this mechanism could be a useful target to prevent the virus from infecting cells.
The article begins to define the mechanism that allows the protein to unfold and fold in the blink of an eye, changing its shape to expose a peptide that attaches the virus to a cell and begins l & # 39; infection.
"This protein starts in a collapsed state and goes through a global transformation, retreating into a completely different state," said Onuchic, co-director of The Center for Theoretical Biological Physics of Rice (CTBP). . "But there is a small part at the center that evolution has kept."
This single preserved amino acid residue is the hitch that causes the protein to pause in the folding process. It allows a fusion peptide buried inside to bind to the target cell and begin to infect it.
Without the pause, the folding would be too fast for the link to take place.
Onuchic added: "We have discovered that there is a heap of energy that makes the final state of HA2 much more stable than the initial state. But with the spring mechanism, most of the energy would already be wasted by the time it forms -coiler and binds the cell and viral membranes. "
The conservative hydrophilic (attracting) residue, known as Thr59, is known as a particular interest to researchers not only for the way it disrupts the folding and allows the virus to attack, Xingcheng Lin, senior author and postdoctoral researcher on rice, said: "Current research has focused on the group that incorporates Thr59 and causes the H3N2 strain responsible for the Hong Kong flu. "
(19659002) Health, Flu, Virus, Rice University, Rice University, Baylor College of Medicine, Proceedings of the National Academy of Sciences, Center of Theoretical Biology. al Physics
Source link
