“The complex protein is in the midst of so many studies a minute,” said co-director Donald Benton, a postdoctoral student at the Laboratory of Structural Disease Process Biology at the Francis Crick Institute in the UK. Understanding how it works “. is very important because it is the goal of maximum vaccination attempts and also of many diagnostic paints. “
To perceive the infection process, Benton and his team combined human ACE2 proteins with complex proteins in the lab. They then used a very bloodless liquid ethanol to temporarily freeze the proteins to “suspend in a special form of ice,” Benton told Live. They then placed these samples under a cryoelectronic microscope and received tens of thousands of high-resolution photographs of complex frozen proteins at other stages of ACE2 receptor binding.
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They found that complex protein undergoes shape adjustments when it is joined to the ACE2 receptor. After the first binding of the complex protein, its arrangement becomes more open to allow for greater binding (imagine how least difficult it would be to embrace someone if the complex protein eventually joins ACE2 at one of its 3 binding sites, revealing its “central core”, according to a statement. This final design probably allows the virus to fuse with moving membranes.
“It’s a very confusing receptor binding procedure to the maximum of complex viral proteins,” Benton said. “Influenza and HIV have an easier activation procedure. “The coronavirus is covered with complex proteins, and a small fraction of them are likely to disappear. through these conformal changes, they join human cells and infect them, Benton said.
“We know that the peak can adopt all those states we were talking about,” said co-director Antoni Wrobel, who is also a postdoctoral researcher at the Structural Disease Process Laboratory at the Francis Crick Institute. “But if each of the peaks adopts them all, we can’t say it because we can only see snapshots. “
The complex protein changes very quickly. In the lab, the beak can reach all those other conformations in less than 60 seconds, Wrobel told WordsSideKick. com. But “it will be very different in a genuine infection; everything will be slower because the receptor will stick to the surface of a cell, so we have to give time for the virus to spread to that receptor,” Benton said.
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Why does complex protein go through so many conformal adjustments to infect a cell?This “can be a way for the virus to recognize itself,” Benton said. When the complex protein is in its closed states, it hides the site that joins the receptor, perhaps to prevent the antibodies from entering and joining this site, he said.
But “it’s very difficult to tell,” Wrobel said. In any case, this study shows more surfaces in the complex protein that is exposed to infection, because another bureaucracy reveals surfaces that were once thought to be hidden. Researchers can then potentially expand vaccines to “Then we can start thinking about curative products that have compatibility somewhere on the surface of the receptor or somewhere in the peak itself that then act like drugs,” Wrobel told Live Science.
Wrobel and Benton hope to perceive why the coronavirus suffers so many conformal adjustments, how it compares to other coronaviruses, and whether those settings can help this new virus spread so easily.
The findings were published on September 17 in the journal Nature.
Originally on Live Science.