![]() ![]() But if I follow your reasoning, a focus on ACE2 proteins would be the closest yet to a front-end assault against the virus. As a layperson (sociology major) I find the very descriptions of these spikes (especially the illustrations) to be nauseating. But if one could produce such a recombinant protein in large amounts, and it is safe, it could provide a cure if it is present for sufficient duration to eliminate an active infection.Wow. However, creating such a "mimic" may not be so simple. Getting the spike to initiate these conformational changes before it can bind to the real receptor may severely limit its ability to infect cells and replicate. Perhaps using a soluble, inactive ACE2 "mimic protein" would trick the spike into latching on to a "dead-end receptor", preventing it from entering a cell. But if one could produce such a recombinant protein in large amounts, and it is safe, it could provide a cure if it is present for sufficient duration to eliminate an active infection.Ĭhem721 said:These are some very curious protein interactions. In any event, it is interesting, and spooky, that the spike undergoes such changes in order to deliver the viral genome. Based on the article, such regions are not usually exposed, except during the conformational changes which occur during binding - likely too late to promote antibodies, or prevent infection. Since the changes appear to occur only after contact with ACE2, it seems unlikely that a vaccine for those "hidden" regions of the spike would be viable. After the spike protein first binds, its structure becomes more open to allow for more binding." "They found that the spike protein undergoes shape changes as it binds to the ACE2 receptor. It seems unlikely that hiding from antibody responses is the reason for the conformational changes since, according to the article, the changes occur only after the spike has made contact with ACE2 and begins the changes to expose these new sites : When the spike protein is in its closed states, it hides the site that binds with the receptor, maybe to avoid antibodies coming in and binding to that site instead, he said." "Why does the spike protein go through this many conformational changes to infect a cell? It "may be a way of the virus protecting itself from recognition by antibodies," Benton said. These are some very curious protein interactions. When the spike protein is in its closed states, it hides the site that binds with the receptor, maybe to avoid antibodies coming in and binding to that site instead, he said. Why does the spike protein go through this many conformational changes to infect a cell? It "may be a way of the virus protecting itself from recognition by antibodies," Benton said. But "this will be very different in a real infection everything will be slower because the receptor will be stuck on the surface of a cell so you have to allow time for the virus to diffuse to this receptor," Benton said. In the lab, the spike can morph into all of these different conformations in less than 60 seconds, Wrobel told Live Science. The spike protein is very quick to change. ![]() "But whether each of the spikes adopts all of them we can't say because we can see only kind of snapshots." "We know that the spike can adopt all these states that we were talking about," said co-lead author Antoni Wrobel, who is also a postdoctoral research fellow at the Francis Crick Institute's Structural Biology of Disease Processes Laboratory. " Flu and HIV have a more simple activation process." The coronavirus is covered in spike proteins, and it's likely only a small fraction of them go through these conformational changes, bind to human cells and infect them, Benton said. "It's a very complicated receptor binding process compared to most virus spike proteins," Benton said. This final structure likely allows the virus to fuse to cell membranes. The spike protein eventually binds to ACE2 at all three of its binding sites, revealing it's "central core," according to a statement. After the spike protein first binds, its structure becomes more open to allow for more binding (imagine how much easier it would be to hug someone if they opened up their arms). They found that the spike protein undergoes shape changes as it binds to the ACE2 receptor. (Image credit: The Francis Crick Institute) The spike protein undergoes a handful of conformations as it binds to the ACE2 receptor that sits on the surface of some human cells.
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