A study shows that the Corona virus has ten types of...

A recent medical study concluded that a result may spoil scientists for all the efforts that they are currently making in order to eliminate the emerging corona virus and stop its spread among people, and this fact indicates that the virus has ten different types of proteins that perform the task of adhering to human cells, which means that they must Today scientists have overcome ten ways to attack the virus, not one or two.

According to the study, which was conducted in cooperation between a Chinese university and a research center in Britain, and its results were published on the “Life Science” website, scientists have found that the emerging corona virus has a “very complex” method to link itself with human cells.

Scientists discovered that the virus depends on what are called “spike proteins” in order to attach to and invade human cells, and to do so, the “spike” turns into at least 10 different forms to adhere to human cells.

The study was conducted by scientists from Sun Yat-sen University in China and the British “Francis Crick” Institute, which is the “former UK Center for Medical Research and Innovation” in London.

Scientists say that “while this may explain why it is difficult to find effective treatments for the disease, it also opens up potential new avenues for investigating a treatment or vaccine for Covid-19.”

At the start of the epidemic, scientists quickly determined the structure of the spike protein, which paved the way for its targeting with vaccines and other drugs. But there is still a lot scientists do not know about the interaction between the protein and the outer surface of human cells.

Co-lead author Donald Benton, a postdoctoral fellow at the Francis Crick Institute for Structural Biology of Disease Processes in Britain, said: “The spike protein is the focus of a lot of research at the moment. Understanding how it works is very important because it is the target of most vaccination attempts and a lot of diagnostic work. Also”.

To understand the infection process, Benton and his team mixed human “ACE2” proteins with “spike” proteins in the laboratory, then used ultra-cold liquid ethane to quickly freeze the proteins so that they “suspended in a special form of ice,” according to Benton.

Then they placed these samples under a cryogenic electron microscope and obtained tens of thousands of high-resolution images of the frozen proteins that are different stages of attachment to a human cell.

They found that the spike protein that is produced by the Corona virus undergoes changes in shape when it binds to the human cell, and after the protein binds, its structure becomes more open to allow more attachment, which increases the spread of the disease and facilitates the transmission of the virus through these proteins.

“It’s a very complex receptor binding process compared to most spike proteins in the virus,” Benton said. “Influenza and HIV have a simpler activation process.” He added that the Corona virus is covered with spike proteins, and it is possible that only a small part of it goes through these harmonic changes, binds to human cells and infects them.

Co-lead author Anthony Roble, who is also a postdoctoral research fellow at the Francis Crick Institute for Structural Biology of Disease Processes, noted: “We know that spike protein can adopt all of these states that we have been talking about. But if all the spike proteins depend on them all, we cannot. Specify that, because we can only see one type of snapshot. ”

The researchers say the spike protein is rapidly changing in the laboratory, and can transform into all these different configurations in less than 60 seconds. But Benton explained that: “This will be completely different in the case of real infection, everything will be slower because the receptor will be stuck on the surface of the cell, so you have to allow time for the virus to spread to this future.”

“This may be a way for the virus to protect itself from the antibodies that recognize it,” he said. He added that when the spike protein is in its closed state, it hides the site that binds to the receptor, which is the human cell, perhaps to avoid entering the antibodies and binding to that site instead.

The team noted that the changing shape of the spike protein revealed more surfaces that could be targeted by vaccines and potential drugs.

“We can then start thinking about treatments that could fit somewhere either on the surface of the receptor or somewhere in the spike protein itself,” Roble says.

Scientists hope to know why the coronavirus has gone through many harmonic changes, how it compares to other coronaviruses, and whether these changes may help explain why this new virus spreads so easily.