Health
UCSD researchers have discovered a SARS-CoV-2 “gate” that causes infection
San Diego (CNS)-In a study published Thursday, a team led by researchers at the University of California, San Diego, said that glycans, the molecules that make up glycans around the ends of peaplomers, are the gateway to SARS infection. I found how it works-a virus that causes CoV-2, COVID-19. This can be the key to combating the virus.
Since the early days of the COVID pandemic, scientists have been actively pursuing the secrets of the mechanisms that allow the virus to invade and infect healthy human cells.
Early in the pandemic, computational biophysical chemist Rommie Amaro of UCSD helped develop a detailed visualization of the SARS-CoV-2 peaplomer that efficiently latches on cell receptors.
It was published in the journal “Nature Chemistry” on Thursday. This research is led by Amaro, co-chief author Lillian Chong of the University of Pittsburgh, lead author and UCSD graduate student Terra Stain, and co-lead author and UCSD postdoctoral fellow Surl-Hee Ahn. Describes the discovery of a glycan “gate” that opens to allow SARS-CoV-2 entry.
“We essentially understood how spikes actually open and infect,” said Amaro, a professor of chemistry and biochemistry and a senior author of new research. “We have unveiled an important secret about how spikes infect cells. Without this gate, the virus is basically infectious.”
Amaro said he believes the discovery of the research team’s gates opens up potential new therapies to combat SARS-CoV-2 infection. The ability to pharmacologically “lock” the glycan gate in a closed position can effectively prevent the virus from opening and invading or infecting.
Spike’s glycan coating helps deceive the human immune system as it is just a residue of glycans. Previous techniques for imaging these structures depicted glycans in static open or closed positions, but were initially of little interest from scientists. Supercomputing simulations have since allowed researchers to develop dynamic “movies” that reveal glycan gates that activate from one position to another, providing an unprecedented infection story. rice field.
“We were able to actually see the opening and closing,” Amaro said. “This is one of the great features these simulations offer and you can watch very detailed movies.
“If you look at them, you’ll notice that you’re looking at something that you would otherwise have ignored,” she continued. “If you look only at the closed structure and then at the open structure, it doesn’t look special. You can see that it’s actually performing that function because you’ve captured a movie of the entire process. . “
The simulation was first run at UCSD’s San Diego Supercomputer Center “Comet” and then at the University of Texas at Austin “Longhorn”. Such computational power provided researchers with an atomic-level view of the peplomer-receptor-binding domain (RBD) from more than 300 perspectives. Research has revealed the glycan “N343” as a linchpin that allows access to host cell receptors by prying RBD from “bottom” to “top” positions. Researchers describe glycan activation as similar to a “molecular clover” mechanism.
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