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Stanford biochemist Christopher Barnes, the structures of viruses and immune formula proteins, and how they interact.
Stanford University.
In January 2020, Caltech biochemist Pamela Bjorkman asked volunteers to help the structures of immune proteins that attack a newly discovered coronavirus. The pathogen originated in China and was causing severe pneumonia-like symptoms in inflamed people. Knowing the molecular arrangements of those antibodies would be a vital step toward the emergence of drugs to fight the virus.
Christopher Barnes, a postdoc working in Bjorkman’s lab on the design of HIV and the antibodies that attack it, seized the possibility of solving a new riddle. “I like it, ‘Oh, I’m going to do it!'” says Barnes. At that time, he didn’t know how pressing the studies would become.
We now know very well about SARS-CoV-2, which causes COVID-19 and has killed more than 6 million people worldwide. Studies on the structure of the virus and the antibodies that attack it have helped scientists develop vaccines and treatments that have stored tens of millions of lives. But the virus continues to adapt, changing the spike protein it uses to enter cells. This has left researchers scrambling for new drugs and updated vaccines.
Using high-resolution imaging techniques, Barnes investigates the complex proteins of the coronavirus and the antibodies that attack them. Their goal: to find a persistent weak spot and exploit it to create a vaccine that works in the opposite way to all coronaviruses.
Barnes’ team used cryo-electron microscopy to reveal the structures of 8 antibodies that close the original edition of SARS-CoV-2. The strategy captures cells, viruses and proteins that do their job by freezing them instantly. In this case, the team moved traces of coronavirus connected to immune-formula proteins away from other people with COVID-19.
The antibodies had four problems in the spike protein receptor binding domain, or RBD, the team reported in Nature in 2020. This finger-shaped region anchors the virus to the mobile device it will infect. When the antibodies bind to RBD, the virus can no longer attach to the mobile.
This symbol shows the three-dimensional molecular design of an antibody blocked in a spike protein on the surface of the virus that causes COVID-19. The binding domain of the receiver is represented in tanning.
Barnes’ team also created an antibody classification formula based on the RBD location where immune formula proteins tend to attach. “This has been very useful in understanding the types of antibody responses caused by an herbal infection,” says structural biologist Jason McLellan, who are not involved in the work, and in identifying the main applicants for drug development.
“One of Chris’ main strengths is that he doesn’t restrict himself or his studies to a single technique,” says McLellan, of the University of Texas at Austin. “It temporarily adapts and integrates new technologies to answer questions in the field. “
Since opening his own lab at Stanford, Barnes and his colleagues have decided on the six-antibody structures that attack the original SARS-CoV-2 virus and the delta and omicron variants. These variants are adept at evading antibodies, adding those manufactured in the lab and administered to patients to treat COVID-19. The newly known antibodies, described June 14 in Immunity, target the N-terminal domain of the spike protein. The structures of the sites where proteins bind are the same in delta and omicron, suggesting that sites may also remain unchanged even in long-term variants, the team explains. Eventually, scientists could possibly mass-produce antibodies that target those sites for use in new therapies.
Barnes has now turned his attention to antibodies that can repel all coronaviruses, from those that cause colds to those found in livestock and other animals that have the potential to spread to humans.
Barnes and immunologist Davide Robbiani of the University of Lugano in Switzerland have known categories of antibodies that target variants of the 4 coronavirus families, blocking the ability of viruses to fuse with cells.
In addition, the design of one of the binding sites in the spike protein is the same in the coronavirus circle tree, Barnes says. an essential component of how you enter the cell. “
Two independent groups know of an action on the same categories of antibodies. Taken together, the effects suggest a universal coronavirus vaccine is possible, Barnes says.
“We all discovered this at the same time,” he says. The teams are now like, “Wow, it exists. So let’s try to make a genuine vaccine against the coronavirus. “
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An edition of this article appears in the October 8, 2022 issue of Science News.
C. Dacon et al. The antibodies, largely neutralizing, target the coronavirus fusion peptide. Science. Published online July 12, 2022. doi: 10. 1126/science. abq3773.
J. Siung Low et al. The ACE2 bond exposes the SARS-CoV-2 fusion peptide to broadly neutralizing anti-coronavirus antibodies. Science. Published on July 12, 2022. doi: 10. 1126/science. abq2679.
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Z. Wang et al. Memory B-cell research identifies neutralizing epitopes conserved in the N-terminal domain of SARS-Cov-2 peak protein variants. Immunity. Vol. 55, June 14, 2022, p. 998.
Co. Barnes et al. SARS-CoV-2 neutralizing antibody structures count healing strategies. Nature. Vol. 558, December 24, 2020, p. 682.
Cassie Martin is an associate editor. He holds a bachelor’s degree in molecular genetics from Michigan State University and a master’s degree in science journalism from Boston University.
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