Scientists from Weill Cornell Medicine, the University of Wisconsin-Madison, Scripps Research, and the University of Chicago have led a team that has discovered an antibody that appears to prevent infection by all dominant versions of the COVID-19 virus, including the most recent one, Omicron. Their discovery might result in new antibody-based therapies and more effective immunizations.
Dr. Patrick Wilson, the Anne E. Dyson Professor of Pediatric Research and a member of the Gale and Ira Drukier Institute for Children’s Health at Weill Cornell Medicine, and his colleagues tested antibodies made from patient blood samples against different strains of the virus that surfaced during the pandemic in a study that was published on March 6 in the Journal of Clinical Investigation. One of these proteins, designated S728-1157, proved to be quite successful in neutralizing seven different subtypes of Omicron in addition to older forms.
The SARS-CoV-2 virus, which causes COVID-19, acquires additional mutations as it replicates in the cells of the people it infects. These modifications serve as the starting point for new varieties, some of which are capable of partially dodging the vaccinations and antibody-based therapies created to combat the original virus. Even though numerous variants have emerged, only a small number of them have the potential to have a substantial global impact on infections. Omicron, which debuted in November 2021, is one among them. One of its varieties, called XBB.1.5, has prevailed in the US as of mid-March.
Dr. Maria Lucia Madariaga, an assistant professor of surgery at the University of Chicago, took blood samples from COVID-19 patients early in the pandemic, before the variations appeared. The immune system produces proteins called antibodies in reaction to the virus that binds to specific regions of the pathogen, preventing it from infecting cells and activating the immune system to kill it.
The antibody-producing cells in these samples were examined by Dr. Wilson’s team for their ability to bind to the virus’s spike protein, which is used by the virus to enter human cells. Dr. Siriruk Changrob, co-first author and a pediatric immunology lecturer in his lab, tested the antibodies they discovered against 12 SARS-CoV-2 variations, including the original strain of the virus.
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One particular antibody, designated S728-1157, stood out for its capacity to obstruct Omicron. Researchers from the University of Wisconsin-Madison School of Veterinary Medicine discovered that administering this antibody to hamsters reduced or eliminated the presence of the original Delta or Omicron virus in the animals’ lungs and nose. (They are currently testing it against XBB.1.5.) To understand where the antibody bound and why Omicron’s mutations didn’t interfere, other Scripps Research team members looked at the antibody’s structure while it was attached to the spike.
Their findings imply that S728-1157 might serve as the foundation for an urgently required replacement for current antibody-based therapies. Many of these treatments, known as monoclonal antibodies, are no longer effective as a result of variations, especially Omicron.
The study may potentially serve as a blueprint for developing novel vaccines that activate the creation of antibodies via the spike protein. The team discovered that the spike’s configuration is important. In particular, when the immune system sees spikes in an open conformation similar to the one they would presume to attack a cell, they make more broadly effective antibodies like S728-1157. However, the newer mRNA-based vaccines, notably those based on Omicron, frequently result in more closed spikes.
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The lesson learned from this study, according to Dr. Changrob, is that the future generation of vaccinations should strive to stabilize the spike in a more open posture.