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Cheat on the new coronavirus once and it can’t infect cells, new research suggests.
Scientists have developed fragments of proteins, called peptides, that fit snugly into a groove in the SARS-CoV-2 Spike protein that it would normally use to gain access to a host cell. These peptides effectively trick the virus into “shaking hands” with a replica rather than the actual protein on the surface of a cell that lets the virus in.
Previous research had determined that the new coronavirus binds to a receptor protein on the surface of a target cell called ACE2. This receptor is located on certain types of human cells in the lungs and nasal cavity, providing SARS-CoV-2 with many access points to infect the body.
For this work, scientists at Ohio State University designed and tested peptides that resemble ACE2 enough to convince the coronavirus to bind to them, an action that blocks the ability of the virus to actually enter the cell.
“Our goal is that every time SARS-CoV-2 comes in contact with the peptides, the virus is inactivated. This is because the virus’s Spike protein is already bound to something it needs to bind to the cell, ”said Amit Sharma, co-lead author of the study and assistant professor of veterinary biosciences at Ohio State. . “To do this, we have to attack the virus while it is still outside the cell.”
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The Ohio State team plans to deliver these peptides made in a nasal spray or aerosolized surface disinfectant, among other applications, to block the circulating SARS-CoV-2 access points with a agent that prevents their entry into target cells.
“With the results we have generated with these peptides, we are well positioned to move on to product development stages,” said Ross Larue, co-lead author and assistant research professor of pharmacy and pharmacology at Ohio State.
The study was published in the January issue of the journal Chemistry of bioconjugates.
SARS-CoV-2, like all other viruses, requires access to living cells to do its damage – viruses hijack cell functions to reproduce and cause infection. Very rapid viral replication can overwhelm the host system before immune cells can effectively defend themselves.
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One of the reasons this coronavirus is so infectious is that it binds very tightly to the ACE2 receptor, which is abundant in human cells and some other species. The Spike protein on the surface of SARS-CoV-2, which has become its most recognizable feature, is also fundamental to its success in binding to ACE2.
Recent advances in protein crystallization and microscopy have made it possible to create computer images of specific protein structures alone or in combination, such as when they bind to each other.
Sharma and her colleagues took a close look at images of the SARS-CoV-2 Spike protein and ACE2, focusing specifically on how their interactions occur and the connections required for the two proteins to lock into place. square. They noticed a spiral ribbon-shaped tail on ACE2 as the focal point of attachment, which became the starting point for peptide design.
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“Most of the peptides we’ve designed are based on the tape in contact with the Spike,” said Sharma, who also holds a professorship in microbial infection and immunity. “We focused on creating the shortest possible peptides with the minimum amount of essential contact.”
The team tested several peptides as “competitive inhibitors” that could not only bind safely to SARS-CoV-2 Spike proteins, but also prevent or reduce viral replication in cell cultures. Two peptides, one with the minimum contact points and one larger, were effective in reducing SARS-CoV-2 infection in cell studies compared to controls.
Sharma described these results as the start of a product development process that will be continued by the team of virologists and pharmaceutical chemists collaborating on this work.
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“We take a multi-pronged approach,” said Sharma. “With these peptides, we have identified the minimum contacts necessary to inactivate the virus. Going forward, we plan to focus on developing aspects of this technology for therapeutic use.
“The goal is to neutralize the virus in an efficient and potent manner, and now, due to the emergence of variants, we want to evaluate our technology against emerging mutations.”
(Source: State of Ohio – Photo by @visuals)
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