Fool the new coronavirus once and it won’t be able to cause cell infection, new research suggests.
The scientists developed protein fragments – called peptides – that fit perfectly into a groove in the SARS-CoV-2 Spike protein, which would normally be used to access a host cell. These peptides effectively trick the virus into “shaking hands” with a replica, rather than the actual protein on the cell surface that allows the virus to enter.
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 lung 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 virus’s ability to actually enter the cell.
“Our goal is that whenever SARS-CoV-2 comes into contact with the peptides, the virus is inactivated. That’s because the virus’s Spike protein is already linked to something it needs to use to bind to the cell, ”said Amit Sharma, co-author of the study and an assistant professor of veterinary biosciences in Ohio. “To do this, we have to catch the virus while it is still outside the cell.”
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The Ohio state team plans to deliver these peptides manufactured in a nasal spray or aerosolized surface disinfectant, among other applications, to block the SARS-CoV-2 access points in circulation with an agent that prevents them from entering the cells. target.
“With the results we generate with these peptides, we are well positioned to move on to product development steps,” said Ross Larue, lead co-author and assistant professor of research in pharmacy and pharmacology in Ohio.
The study was published in the January issue of the journal. Bioconjugate Chemistry.
SARS-CoV-2, like all other viruses, requires access to living cells to cause their damage – viruses hijack cell functions to make copies of themselves and cause infections. The very rapid replication of the virus can overwhelm the host system before immune cells can muster an effective defense.
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One reason this coronavirus is so infectious is because it binds strongly to the ACE2 receptor, which is abundant in cells in humans and in some other species. The Spike protein on the surface of SARS-CoV-2, which has become its most recognizable feature, is also critical 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 bond with each other.
Sharma and his colleagues closely examined the images of the SARS-CoV-2 protein Spike and ACE2, magnifying precisely how their interactions occur and what connections are needed for the two proteins to lock in place. They noticed a spiral ribbon-shaped tail on the ACE2 as the focal point of the accessory, which became the starting point for the peptide project.
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“Most of the peptides we design are based on the tape in contact with Spike,” said Sharma, who also has an appointment as a professor of microbial infection and immunity. “We focus on creating the shortest possible peptides with the minimum of essential contacts.”
The team tested several peptides as “competitive inhibitors” that could not only safely bind to SARS-CoV-2 Spike proteins, but also prevent or decrease viral replication in cell cultures. Two peptides, one with minimal contact points and one larger, were effective in reducing SARS-CoV-2 infection in cell studies compared to controls.
Sharma described these findings as the beginning of a product development process that will be continued by the team of virologists and pharmaceutical chemists who collaborate in this work.
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“We are taking a multifaceted approach,” said Sharma. “With these peptides, we identified the minimum contacts needed to inactivate the virus. In the future, we plan to focus on developing aspects of this technology for therapeutic purposes.
“The goal is to neutralize the virus in an effective and potent way and now, due to the emergence of variants, we are interested in evaluating our technology against emerging mutations.”
(Source: State of Ohio – Photo by @visuals)
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