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Like the Rebel Alliance that detonates the Death Star’s thermal exhaust port or the legendary Greek warrior Achilles victim to nothing more than an arrow lodged in his ankle, seemingly unstoppable forces often harbor a tiny weakness. which turns out to be their downfall.
Now researchers at Northwestern University have discovered a new vulnerability in the genetic structure of SARS-CoV-2 that may well turn out to be the Achilles heel of the coronavirus. The study authors say the revelation paves the way for a new, simple approach to treating coronaviruses.
More specifically, this discovery concerns the coronavirus’ peak protein.
While the word protein stands for dumbbell and bicep supports, in this case, the SARS-CoV-2 spike protein is essentially what gives the virus its nasty ability to infect new people so quickly. The spike protein harbors the virus’ binding site it is what attaches to new host cells, allowing the coronavirus to enter and infect host after host.
All of this isn’t groundbreaking news for scientists, but this is where things get interesting. Through a series of nanoscale-level simulations, the Northwestern team noticed a positively charged area located just 10 nanometers from the spike protein binding site.
This positively charged area, called polybasic cleavage site, seems to work as a kind of aid in the process of binding with a new host. The positive charge of the polybasic cleavage site promotes a stronger connection between the coronavirus spike protein and the negative charge of human cell receptors.
After making this discovery, however, the research team quickly realized that they might be able to take advantage of the polybasic cleavage site. So, they designed and created a personalized negatively charged molecule that would bind to the positively charged polybasic cleavage site just like a human cell.
The idea here is that if the coronavirus binds to this decoy, it will be unable (or at least less able) to actually infect new people and spread further.
“Our work indicates that blocking this cleavage site may act as a viable prophylactic treatment that decreases the ability of the virus to infect humans,” says study leader Monica Olvera de la Cruz, Lawyer Taylor professor of science and materials engineering at the McCormick School of Northwestern. Engineering, in one version. “Our results explain experimental studies showing that mutations in the SARS-CoV-2 spike protein affected the transmissibility of the virus.”
Polybasic cleavage sites are not an entirely new concept. Previous studies conducted long before COVID-19 had suggested that these viral areas, made up of amino acids, are important parts of the spread and transmission of viruses in general. For some reason, however, locating the polybasic cleavage site of SARS-CoV-2 had proven difficult until this study.
“The function of the polybasic cleavage site has remained elusive,” adds Professor Olvera de la Cruz. “However, it appears to be cleaved by an enzyme (furin) which is abundant in the lungs, suggesting that the cleavage site is crucial for the virus to enter human cells.”
“We didn’t expect to see electrostatic interactions at 10 nanometers,” comments study lead author Baofu Qiao, a research assistant professor in the Olvera de la Cruz research group. “Under physiological conditions, all electrostatic interactions no longer occur at distances greater than 1 nanometer.”
The research team is already planning to work with chemists and pharmacologists at Northwestern to begin developing a new drug that incorporates these findings.
The full study can be found here, published in ACS Nano.
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