Health
Researchers discover new vulnerabilities in new coronavirus notorious spike protein
Researchers at Northwestern University discover new vulnerabilities in notorious coronavirus Spike protein -Clarify relatively simple and potential treatment routes.
The spike protein contains the binding site of the virus. It attaches to host cells and allows the virus to enter and infect the body. Using nanometer-level simulations, researchers found a positively charged site (known as a polybasic cleavage site) located 10 nanometers from the actual binding site of the spike protein .. The positively charged site allows for strong binding between the viral protein and the negatively charged human cell receptor.
Using this finding, researchers designed a negatively charged molecule to bind to a positively charged cleavage site. Blocking this site will prevent the virus from binding to the host cell.
“Our research shows that blocking this cleavage site may serve as a viable prophylactic treatment that reduces the ability of the virus to infect humans.” “Our results are: We describe an study showing that mutations in the SARS-CoV-2 spike protein affected viral infectivity.”
The study was published online in a journal last week ACS Nano..
Olvera de la Cruz is a lawyer Professor of Materials Science and Engineering at McCormick School of Engineering in Northwestern. Baofu Qiao, a research associate professor in the Olvera de La Cruz research group, was the first author of this paper.
The polybasic cleavage site of SAV-CoV-2 is composed of amino acids and has remained elusive since the onset of COVID-19. However, previous studies have shown that these mysterious sites are essential for pathogenicity and transmission. Olvera de la Cruz and Qiao found that the polybasic cleavage site is 10 nanometers from the human cell receptor.
“We didn’t expect electrostatic interactions to occur at 10 nanometers,” said Chao. “Under physiological conditions, all electrostatic interactions no longer occur at distances greater than 1 nanometer.”
The function of the polybasic cleavage site remains elusive. However, it appears to be cleaved by a lung-rich enzyme (furin), suggesting that the cleavage site is important for the virus to enter human cells.
Monica Olvera de la Cruz, McCormick School of Engineering, Northwestern
With this new information, Olvera de La Cruz and Chao plan to work with Northwestern chemists and pharmacologists to design new drugs that may bind to spike proteins.
Source:
See journal:
Qiao, B & Oliver de la Cruz, M (2020) Enhanced binding of SARS-CoV-2 spike protein to its receptor by a distal polybasic cleavage site. ACS Nano. doi.org/10.1021/acsnano.0c04798..
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