A new study reveals vulnerability in coronavirus that shows a way to a simple, potential treatment. The spike protein of the COVID-19 virus contains the virus’ binding site adhering to the host cells that enables the virus to enter and infect the body. The researchers, using nanometer-level simulations, have discovered a positively charged site (known as the polybasic cleavage site) located 10 nanometers from the actual binding site on the spike protein. This positively charged site allows a strong bond between the virus protein and the negatively charged human-cell receptors.
Based on this discovery, the researchers designed a negatively charged molecule to block the virus from binding to the host cell. By blocking this cleavage site, it is possible to decrease the virus’s ability to infect humans as the site may act as a viable prophylactic treatment. Made up of amino acids, SARS-CoV-2’s polybasic cleavage sites have remained elusive since the COVID-19 outbreak began. But previous research indicates that these mysterious sites are essential for virulence and transmission. An unexpected insight provides more leverage than this polybasic cleavage site is located 10 nanometers from human cell receptors.
This was entirely a discovery because researchers did not expect to see electrostatic interactions at 10 nanometers. They also stated that in physiological conditions, all electrostatic interactions no longer occur at distances longer than 1 nanometer. The function of the polybasic cleavage site has remained elusive, however; it appears to be cleaved by an enzyme (furin) that is abundant in the lungs, which suggests the cleavage site is crucial for the virus entry into human cells.
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