HIV, Ebola and most recently, COVID-19 viruses have had an enormous impact on our societies world-wide. All these viruses are 'enveloped viruses,' viruses that have an exterior envelope that surrounds them largely composed of their host's cells.
Exploring the molecular basis of how pradimicin A binds to viral N-glycan, a potential SARS-CoV-2 entry inhibitorAn illustration of the PRM-A molecule and the branched oligomannose structure found in N-glycans and how they bind with a graphic representation of the resultant decrease in the relative infectivity of the SARS-CoV-2 virus when exposed to PRM-A. Credit: Yu Nakagawa, Nagoya University
To infect a cell, a virus's envelope uses specific receptors on its surface called spike proteins—which are usually glycoproteins, meaning carbohydrates, specifically sugar attached to proteins—to bind to the cellular membrane of a host's cell, causing a conformational change in the cell membrane which allows the virus to enter the cells. Once there, it uses the cell's resources to replicate its own genome, safe from the host's immune system.
The Japanese team looked at PRM-A, a naturally occurring lectin mimic. It has shown promise as a viral entry inhibitor as there is evidence it binds to the N-glycans of the viruses' envelope glycoproteins.
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