As the world anxiously awaits development of one or more vaccines to tame the SARS-CoV-2 virus, other research continues at a feverish pace to find effective treatments for the disease it causes, COVID-19. That work, in which physicists and chemists are deeply involved, has made significant strides in the past several months and has turned up a few surprises.
Researchers at the University of Alberta reported at the August virtual meeting of the American Crystallographic Association that a dipeptide-based protease inhibitor used to treat a fatal coronavirus infection in cats also blocks replication of the SARS-CoV-2 virus in samples of monkey lung tissue. Joanne Lemieux, a biochemist at the university, says the antiviral, known as GC373, works by blocking the function of the main protease (Mpro), an enzyme that cleaves the polyproteins translated from viral RNA into individual proteins once it enters human cells.
Lemieux says GC373 has been shown to have no toxic effects in cats. Anivive, a California company that develops pet medicines, has applied for US Food and Drug Administration approval to begin trials in humans. Lemieux’s group crystallized the Mpro in combination with the drug and produced three-dimensional images of how the drug binds strongly to the active pocket on the enzyme. Although GC373 should be effective in its current form, the group is planning further crystallography experiments at the Stanford Synchrotron Radiation Lightsource (SSRL) and the Canadian Light Source to see if a reformulation could optimize it for human use, she says.
Finding or manufacturing antibodies may present a more expedient path to a COVID-19 treatment. Antibodies don’t enter cells, so they have fewer safety issues, and potential side effects are of less concern than those of drugs. Compared with a drug–protein interaction, an antibody has the entire surface area of the virus to which it could potentially bind, notes Sean McSweeney, director of Brookhaven’s Center for Biomolecular Structure.
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