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Researchers have developed a ‘bait’ protein that mimics the interface at which the SARS-CoV-2 spike protein binds to a human cell, a version of which could neutralize viral infection in cells and protect hamsters from viral challenges. . The SARS-CoV-2 virus enters human cells when the spike protein binds to the human ACE2 receptor. Although neutralizing antibodies against the spike protein have been isolated, the spike can develop “escape mutations” that help avoid them. There is therefore an urgent need to develop therapies that may be more resistant to the escape of SARS-CoV-2 mutations. To address this challenge, Thomas Linsky and colleagues developed a computational protein design strategy that enabled the rapid design of de novo stable protein “baits” that replicate the protein receptor interface in hACE2 to SARS-CoV- 2 binds. After using their approach to generate some 35,000 computational lures, the researchers selected the high-level designs for further testing and identified a particularly strong candidate. Administering a version of this prevented SARS-CoV-2 from infecting several human cell lines. In a Syrian hamster model, a single prophylactic dose administered 12 hours prior to exposure to the virus allowed all animals to survive the lethal dose with little weight loss. Because the decoy replicates the target cleavage site of the spike protein in hACE2, the authors believe it is inherently resistant to viral mutation escape.
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