A novel antibody against the furin cleavage site of SARS-CoV-2 spike protein: Effects on proteolytic cleavage and ACE2 binding.
SARS-CoV-2 harbors a unique S1/S2 furin cleavage site within its spike protein, which can be cleaved by furin and other proprotein convertases. Proteolytic activation of SARS-CoV-2 spike protein at the S1/S2 boundary facilitates interaction with host ACE2 receptor for cell entry. To address this, high titer antibody was generated against ... the SARS-CoV-2-specific furin motif. Using a series of innovative ELISA-based assays, this furin site blocking antibody displayed high sensitivity and specificity for the S1/S2 furin cleavage site, including with a P681R mutation, and demonstrated effective blockage of both enzyme-mediated cleavage and spike-ACE2 interaction. The results suggest that immunological blocking of the furin cleavage site may afford a suitable approach to stem proteolytic activation of SARS-CoV-2 spike protein and curtail viral infectivity.
Mesh Terms:
Amino Acid Motifs, Angiotensin-Converting Enzyme 2, Antibodies, Viral, Furin, Humans, Mutation, Nose, Proprotein Convertases, Protein Binding, Proteolysis, SARS-CoV-2, Spike Glycoprotein, Coronavirus
Amino Acid Motifs, Angiotensin-Converting Enzyme 2, Antibodies, Viral, Furin, Humans, Mutation, Nose, Proprotein Convertases, Protein Binding, Proteolysis, SARS-CoV-2, Spike Glycoprotein, Coronavirus
Immunol Lett
Date: Dec. 01, 2021
PubMed ID: 35007661
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