Journal
IMMUNOLOGY LETTERS
Volume 242, Issue -, Pages 1-7Publisher
ELSEVIER
DOI: 10.1016/j.imlet.2022.01.002
Keywords
SARS-CoV-2; COVID-19; Spike; Furin; Proprotein convertase; ACE2; Furin site blocking antibody
Categories
Funding
- EpiGentek
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A study found that an antibody generated against the furin motif of SARS-CoV-2 can block the cleavage of spike protein and inhibit its interaction with host cell receptors, reducing viral infectivity.
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.
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