PT  - JOURNAL ARTICLE
AU  - Michael G. Spelios
AU  - Jeanne M. Capanelli
AU  - Adam W. Li
TI  - A novel antibody against the furin cleavage site of SARS-CoV-2 spike protein: effects on proteolytic cleavage and ACE2 binding
AID  - 10.1101/2021.02.09.430451
DP  - 2021 Jan 01
TA  - bioRxiv
PG  - 2021.02.09.430451
4099  - http://biorxiv.org/content/early/2021/02/09/2021.02.09.430451.short
4100  - http://biorxiv.org/content/early/2021/02/09/2021.02.09.430451.full
AB  - 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, 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.Competing Interest StatementThe authors have declared no competing interest.