Anti-CoV-S[679-833]-H7 antibody

General information on Anti-CoV-S[679-833]-H7 antibody

The anti-CoV-S[679-833]-H7 antibody was shown to possess a very strong affinity towards the S1/S2 border region of the spike glycoprotein found in SARS-CoV-2. The antibody was developed by phage display screening of our extremely diverse COVID-12 human antibody library (LiAb-SFCOVID-19™) for relevant binders against the spike fragment CoVs[679-833]. This fragment is predicted to contain the furin cleavage site, a vital domain for viral internalization in the COVID-19 pathology. In detail, this site is located between the S1 and S2 subunits of the spike glycoprotein and it is prone to catalysis by ubiquitous human proteases (furin). Once cleaved, this process exposes the S2 domain which, in turn, initiates the process of fusion between the viral and the human epithelial membranes.
This region thus represents the second stage of infection by SARS-CoV-2 and it is preceded only by the recognition and binding of the angiotensin-converting enzyme 2 (ACE2) receptor. For this reason, the antibody represents an opportunity to better understand the mechanism of infection in SARS-CoV-2 and to determine if the region containing the furin cleavage site could be a potentially interesting new therapeutic target to prevent the onset or treat COVID-19 pneumonia.
The antibody has been thoroughly validated against its intended target – CoV-S[679-833] – through enzyme-linked immunosorbent assay (ELISA). Moreover, no cross-reactivity was found against other regions of SARS-CoV-2 spike glycoprotein indicating the specificity of the newly developed reagent. The new fully human IgG antibody was also shown to be stable and easily produced with high yields in XtenCHO™, a transient recombinant mammalian system with optimal productivity.