Anti-CoV-RBD (B6) antibody

General information on Anti-CoV-RBD (B6) antibody

The receptor-binding domain (RBD) of the new strain of coronavirus, SARS-CoV-2, is considered by many experts as the key domain contributing to the high transmission rate of the COVID-19 disease. Thus, designing antibodies targeting this region became an essential step in controlling the on-going pandemic. Moreover, obtaining anti-CoV-RBD antibodies became crucial not only from a therapeutic point of view but also from a research point of view.

Despite the similarity between SARS-CoV, the etiological agent behind the 2003 pandemic, and SARS-CoV-2, significant differences were found between their respective binding domains. This could explain SARS-CoV-2 higher infectivity as well as its significantly faster spread among the world’s population. Further comparative studies between the two pandemic strains may prove useful for the design of more effective immunotherapies.

The anti-CoV-RBD (B6) antibody is a fully human IgG immunoglobulin derived from a complex COVID-19 human antibody library (LiAb-SFCOVID-19™). The library comprises the immune diversity of dozens of patients who have survived the COVID-19 disease; moreover, it is fully adapted for fast screening with phage display technologies. The affinity and specificity of this phage display-derived antibody were tested and validated with ELISA. Additionally, its SARS-CoV-2 neutralizing activity was further tested in vitro using a competition assay using recombinantly expressed RBD and human ACE2 receptor (SARS-CoV-2 Surrogate Virus Neutralization Test, sVNT). Lastly, the ease of expression and stability of the anti-CoV-RBD (B6) antibody was further confirmed by recombinant production in the transient mammalian system (XtenCHO™).

This antibody is thus a suitable reagent to aid in the efforts for better understanding the infection mechanisms of SARS-CoV-2. Moreover, it can be useful for epidemic surveillance and optimization of SARS-CoV-2 neutralizing reagents.