General information on Anti-CoV-RBD (A12) antibody
The receptor-binding domain (RBD) of the spike protein of SARS-CoV-2 is the most relevant target used for the design of new treatments for COVID-19. The development of antibodies able to target this specific region can be carried out either in vivo, which is a time-demanding process or in vitro, which capitalizes on the flexibility of display technologies such as phage display.
The anti-CoV-RBD (A12) antibody was developed by phage display screening of a vast COVID-19 antibody library (LiAb-SFCOVID-19™) against the RBD of SARS-CoV-2. Given that antibody production by phage display does not require animal immunization nor the use of immunogenic antigens, only the small RBD protein was used to isolate specific RBD-binders from the LiAb-SFCOVID-19™ library. Moreover, since this library comprises the immune repertoire of COVID-19 patients, it has the greatest abundance of biologically relevant antibodies with potent neutralizing activity.
This specific antibody is thus a fully human immunoglobulin in IgG format. Its affinity towards recombinantly expressed RBD was tested and validated through enzyme-linked immunosorbent assay (ELISA). Additionally, the neutralizing activity was tested using the SARS-CoV-2 Surrogate Virus Neutralization Test (sVNT) assay which was designed to quickly assess the neutralizing potential of new antibodies without the need of using native viral particles.
Lastly, the IgG antibody was expressed in XtenCHO™, a highly productive transient mammalian system, and shown to be very stable and consistently generate high production yields.
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