Anti-CoV-S2 domain (F8) antibody

General information on Anti-CoV-S2 domain (F8) antibody

The spike glycoprotein of coronaviruses has been extensively studied since the emergence of the extremely virulent strains SARS-CoV and MERS-CoV. These studies have been crucial for increasing our knowledge and understanding of the pathology caused by the new strain of coronavirus, SARS-CoV-2. Despite the phylogenetic proximity between this strain and the etiological agent of the severe acute respiratory syndrome coronavirus (SARS) disease, significant differences were found in terms of infectivity between the two.
More specifically, the presence of a furin cleavage site between the N-terminal region (S1 subunit) and the C-terminal (S2 subunit) alongside the presence of compensatory mutations is believed to have contributed to the higher overall infectivity in SARS-CoV-2. After the spike binds to the human receptor ACE2, it suffers important modifications including the proteolytic cleavage catalyzed by the ubiquitous human furin proteases and the conformational reorganization driven by the two heptad repeats, HR1 and HR2.
The anti-CoV-S2 (F8) antibody is a fully human IgG immunoglobulin shown to strongly bind to the S2 subunit of the spike. The antibody was isolated from a vast pool of COVID-19 human antibodies (LiAb-SFCOVID-19™) via phage display. Moreover, its stability and ease of production have been established by transient expression in the CHO-based mammalian recombinant system – XtenCHO™. This antibody and similar products obtained from the COVID-19 human library have all been validated for ELISA applications using purified forms of the SARS-CoV-2 S2 protein.