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JS026 is a recombinant fully human monoclonal neutralizing antibody that targets the receptor binding domain (RBD) of the S1 subunit of the SARS-CoV-2 spike protein. By binding with high affinity to this region, it blocks the interaction between the viral RBD and angiotensin converting enzyme 2 (ACE2) on host cells, thereby preventing viral entry and infection. The antibody was selected from memory B cells of COVID-19 survivors and does not bind to human self-antigens, suggesting a low risk for immunogenicity or side effects. Its epitope is located in a relatively conserved region of RBD with minimal overlap with ACE2 interaction sites; thus far, no known RBD mutations have affected its binding. Preclinical studies demonstrated that JS026 reduces virus titers and pathological changes in animal models infected with SARS-CoV-2. It has also been studied as part of an antibody cocktail (notably with etesevimab/JS016) to enhance neutralization breadth against multiple variants[1][3][5][7].
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