Monoclonal antibodies have proved effective in the prevention and treatment of Covid-19. Their effectiveness depends on the recognition of specific structures on the surface of the viral spike protein. Over the past six months, we have learned that many of these shape-specific determinants change in ways that abrogate the effectiveness of individual antibodies and even of antibody cocktails. This is the fifth in a series that describes a search for monoclonal antibodies that may successfully address the problem of antigenic variation. Read more from this series in parts one, two, three, and four. Monoclonal antibodies have been successful in both prevention and early treatment of Covid-19. The monoclonal antibodies that have been studied to date bind to and interact with the spike protein, and more specifically, the receptor-binding domain. Over the past several months, as reviewed in this series, new monoclonal antibodies have been discovered that have broad neutralizing capabilities. All of these antibodies bind to the receptor-binding domain, either to the receptor-binding motif, which interacts directly with the ACE2 receptor, or to other parts of the receptor-binding domain to inhibit function. Despite the broad activity of these antibodies or camelid nanobodies, none are entirely neutralizing. SARS-CoV-2 is capable of mutating, leading to viral variants which inhibit antibody function that escape neutralization, triggering a search for effective neutralizing antibodies that recognize epitopes in regions outside the receptor-binding domain which might be constrained functionally, and therefore, less likely to mutate. Read the full article on Forbes.
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