Abstract:We have reported that anti-prM antibody is an enhancing antibody that enhances DV infection of non-Fc receptor bearing cells by dual specificity. We identified the epitope recognized by this anti-prM antibody, M3, which is located at the a.a.53-67of the prM protein nearby the prM/M cleavage junction and these anti-M3 antibodies could be detected in dengue patients sera. Surprisingly, this anti-prM antibody not only recognizes the prM protein of dengue virions, but also cross-reacts with epithelial cells, endothelial cells as well as T cells. The binding of anti-prM antibody to endothelial cells was dose-dependent and could be blocked by M3 peptides. Human M3-specific antibodies from dengue patient sera were demonstrated to be able to bind to endothelial cells and mediate ADE infection on K562 cells. Furthermore, the anti-prM antibody will mediate the antibodydependent cell phagocytosis, leading to the similar severe form of DHF/DSS. In conclusion, anti-prM antibody plays two roles in the pathogenesis of dengue virus infection: to be an enhancing antibody and an autoantibody as well.
scite is a Brooklyn-based organization that helps researchers better discover and understand research articles through Smart Citations–citations that display the context of the citation and describe whether the article provides supporting or contrasting evidence. scite is used by students and researchers from around the world and is funded in part by the National Science Foundation and the National Institute on Drug Abuse of the National Institutes of Health.