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ID93 is a recombinant fusion protein vaccine candidate designed to provide protection against Mycobacterium tuberculosis (Mtb). It is composed of four Mtb antigens: Rv2608, Rv3619, Rv3620, and Rv1813, which are associated with virulence or latency (Baldwin et al., 2012). The B-cell receptors (BCRs) and antigen-specific antibodies that recognize ID93 epitopes are the primary mediators of the humoral immune response elicited by the vaccine (Coler et al., 2018). Upon administration, the ID93 protein binds to specific BCRs on the surface of B cells, initiating a process of activation and clonal expansion that results in the production of high-affinity IgG antibodies. These antibodies are intended to assist in the control of Mtb infection through mechanisms such as opsonization and neutralization (Penn-Nicholson et al., 2015). The induction of these specific BCRs and antibodies is a critical endpoint in clinical trials evaluating the efficacy and immunogenicity of ID93-based vaccines (NCT02465216). This target population of receptors is essential for establishing long-term immunological memory against tuberculosis.
The ID93 vaccine acts as an exogenous antigen that binds to and clusters B-cell receptors (BCRs) specific for its epitopes, triggering B-cell activation, proliferation, and differentiation into antibody-secreting plasma cells and memory B cells (Coler et al., 2018).
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