B-cell receptor recognizing Dengue virus envelope protein (BCR-DENV-E)

The B-cell receptor (BCR) recognizing the Dengue virus (DENV) envelope (E) protein is a critical component of the adaptive immune response against dengue infection (Screaton et al., 2015, Science). The E protein is the primary surface glycoprotein of the virus, responsible for host cell attachment and membrane fusion, making it the dominant target for neutralizing antibodies. BCRs on the surface of naive and memory B cells recognize specific epitopes on the E protein, such as the fusion loop in domain II or the receptor-binding site in domain III (Beltramello et al., 2010, Cell Host & Microbe). Upon activation, these B cells differentiate into antibody-secreting plasma cells that produce soluble immunoglobulins to neutralize the virus. However, the interaction is complex due to the existence of four distinct DENV serotypes; sub-neutralizing levels of antibodies can lead to antibody-dependent enhancement (ADE), where the virus-antibody complex facilitates entry into Fc-receptor-bearing cells, increasing viral load and disease severity (Katzelnick et al., 2017, Science). Therapeutic strategies focus on developing vaccines like Dengvaxia and Qdenga, as well as monoclonal antibodies like VIS513, that target highly conserved or quaternary epitopes to provide broad protection across all serotypes while minimizing the risk of ADE (Robinson et al., 2015, Nature).

Other names

Dengue virus-specific B-cell receptorDENV E-specific BCRAnti-DENV BCRDengue virus envelope-specific B-cell receptor

Antigen-mediated activation of B-cell receptors leads to the clonal expansion and differentiation of B cells into plasma cells that secrete neutralizing antibodies. These antibodies bind to the Dengue virus envelope protein, preventing viral entry into host cells and facilitating viral clearance.