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The Poliovirus capsid D-antigen refers to the native, infectious conformation of the poliovirus particle, which is a non-enveloped, positive-sense RNA virus (Hogle, 2002). The capsid is an icosahedral structure composed of 60 protomers, each containing four structural proteins: VP1, VP2, VP3, and VP4 (Minor, 1996). The D-antigen (or "Dense" antigen) state is characterized by its ability to bind to the host cell receptor CD155 (PVR) and, crucially, to elicit the production of neutralizing antibodies in the host (Ferguson et al., 2020). This antigenic form is the primary target for both Inactivated Poliovirus Vaccines (IPV) and Oral Poliovirus Vaccines (OPV), as the alternative C-antigen (or "Coreless") form is non-infectious and does not induce protective immunity (WHO, 2023). The epitopes within the D-antigen are primarily located on the surface-exposed loops of VP1, VP2, and VP3, which are the sites of interaction for neutralizing antibodies (Minor, 1996). In therapeutic development, these epitopes are targeted by monoclonal antibodies and small-molecule inhibitors to prevent viral attachment and uncoating (Hogle, 2002). Maintaining the integrity of D-antigen epitopes is a critical quality control parameter in vaccine manufacturing to ensure clinical efficacy against poliomyelitis (WHO, 2023).
Induction of neutralizing antibodies that bind to surface epitopes, preventing viral attachment to the host receptor CD155 and subsequent cell entry.
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