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Canine parvovirus major capsid protein VP2 is the primary structural component of the Canine Parvovirus (CPV) capsid, constituting approximately 90% of the protein shell [8, 10]. It plays a pivotal role in viral pathogenesis by mediating host cell entry through binding with the host transferrin receptor (TfR) [3, 10]. VP2 is the most immunogenic protein of the virus, containing the major epitopes that elicit neutralizing antibodies, which makes it the central target for vaccine development and monoclonal antibody therapies [5, 11]. Mutations within the VP2 gene are responsible for the emergence of distinct antigenic variants (CPV-2a, 2b, and 2c), which influence the virus's host range, tissue tropism, and ability to evade existing immunity [1, 4, 10]. In therapeutic contexts, VP2 is targeted by neutralizing monoclonal antibodies to inhibit viral spread during acute infection, and it serves as the primary antigen in diagnostic assays for detecting viral shedding in feces [6, 11].
Neutralization of viral entry by blocking the interaction between the viral capsid and host transferrin receptors, and induction of long-term humoral immunity through the presentation of neutralizing epitopes.
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