Canine parvovirus capsid protein (CPV capsid protein)

The canine parvovirus capsid protein is the primary structural protein of the canine parvovirus (CPV) virion and forms the icosahedral shell that encapsulates the viral single-stranded DNA genome. The capsid consists of 60 copies of the capsid protein, mainly the product called VP2, with a minority of slightly larger VP1 subunits. These proteins are related by icosahedral symmetry and assemble into a robust, highly antigenic particle that is critical for virus assembly, stability, and infectivity. The external surface is characterized by distinct features such as a threefold spike and depressions referred to as canyons and dimples, which serve as major antigenic sites recognized by host antibodies and overlap with the host transferrin receptor binding footprint, mediating cell attachment and viral entry[2][3][4][5]. The capsid protein is the primary immunogen for vaccine development due to its potent ability to elicit neutralizing antibody responses, but it is not considered a drug target in the typical sense (such as a receptor, enzyme, or transporter). Its main role in disease is to drive the infectious process of canine parvovirus, a highly contagious and often fatal viral infection in dogs[1][3][4]. Notes on therapeutic targeting: This protein is not typically considered a small-molecule drug target but is important as a vaccine antigen and for antibody-mediated immunotherapy and infection diagnostics[1][3]. There are no approved direct-acting antiviral drugs that bind the capsid protein; current interventions rely on vaccines, with some research into monoclonal antibodies[1][3].

Other names

CPV VP2 (the major capsid protein)CPV VP1 (minor capsid protein)Canine parvovirus structural protein

Neutralizing antibodies block viral cell entry by binding capsid epitopes, preventing attachment to host transferrin receptor (TfR)