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The Feline panleukopenia virus (FPV) VP2 protein is the major structural component of the viral capsid, comprising approximately 90% of the 60-subunit icosahedral shell (UniProt: P03304). It is essential for the viral infection process, as it directly binds to the feline transferrin receptor (TfR) to facilitate cell entry via receptor-mediated endocytosis (PubMed: 12767992). Mutations within the VP2 protein are primarily responsible for determining the host range of the virus, allowing it to adapt to different feline and canine species (PubMed: 21183405). Because it is exposed on the viral surface, VP2 is the primary target for neutralizing antibodies produced by the host's immune system during infection or following vaccination. Most commercial vaccines for feline panleukopenia utilize the VP2 protein, either in inactivated or modified-live virus forms, to induce protective immunity. In diagnostics, VP2 is the target for various assays, including enzyme-linked immunosorbent assays (ELISA) and polymerase chain reaction (PCR) tests used to detect the virus in clinical samples. Research into therapeutic interventions often focuses on blocking the interaction between VP2 and the host transferrin receptor to prevent viral spread. Understanding the structural biology of VP2 is crucial for monitoring the evolution of parvoviruses and ensuring the continued efficacy of feline vaccination programs.
Neutralization of viral particles by binding to the VP2 capsid protein, thereby preventing the virus from attaching to the host transferrin receptor and inhibiting subsequent cellular entry and replication.
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