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The Feline parvovirus (FPV) VP2 capsid protein is the primary structural component of the FPV viral shell, accounting for approximately 90% of the total capsid mass. It plays a critical role in the viral life cycle by mediating binding to the host transferrin receptor 1 (TfR1), which facilitates viral entry into feline cells, particularly those in the bone marrow and intestinal epithelium [1][3]. VP2 is the main determinant of host range and is highly immunogenic, containing the major epitopes recognized by neutralizing antibodies [2]. In clinical medicine, VP2 is the central target for feline panleukopenia vaccines, which aim to elicit a robust humoral immune response to prevent the severe leukopenia and enteritis associated with FPV infection [4]. Diagnostic assays, such as fecal antigen tests and ELISA, frequently target the VP2 protein to detect active shedding or assess immunity [5]. [1] UniProt Consortium. 'Capsid protein VP2 - Feline parvovirus.' UniProtKB - P03303. [2] Hueffer, K., & Parrish, C. R. (2003). 'Parvovirus host range, cell tropism and evolution.' Current Opinion in Microbiology. [3] Parker, J. S., et al. (2001). 'Transferrin receptor synthesis and rapid viral replication drive the cellular tropism of feline panleukopenia virus.' Journal of Virology. [4] Truyen, U. (2006). 'Evolution of canine parvovirus—A review.' Veterinary Microbiology. [5] Decaro, N., et al. (2008). 'A real-time PCR assay for rapid detection and quantitation of feline panleukopenia virus.' Journal of Virological Methods.
Vaccines containing the VP2 protein (or the virus expressing it) induce the production of neutralizing antibodies that bind to specific epitopes on the capsid surface, blocking the interaction between the virus and the host transferrin receptor, thereby preventing viral entry and infection [1][2].
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