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The Rabbit Hemorrhagic Disease Virus (RHDV) capsid protein VP60 is the primary structural protein of the virus, forming an icosahedral shell that protects the viral genome [4, 11]. It plays a critical role in the viral life cycle by mediating attachment to host cells through interactions with histo-blood group antigens (HBGAs), which triggers viral entry via endocytosis [4, 11]. As the most prominent surface protein, VP60 is the major target for the host's immune response and is the central component of most RHDV vaccines, including inactivated, recombinant, and virus-like particle (VLP) formulations [2, 3, 5]. These vaccines function by inducing neutralizing antibodies that block the protein's ability to bind to host receptors, thereby preventing infection [10, 16]. VP60 is also essential for diagnostic applications, serving as a key antigen in serological assays and a target for molecular detection of the virus in clinical samples [1, 10].
Induction of neutralizing antibodies that block viral attachment to host histo-blood group antigens (HBGAs) and prevent viral entry into host cells [10, 16].
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