Rabbit hemorrhagic disease virus capsid protein VP1 (VP1)

The Rabbit hemorrhagic disease virus capsid protein VP1, also widely known as VP60, is the primary structural protein of the RHDV virion, a highly contagious calicivirus affecting lagomorphs [1, 5]. It self-assembles into an icosahedral shell composed of 180 subunits that protects the viral genome and facilitates host cell entry [15, 17]. The protein features a conserved shell (S) domain and a variable protruding (P) domain, with the P2 subdomain serving as the site for binding host histo-blood group antigens (HBGAs) that act as attachment factors [4, 6]. As the major surface-exposed antigen, VP1 is the principal target for neutralizing antibodies, making it the essential component of both traditional inactivated vaccines and modern recombinant virus-like particle (VLP) vaccines [5, 13]. Mutations within the P2 subdomain drive the emergence of new antigenic variants, such as RHDV2 (GI.2), which can evade immunity generated against older strains [1, 14]. Consequently, VP1 is the primary focus for diagnostic assays and the development of multivalent vaccines to control outbreaks in domestic and wild rabbit populations [9, 12].

Other names

VP60Major capsid proteinCapsid protein

Induction of neutralizing antibodies that bind to the VP1 protein, sterically blocking the virus from attaching to host histo-blood group antigens (HBGAs) and preventing viral entry into host cells [4, 13].