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Bluetongue virus (BTV) molecular components comprise the structural and non-structural proteins of a double-stranded RNA virus within the Orbivirus genus (Mertens et al., 2005). The virion is composed of seven structural proteins (VP1–VP7) organized into a complex multi-layered capsid, with the outer layer consisting of VP2 and VP5 (UniProt). VP2 is the primary determinant of viral serotype and the main target for neutralizing antibodies, making it a critical component for vaccine development (Schwartz-Cornil et al., 2008). The inner core is dominated by the highly conserved VP7 protein, which serves as the principal antigen for diagnostic competitive ELISAs (WOAH). Additionally, the virus encodes several non-structural proteins, such as NS1 and NS2, which are essential for viral replication, mRNA synthesis, and the formation of viral inclusion bodies (Belhouchet et al., 2011). While no small-molecule antivirals are currently used in clinical veterinary practice, these molecular components are the primary targets for a variety of inactivated, live-attenuated, and recombinant subunit vaccines designed to control outbreaks in livestock. Therapeutic challenges include the high rate of genomic reassortment and the necessity for multivalent formulations to cover the numerous distinct serotypes (PubMed).
Neutralization of viral entry via antibodies targeting VP2; induction of systemic immunity to prevent viral replication and viremia.
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