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The Equine infectious anemia virus (EIAV) capsid protein p26 is the primary structural component of the viral core, produced by the proteolytic cleavage of the Gag polyprotein (UniProt: P03346). It assembles into a conical shell that encapsulates the viral RNA genome and essential enzymes, playing a critical role in both the late stages of the viral life cycle, such as assembly and budding, and the early stages, such as uncoating and reverse transcription (PubMed: 11160735). Due to its high conservation among EIAV strains and its strong immunogenicity, p26 is the primary target for diagnostic assays, including the gold-standard Coggins test (agar gel immunodiffusion) and various ELISAs used to identify infected equids (USDA APHIS). While there are currently no approved antiviral drugs targeting p26, it remains a subject of interest for the development of capsid assembly inhibitors, drawing on strategies used for other lentiviruses like HIV-1 (PubMed: 20118268). The protein's stability and ability to self-assemble make it a key focus for understanding lentiviral architecture and host-pathogen interactions.
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