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African swine fever virus major capsid protein p72 is the most abundant and immunogenic structural component of the virion, constituting approximately 31–33% of the total viral mass[2][3][6]. It is encoded by the B646L gene and forms the outer icosahedral capsid of ASFV via trimeric homomultimerization, adopting a double jelly-roll fold typical of viral capsid proteins[2][3][6]. As the primary antigenic determinant, p72 elicits strong antibody responses and is a critical marker in serological diagnosis and vaccine development[1][4][6]. Monoclonal antibodies against p72 can neutralize the virus and interfere sterically with capsid integrity or receptor binding, offering mechanistic justification for its study as a vaccine antigen[6]. However, p72 does not independently provide robust protection in vivo when used as a subunit vaccine[1]. Co-expression with the pB602L chaperone is required for proper folding and trimerization, which is necessary for accurate structural and immunogenic properties[2][4]. p72’s presence and integrity serve as indicators of ASFV replication, and the protein is essential for virion assembly and infectivity[1][2][3]. Its central role in virus structure and immunity makes it a key molecular target for African swine fever research and a focus of ongoing diagnostic and preventive strategies.
Neutralization by blocking virus entry (monoclonal antibodies) - Impairment of capsid assembly (by interfering with protein folding/assembly) - Antigen presentation for immune response (vaccine mechanism)
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