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Rotavirus VP6 protein is the major inner capsid (intermediate layer) protein of the rotavirus virion, making up over half of the viral mass[1][2][5]. It self-assembles into trimers that form the rigid lattice of the middle layer of the triple-layered particle, playing a central role in viral architecture and infectivity[1][2][4][5]. VP6 interacts extensively with both the outer capsid proteins (VP4, VP7) and the inner layer (VP2), contributing to structural integrity, proper capsid assembly, and viral genome packaging[1][2][5]. It is essential for viral RNA transcription, as nascent transcripts exit through pores formed by the VP6 lattice[2]. VP6 is also highly immunogenic, carrying epitopes recognized by monoclonal antibodies and the host immune system, and is the basis for most diagnostic antigen detection tests[1][3]. As a structural (not enzymatic or receptor) viral protein, VP6 does not serve as a receptor or classical therapeutic target but is a key component in vaccine development, serological assays, and diagnostic tools[1][2][3][4][5].
VP6 is the primary target for neutralizing antibodies and vaccine-induced immune responses
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