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Intermediate capsid protein VP6 is the most abundant and highly conserved structural protein of the rotavirus, forming the middle layer of its triple-layered icosahedral capsid [NIH, 2022]. It serves as a critical physical adaptor between the inner core (VP2) and the outer capsid (VP4 and VP7), and it is indispensable for the endogenous transcription of the viral double-stranded RNA genome [NIH, 2001]. While VP6 does not induce traditional neutralizing antibodies on the virion surface, it is highly immunogenic and a primary target for protective IgA and IgG antibodies that inhibit viral replication intracellularly by rendering the virus transcriptionally inactive [NIH, 2002; PLOS, 2020]. Due to its ability to self-assemble into stable nanotubes and virus-like particles, VP6 is a prominent candidate for next-generation non-live subunit vaccines and is being explored as a versatile scaffold for drug delivery and as an immunological adjuvant [NIH, 2022; MDPI, 2021]. Its conservation across different rotavirus groups makes it a valuable target for broad-spectrum therapeutic and diagnostic applications [Creative Diagnostics, 2024; NIH, 2013].
Intracellular neutralization by interfering with viral transcription and replication; enhancement of immune responses through adjuvant activity [NIH, 2002; MDPI, 2021].
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