Rotavirus VP6 inner capsid protein (VP6)

The Rotavirus VP6 inner capsid protein forms the intermediate layer of the rotavirus triple-layered capsid, self-assembling into icosahedral structures with T=13 symmetry composed of 230 trimers, which encase the viral genome and inner VP2 layer. This protein exhibits structural polymorphism, forming spherical or helical particles depending on pH and divalent cation concentrations, with protonation states controlling intertrimer contacts essential for assembly. VP6 trimers feature a β-sheet head domain for trimerization and outer layer interactions, and an α-helical base domain interfacing with VP2, enabling symmetry mismatch accommodation and transcription activation upon outer layer loss during infection. It interacts with VP7, VP4, VP2, and host proteins like hsc70 to facilitate cell entry, uncoating, and viral replication in the intestine. As a highly immunogenic component recognized by neutralizing antibodies, VP6 underpins rotavirus subgroup classification and serves in vaccine development, virus-like particles, and nanobiomaterials due to its self-assembly properties. Its role in rotavirus, a major cause of severe diarrhea in children, highlights potential for VP6-based prophylactics, though no direct small-molecule drugs target it.

Other names

VP6major capsid proteinintermediate capsid protein