Rotavirus VP7 (G3 serotype) (VP7)

Rotavirus VP7 is a calcium-stabilized trimeric glycoprotein forming the outermost layer of the rotavirus capsid with T=13 icosahedral symmetry, capping VP6 pillars on the double-layered particle (DLP). It displaces the transient ER membrane during maturation, locks VP4 spikes in place, and undergoes Ca2+ withdrawal-induced dissociation during cell entry to trigger VP4 conformational changes for membrane penetration. The G3 serotype (e.g., rhesus rotavirus RRV) features two domains: a Rossmann fold (domain I, residues ~78-161 and 256-321) and a jelly-roll beta-sandwich (domain II, residues ~161-256), with four intrasubunit disulfide bonds and two Ca2+ sites per subunit interface. The outward-facing surface bears neutralizing epitopes (regions 7-1 and 7-2) targeted by protective antibodies, which bind trimeric VP7 to prevent uncoating; the inward-facing surface interacts with VP6 via N-terminal arms. VP7 is a principal immunogen for vaccines, with disulfide-linked trimers proposed as stable subunit candidates.[1][2][3][4]

Other names

outer-layer protein VP7outer capsid protein VP7coat protein VP7

Neutralizing antibodies stabilize VP7 trimer to inhibit uncoating and VP4 rearrangement