Rotavirus outer capsid glycoprotein VP7 (VP7)

Rotavirus outer capsid glycoprotein VP7 is a trimeric, calcium-stabilized glycoprotein that forms the outermost layer of the rotavirus virion, organized in a T=13 icosahedral lattice with 260 trimers[3][6][10]. VP7, along with VP4, defines the serotype (G type for glycoprotein, P type for protease-sensitive) of group A rotaviruses[4][8][10]. VP7 is synthesized in the endoplasmic reticulum, where it undergoes glycosylation and correct folding, involving disulfide bond formation that is facilitated by associated carbohydrates[1][5]. The mature VP7 protein is essential for viral infectivity, facilitating virion assembly and entry into host cells, and presenting major neutralizing epitopes targeted by protective antibodies[2][3][6]. Removal of Ca²⁺ destabilizes the VP7 trimer, leading to uncoating and enabling subsequent membrane penetration events by the other outer-layer protein, VP4[3][6]. VP7 is a principal antigen in current rotavirus vaccines, and its G-type variants (G1, G2, G3, G4, G9) correspond to the most clinically important serotypes implicated in human rotavirus disease[8][4]. The protein is a critical therapeutic target for neutralizing antibody–based immunity and vaccine design, but genetic and antigenic diversity among G types poses challenges for broad and long-term vaccine protection[4][8].

Other names

Rotavirus glycoprotein VP7Rotavirus VP7Outer capsid glycoprotein VP7

Induction of neutralizing antibodies that block viral infectivity by stabilizing VP7 and preventing uncoating