Rotavirus Outer Capsid Glycoprotein VP7 (G3) (VP7 (G3))

Rotavirus Outer Capsid Glycoprotein VP7 (G3) is a major structural protein of Group A Rotavirus, serving as the primary component of the virion's outermost shell [8, 11]. This approximately 34-37 kDa glycoprotein forms trimers stabilized by calcium ions, which are essential for maintaining the integrity of the triple-layered particle and locking the VP4 attachment protein in place [8, 11, 13]. During infection, the reduction of calcium concentrations within host cell endosomes triggers the dissociation of the VP7 layer, an event that is a prerequisite for viral uncoating and subsequent genome release into the host cytoplasm [8, 11]. As a highly immunogenic antigen, VP7 (G3) is the primary target for neutralizing antibodies that define the G-serotype of the virus and can induce polyclonal B-cell activation [12, 13]. It is a critical component of several globally licensed vaccines, such as the pentavalent RotaTeq and Rotasiil, and the neonatal-targeted candidate RV3-BB, which utilize G3-specific antigens to elicit protective immunity [1, 2, 10]. Therapeutic strategies targeting this molecule primarily focus on preventing severe dehydrating gastroenteritis in infants by inducing neutralizing antibody responses that block viral entry [1, 5, 8]. Monitoring the genetic diversity and mutation of the VP7 (G3) protein is also vital for assessing vaccine efficacy and the risk of serotype replacement in the population [5].

Other names

Rotavirus Glycoprotein VP7 (G3 serotype)Rotavirus G3 antigenVP7 serotype G3Major outer capsid glycoprotein VP7G3-serotype rotavirus protein

Prevention of viral entry and uncoating via antibody-mediated neutralization; induction of long-term humoral immunity through vaccination with live-attenuated strains expressing the G3 antigen [1, 8].