Rotavirus outer capsid glycoprotein VP7 (G2 type) (VP7 (G2))

Rotavirus outer capsid glycoprotein VP7 (G2 type) is a critical structural protein of the rotavirus virion, forming the outermost icosahedral shell. It is a 37-kDa calcium-binding glycoprotein that organizes into 260 trimers, which are essential for maintaining the integrity of the viral particle [1.3.1, 1.3.5]. VP7 is the primary determinant of the G-serotype classification and serves as a major target for neutralizing antibodies during infection [1.2.1, 1.3.4]. The G2 type is one of the most prevalent serotypes causing severe gastroenteritis in infants and young children worldwide [1.2.2, 1.4.3]. Biologically, VP7 facilitates viral entry by undergoing decapsidation upon exposure to low calcium environments in the host cell, a process that triggers the release of the viral core [1.3.1, 1.3.3]. In the context of therapeutics, VP7 G2 is a key antigen included in multivalent live-attenuated vaccines, such as RotaTeq and Rotasiil, to elicit protective immunity [1.4.3, 1.4.5]. Neutralizing antibodies against VP7 typically act by stabilizing the trimeric structure, thereby preventing the uncoating necessary for infection [1.1.1, 1.3.3]. Monitoring the genetic evolution of the G2 type is vital, as mutations in its antigenic regions, such as the D96N substitution, can lead to vaccine escape and shifts in dominant circulating strains [1.2.2, 1.3.4].

Other names

Outer capsid glycoprotein VP7G-proteinG2 serotypeVP7 proteinRotavirus A VP7

Vaccines containing the VP7 G2 antigen induce the production of G2-specific neutralizing antibodies. These antibodies bind to major antigenic sites (A, B, and C) on the VP7 trimer, preventing viral entry by blocking attachment or by stabilizing the trimer to inhibit the calcium-dependent uncoating process required for infection [1.1.1, 1.3.3, 1.3.4].