Rotavirus outer capsid glycoprotein VP7 and spike protein VP4 (VP7 and VP4)

The Rotavirus outer capsid glycoprotein VP7 and spike protein VP4 are the two primary structural proteins forming the outermost layer of the rotavirus virion [6, 15]. VP4 functions as a spike protein that mediates viral attachment to host cells and is proteolytically cleaved by trypsin into VP8* and VP5* subunits to facilitate membrane penetration [5, 12]. VP7 is a calcium-dependent glycoprotein that forms the bulk of the outer capsid and interacts with host co-receptors, such as integrins, to mediate viral entry and subsequent uncoating (decapsidation) within the host cell [2, 4, 16]. These proteins are the principal targets for neutralizing antibodies and serve as the basis for the G (glycoprotein) and P (protease-sensitive) dual classification system for rotavirus strains [1, 7, 14]. Therapeutic strategies, primarily live-attenuated vaccines like Rotarix and RotaTeq, target these proteins to elicit protective immunity against severe gastroenteritis in infants [8, 13, 18]. Ongoing research also explores monoclonal antibodies and subunit vaccines targeting specific domains of VP4 and VP7 to overcome challenges like antigenic diversity and vaccine-escape mutants [10, 13, 19].

Other names

G proteinP proteinOuter capsid proteinsVP7 glycoproteinVP4 spike proteinNeutralization antigens

Induction of neutralizing antibodies that inhibit viral attachment, membrane penetration, and virion decapsidation [5, 16, 18].