Rotavirus VP8* antigen (VP8*)

Rotavirus VP8* is the distal, globular head of the VP4 spike protein, generated through the proteolytic cleavage of VP4 by intestinal trypsins into VP8* and VP5* subunits. It functions as the primary viral attachment protein, mediating the initial recognition of host cells by binding to specific glycans, such as sialic acids in some animal strains or histo-blood group antigens (HBGAs) like Lewis and H-type antigens in human strains. This interaction is a critical determinant of viral host range, tissue tropism, and the P-genotype classification of rotaviruses. As the major target for neutralizing antibodies, VP8* is the primary focus for developing next-generation, non-replicating parenteral vaccines, including subunit and nanoparticle-based candidates like P2-VP8* and P24-VP8*. These vaccines aim to elicit high titers of antibodies that sterically block the VP8*-glycan interaction, thereby preventing viral entry and protecting against severe gastroenteritis. Additionally, some studies suggest that VP8* may modulate epithelial tight junctions to facilitate viral spread or drug delivery. The development of VP8*-based vaccines is particularly important for improving protection in low-income regions where current live-attenuated oral vaccines show reduced efficacy.

Other names

VP8* domainVP4 N-terminal fragmentRotavirus spike protein headP-genotype antigenVP8 fragment

Vaccine immunogen that elicits neutralizing antibodies to block viral attachment to host cell receptors.