Rotavirus spike glycoprotein VP8* domain (VP8*)

The rotavirus spike glycoprotein VP8* domain is the distal globular fragment of the spike protein VP4, generated by proteolytic cleavage of VP4 into VP8* and VP5* following viral binding to the host cell[5][1]. The VP8* domain forms the globular "head" of the spike and is directly responsible for recognizing and binding to specific host cell surface glycans—this glycan binding is essential for viral attachment, host cell entry, and subsequent infection[1][4][5]. Structural studies show that VP8* commonly adopts a galectin-like fold with a cleft for glycan binding, but the fold can vary among rotavirus groups[1][4]. Different rotavirus genotypes exhibit variation in the glycan specificity of VP8*: human rotavirus VP8* domains typically bind histo-blood group antigens (HBGAs) in a sialic acid-independent manner, while some animal strains use sialic acid or other carbohydrates as receptors[7][5][2]. VP8* is essential for host range, pathogenesis, and is a major determinant of zoonotic transmission and immune response[4][5]. Because of its key role in host recognition and cell entry, VP8* is considered a prime target for antiviral vaccines and neutralizing antibodies[1][4][5]. Current rotavirus vaccines may stimulate immune responses that include VP8*-specific neutralizing antibodies[2]. The high degree of sequence and structural variability within VP8* among diverse rotavirus strains is a core challenge for universal therapeutic targeting[1][5].

Other names

VP8 starRotavirus VP8*VP8* domainRotavirus outer capsid spike protein VP8*

Inhibition of virus attachment to host cell by blocking glycan interaction; Neutralizing antibodies that target VP8* to prevent viral entry