Studies on the single-shelled rotavirus receptor with a synthetic peptide derived from the cytoplasmic domain of NS28.

The nonstructural glycoprotein NS28 of rotaviruses plays an important part in the assembly of double-shelled rotaviruses. C-terminal domains of the protein function as a receptor for single-shelled rotavirus particles at the membrane of the rough endoplasmic reticulum. In the present report we describe studies performed with a synthetic peptide corresponding to amino acid (aa) 160 to 169, the most hydrophilic C-terminal epitope of NS28. An antipeptide serum raised against this peptide demonstrated that this epitope was accessible in infected MA104 cells. Moreover, polymeric peptide was demonstrated to aggregate single-shelled rotavirus particles. This aggregation could be almost completely inhibited by preincubation with monomeric peptide. Our results clearly demonstrate that the epitope corresponding to aa 160-169 is able to bind single-shelled rotavirus particles.