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 pa rticles at the membrane of the rough endoplasmic reticulum. In the pre sent report we describe studies performed with a synthetic peptide cor responding to amino acid (aa) 160 to 169, the most hydrophilic C-termi nal 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-shel led rotavirus particles. This aggregation could be almost completely i nhibited by preincubation with monomeric peptide. Our results clearly demonstrate that the epitope corresponding to aa 160-169 is able to bi nd single-shelled rotavirus particles.