Summary
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.
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Olivo, M., Streckert, H.J. Studies on the single-shelled rotavirus receptor with a synthetic peptide derived from the cytoplasmic domain of NS28. Archives of Virology 140, 2151–2161 (1995). https://doi.org/10.1007/BF01323237
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DOI: https://doi.org/10.1007/BF01323237