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.
Olivo
M
M
Abteilung für Medizinische Mikrobiologie und Virologie, Ruhr-Universität Bochum, Federal Republic of Germany.
Streckert
H J
HJ
D000818:Animals; D000906:Antibodies; D018870:Endoplasmic Reticulum, Rough / Q000502:physiology / Q000821:virology; D004797:Enzyme-Linked Immunosorbent Assay; D006023:Glycoproteins / Q000032:analysis / Q000378:metabolism*; D006168:Guinea Pigs / Q000276:immunology; D006801:Humans; D016253:Microscopy, Immunoelectron; D010455:Peptides / Q000138:chemical synthesis / Q000276:immunology; D011991:Receptors, Virus / Q000502:physiology*; D012401:Rotavirus / Q000502:physiology*; D014118:Toxins, Biological; D017361:Viral Nonstructural Proteins / Q000032:analysis / Q000378:metabolism*
D000906:Antibodies; D006023:Glycoproteins; C081369:NS28 protein, rotavirus; D010455:Peptides; D011991:Receptors, Virus; D014118:Toxins, Biological; D017361:Viral Nonstructural Proteins