Posttranslational side chain modification of a viral epitope results in diminished recognition by specific T cells.
A stretch of 16 amino acid residues within the nominal phosphoprotein of rabies virus was shown to carry an immunodominant epitope for class I- and class II-restricted T cells. The nominal phosphoprotein of rabies virus is thought to be heterogeneously phosphorylated at multiple serine and threonine residues. The synthetic peptide that expressed the T-cell epitope contained a single serine residue corresponding to position 196 of the protein. Phosphorylation of this serine within the synthetic peptide caused a significant decrease of the antigenic potency of the peptide. A similar effect was seen if the serine was replaced by an alanine or if the peptide was glycosylated at its acidic residues. These data suggest that T-cell-mediated recognition of antigen presented by major histocompatibility complex class I- or II-positive cells is impaired not only by point mutations but also by posttranslational side chain modifications of residues within viral epitopes.
Larson
J K
JK
Wistar Institute, Philadelphia, Pennsylvania 19104.
Otvos
L
L
Ertl
H C
HC
D000595:Amino Acid Sequence; D000818:Animals; D002213:Capsid / Q000276:immunology* / Q000378:metabolism; D002460:Cell Line; D002851:Chromatography, High Pressure Liquid; D000939:Epitopes / Q000276:immunology* / Q000378:metabolism; D005260:Female; D006031:Glycosylation; D007700:Kinetics; D051379:Mice; D008809:Mice, Inbred C3H; D008969:Molecular Sequence Data; D010766:Phosphorylation; D011499:Protein Processing, Post-Translational; D011820:Rabies virus / Q000276:immunology* / Q000378:metabolism; D013601:T-Lymphocytes / Q000276:immunology*; D014758:Viral Core Proteins / Q000276:immunology* / Q000378:metabolism; D017361:Viral Nonstructural Proteins
D000939:Epitopes; D014758:Viral Core Proteins; D017361:Viral Nonstructural Proteins