Epitopes described in "Polymorphism within the herpes simplex virus (HSV) ribonucleotide reductase large subunit (ICP6) confers type specificity for recognition by HSV type 1-specific cytotoxic T lymphocytes."

Reference
Article Authors:L A Salvucci; R H Bonneau; S S Tevethia
Article Title:Polymorphism within the herpes simplex virus (HSV) ribonucleotide reductase large subunit (ICP6) confers type specificity for recognition by HSV type 1-specific cytotoxic T lymphocytes.
Reference Detail
Reference ID:1004099
Abstract:A panel of herpes simplex virus type 1 (HSV-1)-specific, CD8+, major histocompatibility complex class I (H-2Kb)-restricted cytotoxic T-lymphocyte (CTL) clones was derived from HSV-1-immunized C57BL/6 (H-2b) mice in order to identify the HSV-1 CTL recognition epitope(s) which confers type specificity. HSV-1 x HSV-2 intertypic recombinants were used to narrow the region encoding potential CTL recognition epitopes to within 0.51 to 0.58 map units of the HSV-1 genome. Using an inhibitor of viral DNA synthesis and an ICP6 deletion mutant, the large subunit of ribonucleotide reductase (ICP6, RR1) was identified as a target protein for these type-specific CTL. Potential CTL recognition epitopes within RR1 were located on the basis of the peptide motif predicted to bind to the MHC class I H-2Kb molecule. A peptide corresponding to residues 822 to 829 of RR1 was shown to confer susceptibility on H-2Kb-expressing target cells to lysis by the type 1-specific CTL. On the basis of a comparison of the HSV-1 RR1 epitope (residues 822 to 829) with the homologous sequence of HSV-2 RR1 (residues 828 to 836) and by the use of amino acid substitutions within synthetic peptides, we identified HSV-1 residue 828 as being largely responsible for the type specificity exhibited by HSV-1-specific CTL. This HSV-1 RR1 epitope, when expressed in recombinant simian virus 40 large T antigen in primary C57BL/6 cells, was recognized by the HSV-1 RR1-specific CTL clones. These results indicate that an early HSV protein with enzymatic activity provides a target for HSV-specific CTL and that type specificity is dictated largely by a single amino acid.
Date:1995
Reference Type:Literature
PubMed ID:7529328
Journal:J Virol
Journal Volume:69
Article Pages:1122-31
Journal ISSN:1098-5514
Article Chemical List:Antigens, Polyomavirus Transforming;Epitopes;H-2 Antigens;H-2Kb protein, mouse;Viral Proteins;herpes simplex virus type 1-protein ICP6;Dactinomycin;Ribonucleotide Reductases
Article MeSH List:Amino Acid Sequence; Animals; Antigens, Polyomavirus Transforming(immunology); Dactinomycin(pharmacology); Epitopes(genetics); H-2 Antigens(immunology); Herpesvirus 1, Human(genetics; immunology); Mice; Mice, Inbred C57BL; Molecular Sequence Data; Polymorphism, Genetic; Ribonucleotide Reductases(immunology); T-Lymphocytes, Cytotoxic(immunology); Viral Proteins(immunology)
Curation Last Updated:2014-07-16 20:59:33