Cellular and humoral immune responses to synthetic peptides deduced from the amino-acid sequences of Epstein-Barr virus-encoded proteins in EBV-transformed cells

✍ Scribed by Joakim Dillner; Robert Szigeti; Werner Henle; Gertrude Henle; Richard A. Lerner; George Klein

• Publisher: John Wiley and Sons
• Year: 1987
• Tongue: French
• Weight: 576 KB
• Volume: 40
• Category: Article
• ISSN: 0020-7136
• DOI: 10.1002/ijc.2910400404

✦ Synopsis

Ten synthetic peptides containing 18-22 residues deduced from the amino-acid sequences of the EBV-encoded latentinfection-associated membrane protein (LMP) and the 2 principal nuclear antigens, EBNA-I and EBNA-2, were tested for their ability to induce lymphokine release from sensitized Tcells of EBV-seropositive donors, as measured by the leukocyte migration inhibition assay (LMI). Only one of the 10 free peptides induced EBV-specific LMI. After Sepharose-coupling, 4 additional peptides were regularly active. In parallel, the sera of the same and other donors were screened for synthetic peptide-binding antibodies, as measured by an ELSA assay. Antibodies to 9 of the 10 peptides were detected in 25-80% of EBV-antibody-positive, but not in EBV-antibody-negative sera. A comparison of the two responses indicates that the humoral immune system tends to react with more epitopes on a given protein than the cellular immune system. Furthermore. the antibody reactivity pattern to different epitopes is more variable from individual to individual than the T-cell response. Also, the epitopes detected by antibodies and sensitized Tcells are often not identical.