IMMUNOGENICITY OF MICROBIAL PEPTIDES GRAFTED IN SELF IMMUNOGLOBULIN MOLECULES

The advent of genetic engineering has allowed for the expression and p roduction of recombinant proteins carrying short immunogenic epitopes of foreign antigens. These antigenized molecules represent valuable to ols to investigate the molecular basis of antigen fragmentation, gener ation and presentation of peptide to lymphocytes, the induction of epi tope specific immunity and potentially the development of a new genera tion of vaccines. Recently, we expressed viral epitopes on immunoglobu lin molecules by replacing the D segment of a variable region of the h eavy chain (VH) gene with a B cell epitope from the V-3-loop of HIV-1 envelope protein, as well as a cytotoxic T lymphocyte (CTL) and a T he lper epitope from influenza virus nucleoprotein and hemagglutinin, res pectively. The T cell peptides generated from the immunoglobulin molec ules produced by cells transfected with chimeric V genes, activated sp ecific T cells as they do when generated from viral proteins. Possible practical applications for the development of prophylactic and immuno therapeutic reagents are envisioned for immunoglobulin molecules beari ng foreign epitopes.