T细胞进展TCRMHC.ppt

* * * Green: anchor residues red: carboxyl termini blue: amino termini F: phenylalanine Y: tyrosine V: valin L: leucine I: isoleucine The upper and the lower panels show peptides that bind to two different alleles of MHC class I molecules respectively. Peptides also bind to MHC class I molecules through their amno (blue) and caboxyl termini. * The upper panel: a set of peptides that bind to the mouse MHC class II molecules AK allele. All contain the same core sequence but differ in length. The lower panel: different peptides binding to the human MHC class II allele HLA-DR3. The lengths of these peptides can vary, and so by convention the first anchor residue is denoted as residue 1. Note that all of the peptides share a negatively charged residue (aspartic acid (D) or glutamic acid (E) in P4 position (blue) and tend to have a hydrophobic residue (for example, tyrosin (Y), leucin (L), phenylalanine (F)), in P9 position (green) * * * * * * * * * * * * * Figure 1. Schematic illustration of major steps in this work (A) Via the interaction of the Fc part and IgG Fc receptor type I (Fc?RI), binding of a dimeric HLA-DR15/IgG1-Fc fusion protein (the dimer) to HLA-DR15-ve monocytes makes the monocytes loaded with the allogeneic epitope. (B) The E7/HLA-DR15 dimer-loaded monocytes “present” the allogeneic epitope to autologous lymphocytes when co-culturing in vitro. (C) The expended CD4+ T cells exhibit allo-restricted and E7-specific properties. (D) Tumor rejection effects of the allo-restricted E7-specific CD4+ T cells are observed in nude mice challenged with human cervical cancer cell SiHa expressing both HLA-DR15 and E7 antigen. Dengue virus NS3 protein Human Papillomavirus * Figure 2. Preparation of the HLA-DR15/IgG1-Fc fusion protein and its binding to HLA-DR15-ve monocyte (A) Schematic structure of HLA-DR15/IgG1-Fc fusion protein (the dimer). The extracellular domains of HLA-DR? and ? are associated by leucine zipper dimerization domains from the transcription