Kirschmann D A, De Ciechi P A, Bono C P, Zacheis M L, Schwartz B D, Woulfe S L
Department of Immunology and Glycobiology, Monsanto Corporate Research/G. D. Searle, St. Louis, Missouri 63198, USA.
Cell Immunol. 1995 Feb;160(2):193-8. doi: 10.1016/0008-8749(95)80027-g.
A peptide display library was evaluated as a means to identify peptide binding motifs for class II molecules. Peptides expressed as part of a soluble fusion protein with a maltose binding protein (malE) were produced by Escherichia coli. Constructs containing the high-affinity binding influenza hemagglutinin peptide 307W-319 (mal-HA) or the low-affinity binding tetanus toxoid peptide 830-843 (mal-TT) were used as controls. mal-HA, but not mal-TT, inhibited synthetic biotinylated-HA peptide from binding to purified DR4 Dw4 molecules in a dose-dependent manner. The fusion-peptide presentation system was also evaluated for its ability to induce antigen-specific T cell proliferation. DR4 Dw4+ B cells pulsed with mal-HA, but not mal-TT, induced dose-dependent proliferation of an HA-specific DR4 Dw4-restricted T cell line to the same extent as synthetic HA peptide. Using this type of peptide display library, it may be possible to determine the antigenic specificity of T cell clones isolated from patients with autoimmune diseases.
