作者: Emil R. Unanue , Clifford V. Harding , David S. Collins
DOI:
关键词: Antigen presentation 、 Antigen processing 、 Endocytic cycle 、 Peptide 、 Proteolysis 、 Chemistry 、 Biochemistry 、 Protein disulfide-isomerase 、 Lysosome 、 Endosome
摘要: Reduction of disulfide bonds is a key step in antigen processing both to allow the unfolding of protein antigens, increasing the access of proteolytic processing enzymes, and to expose free Cys residues within linear peptide epitopes recognized by T cells. We show here that reduction and alkylation of Ag (hen egg lysozyme and ribonuclease A) vastly increased their proteolysis (by specific enzymes or lysosomal fractions) and the production of specific immunogenic peptides that bound to class II MHC molecules recognized by T hybridoma …