61 Scopus citations


We examined the specificity of glycopeptide-specific CD4 T cells following procedures similar to those previously reported by us. The disaccharide galabiose (Galα1-4Gal) was attached to the middle of the 52-61 peptide of hen egg lysozyme. This peptide is well known to bind to I-A(k) molecules. CBA/J mice were immunized and T cell hybridomas were derived from the popliteal lymph node T cells. For this study, we selected hybridomas that recognized galabiose conjugated to 52-61 at residue Ser 56. We demonstrate here that these hybridomas showed specificity for galabiose and not cellobiose (Glcβ1-4Glc). Peptides containing galabiose at residue 53 did not stimulate the T cell hybridomas and neither did galabiose conjugated to the 34-45 peptide of HEL. Acetylation of the hydroxyl groups of the disaccharide resulted in loss of T cell reactivity. These results need to be contrasted with those in which the T cells were directed to galabiose, attached to the amino terminus of 52-61 or to Ser at residue 53. With these results, the fine specificity of recognition of the disaccharide was not apparent. Our results indicate two sets of glycopeptide-specific T cells. One is probably induced by a conformational change induced by the disaccharide on the peptide bound to class II MHC molecules. The second set contains elements of specificity for both the disaccharide and the peptide.

Original languageEnglish
Pages (from-to)1074-1078
Number of pages5
JournalJournal of Immunology
Issue number3
StatePublished - 1995


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