Interaction between a "processed" ovalbumin peptide and Ia molecules
Research output: Contribution to journal › Journal article › Research › peer-review
The binding of 125I-labeled immunogenic peptides to purified Ia molecules in detergent solution was examined by equilibrium dialysis. We used the chicken ovalbumin peptide ovalbumin-(323-339)-Tyr, which is immunogenic in the BALB/c mouse and restricted to I-Ad. 125I-labeled ovalbumin-(323-339)-Tyr was shown to bind to I-Ad but not to I-Ed, I-Ek, or I-Ak. This binding was inhibited by unlabeled ovalbumin-(323-339) but not by ovalbumin-(329-339), which is the longest N-terminally truncated peptide that fails to stimulate any of the I-Ad-restricted hybridomas that have been raised to ovalbumin-(323-339)-Tyr. As a further specificity control, we also used the chicken egg lysozyme peptide Tyr-(46-61), which has recently been studied by similar methods [Babbitt, B. P., Allen, P. M., Matsueda, G., Haber, E. & Unanue, E. R. (1985) Nature (London) 317, 359-361]. We have confirmed that it bound to I-Ak but not to I-Ek, I-Ad, or I-Ed. Thus, a specific interaction between Ia and antigen that correlates with the major histocompatibility complex restriction was demonstrated, strongly arguing in favor of a determinant selection hypothesis for such restriction.
Original language | English |
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Journal | Proceedings of the National Academy of Science of the United States of America |
Volume | 83 |
Issue number | 11 |
Pages (from-to) | 3968-71 |
Number of pages | 3 |
ISSN | 0027-8424 |
Publication status | Published - 1986 |
Bibliographical note
Keywords: Animals; Antigen-Presenting Cells; B-Lymphocytes; Histocompatibility Antigens Class II; Mice; Ovalbumin; Peptide Fragments; Protein Binding; T-Lymphocytes
ID: 9948130