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Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1986 Jun;83(11):3968–3971. doi: 10.1073/pnas.83.11.3968

Interaction between a "processed" ovalbumin peptide and Ia molecules.

S Buus, S Colon, C Smith, J H Freed, C Miles, H M Grey
PMCID: PMC323646  PMID: 3487084

Abstract

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.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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