Important quantitative parameters can be utilized to define the selection and the immunogenicity of protein antigens precisely at a biochemical and a cellular level. Here we describe a naturally processed family of peptides comprising the dominant hen egg white lysozyme epitope, its major contribution to surface I-A(k) molecules, the primary and auxiliary peptide anchors involved in its selection, and its display of T-cell receptor contacts. In addition, we explore the importance of the processing events that lead to the generation of residues flanking the minimal core epitope, the quantification of T-cell responses directed toward the epitope, and the ability of the dominant epitope to form two unique conformations within the binding groove. Lastly, we address the relationship between this dominant and a minor lysozyme epitope.
|Number of pages||20|
|State||Published - Jan 1 1999|