TY - JOUR
T1 - Antigenic competition at the level of peptide-Ia binding
AU - Babbitt, B. P.
AU - Matsueda, G.
AU - Haber, E.
AU - Unanue, E. R.
AU - Allen, P. M.
PY - 1986
Y1 - 1986
N2 - We examined the direct binding of a hen egg white lysozyme peptide, HEL(46-61), to membrane I-A(k) (protein encoded in the A locus of the I region) molecules in the presence of detergent. A number of synthetic peptide derivatives, which did not stimulate our T-cell reactive hybridomas, competed for the binding of HEL(46-61) to I-Aκ and also inhibited the functional presentation of HEL (46-61). Inhibitors included a peptide lacking a tyrosine at position 53 and a peptide corresponding to the autologous lysozyme peptide. Presentation was examined with cells or with supported planar phospholipid membranes bearing only I-A(k) and HEL(46-61). Other peptides that did not complete for the binding did not inhibit functional presentation. We concluded that the binding of an immunogenic peptide to I-A is critical for presentation, that the I-A molecule does not discriminate between autologous and foreign related determinants but does recognize structurally different peptides. Our evidence suggests that our immunogenic peptide bears noncontiguous amino acids critical for contact I-A binding interspersed with amino acids critical for interaction with T cells.
AB - We examined the direct binding of a hen egg white lysozyme peptide, HEL(46-61), to membrane I-A(k) (protein encoded in the A locus of the I region) molecules in the presence of detergent. A number of synthetic peptide derivatives, which did not stimulate our T-cell reactive hybridomas, competed for the binding of HEL(46-61) to I-Aκ and also inhibited the functional presentation of HEL (46-61). Inhibitors included a peptide lacking a tyrosine at position 53 and a peptide corresponding to the autologous lysozyme peptide. Presentation was examined with cells or with supported planar phospholipid membranes bearing only I-A(k) and HEL(46-61). Other peptides that did not complete for the binding did not inhibit functional presentation. We concluded that the binding of an immunogenic peptide to I-A is critical for presentation, that the I-A molecule does not discriminate between autologous and foreign related determinants but does recognize structurally different peptides. Our evidence suggests that our immunogenic peptide bears noncontiguous amino acids critical for contact I-A binding interspersed with amino acids critical for interaction with T cells.
UR - http://www.scopus.com/inward/record.url?scp=0022494327&partnerID=8YFLogxK
U2 - 10.1073/pnas.83.12.4509
DO - 10.1073/pnas.83.12.4509
M3 - Article
C2 - 3459185
AN - SCOPUS:0022494327
SN - 0027-8424
VL - 83
SP - 4509
EP - 4513
JO - Proceedings of the National Academy of Sciences of the United States of America
JF - Proceedings of the National Academy of Sciences of the United States of America
IS - 12
ER -