Journal of Experimental Medicine, Vol 156, 289-293, Copyright © 1982 by Rockefeller University Press
T lymphocyte recognition of peptide antigens: evidence favoring the formation of neoantigenic determinants
DW Thomas, MD Hoffman and GD Wilner
To more precisely define the nature of exogenous antigenic determinants
recognized by T cells, the response to fibrinopeptide fragment B beta 7- 14
and a peptide of the inverted amino acid sequence of B beta 7-14 was
examined. Strain 2 guinea pig T cells immunized with B beta 7-14 showed in
vitro proliferative responses with B beta 7-14, but failed to respond to
the inverted B beta 7-14 peptide. Moreover, the inverted B beta 7-14
peptide was nonimmunogenic and failed to prime strain 2 T cells for
responses to native or inverted B beta 7-14. These results suggest that T
cell recognition of peptide antigens involves more than simple interactions
with amino acid side chains and that the ordering of the amino acids within
the peptide is critical. One interpretation of these results is that T
cells exhibit polarity in reading of antigenic determinants and peptides
become associated with self in some fashion to form a neoantigenic
determinant. To test this possibility, a Gly residue was added to the
carboxyl end of B beta 7-14 (B beta 7-15), which is the likely site of
attachment to self. It was found that strain 13 guinea pigs, which are
totally unresponsive to B beta 7-14, produced T cell responses to B beta
7-15. This observation is consistent with the interpretation that Gly
spaces the B beta 7-14 away from self to form an antigenic determinant
complementary to strain 13 T cell antigen recognition structures. These
results are discussed with respect to several mechanisms for immune
response gene control of T cell responses.
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