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Dissection of binding vs. recognition functions of H‐2 class‐I synthetic peptides which are recognized by alloreactive cytotoxic T lymphocytes
Author(s) -
Olson Clifford A.,
McMillan Minnie
Publication year - 1991
Publication title -
international journal of cancer
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.475
H-Index - 234
eISSN - 1097-0215
pISSN - 0020-7136
DOI - 10.1002/ijc.2910470710
Subject(s) - allorecognition , cytotoxic t cell , ctl* , peptide , biology , major histocompatibility complex , cytotoxicity , mhc class i , t cell receptor , immunology , microbiology and biotechnology , antigen , t cell , biochemistry , immune system , in vitro
Cytotoxic T lymphocytes (CTLs) cause specific destruction of allografts and viral‐infected cells. While viral‐restricted CTLs recognize viral peptides in association with class‐1 molecules encoded in the major histocompatibility complex, the role which peptides play during allorecognition remains obscure. We have shown previously that L d ‐specific alloreactive CTLs can recognize the peptide L d 61‐80 (or L d 61‐85) in association with the dm I class‐1 molecule. We have now developed an assay, based on inhibition of cytotoxicity, in which we can monitor peptide binding to the dm I molecule in the absence of CTL recognition. In this report we have used this assay to differentiate those amino acids of the peptide L d 61‐80 which contribute to class‐1 binding from those involved with T‐cell‐receptor (TCR) interactions.