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T‐ LYMPHOCYTE RECOGNITION OF SPERM‐WHALE MYOGLOBIN. RECOGNITION OF SYNTHETIC PEPTIDES CARRYING ANTIGENIC SITE 5 BY MYOGLOBIN‐PRIMED T‐CELLS
Author(s) -
Young C. R.,
Atassi* M. Z.
Publication year - 1983
Publication title -
international journal of immunogenetics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.41
H-Index - 47
eISSN - 1744-313X
pISSN - 1744-3121
DOI - 10.1111/j.1744-313x.1983.tb01026.x
Subject(s) - myoglobin , sperm whale , peptide , antigen , epitope , t lymphocyte , biology , t cell , microbiology and biotechnology , biochemistry , sperm , chemistry , immune system , immunology , genetics
SUMMARY Previous studies from this laboratory have resulted in the determination of the antigenic structure of sperm‐whale myoglobin (Mb). In the present work, we have investigated the fine specificity requirements for T‐cell recognition of one of the Mb antigenic sites (antigenic site 5). The antigenic site (peptide 145‐153) and seven progressively longer peptides, increasing in length stepwise by two residues at a time, up to 22 residues in length (peptide 132‐153), were synthesized. In addition, four truncated peptides were synthesized with intentional deletions at Tyr‐ 151 and Ala‐ 144. The T‐cell recognition of these purified synthetic peptides was examined here in detail in three strains of mice (BALB/cByJ, B10.D2/n and SJL/J). Mb‐primed mice afforded T‐cells which proliferated to smaller peptides (two or four residues longer than the site; i.e. peptides 145‐153 and 143‐153) and more so to the longer peptides 135‐153 and 132‐153 and to Mb. No response was obtained to the truncated peptides, thus underscoring the fine specificity T‐cells. No response was obtained also to intermediate‐sized peptides. The latter result, due to an unfavourable mode of folding, suggested a conformational dependency in T‐lymphocyte recognition.