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Site recognition by protein-primed T cells shows a non-specific peptide size requirement beyond the essential residues of the site Demonstration by defining an immunodominant T site in myoglobin

Garvin S. BixlerDepartment of Biochemistry, Baylor College of Medicine, Houston, TX 77030, U.S.AMark F. BeanDepartment of Biochemistry, Baylor College of Medicine, Houston, TX 77030, U.S.AM. Zouhair AtassiDepartment of Biochemistry, Baylor College of Medicine, Houston, TX 77030, U.S.A
1986en
ABI

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In previous studies, six T sites within myoglobin (Mb) were localized. To define precisely the boundaries of the T sites, a new approach is introduced and applied here to the T site residing within residues 107-120 of Mb. Two sets of peptides were synthesized. One set represents a stepwise elongation by one-residue increments of the Mb sequence. The other set represents an identical stepwise addition of one-residue increments of the Mb sequence, but which were extended by additional unrelated (nonsense) residues to a uniform size of 14 residues. The longer peptides (nonsense-extended) usually gave higher proliferative responses than did their shorter counterparts having the same Mb region. Thus a minimum peptide size is required for optimal T-cell stimulation. The T site subtends, in three high-responder mouse strains, residues 109-119 or 110-120, depending on strain, and, in three low-responder strains, maps to residues 108-120. Thus, in this case, the T site coincides with the site of B-cell recognition and resides in a small discrete surface region of the protein chain.

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