K. Udaka et al., A UBIQUITOUS PROTEIN IS THE SOURCE OF NATURALLY-OCCURRING PEPTIDES THAT ARE RECOGNIZED BY A CD8-CELL CLONE( T), Proceedings of the National Academy of Sciences of the United Statesof America, 90(23), 1993, pp. 11272-11276
We previously isolated from mouse spleen an octapeptide (LSPFPFDL) tha
t in association with the class I major histocompatibility complex pro
tein L(d) is recognized by the antigen-specific receptor of an allorea
ctive CD8+ T-cell clone (2C). Guided by an assay dependent upon the sa
me 2C T-cell receptor, we have now isolated from the same source anoth
er naturally occurring peptide. The second peptide (VAITRIEQLSPFPFDL)
includes the entire octapeptide sequence and preliminary evidence sugg
ests that it may be a natural precursor of the octapeptide. On finding
extensive sequence homology between the 16-mer and part of human 2-ox
oglutarate dehydrogenase, we determined the cDNA sequence of mouse 2-o
xoglutarate dehydrogenase and found that the deduced amino acid sequen
ce matches precisely the two naturally occurring peptides, indicating
their origin by cellular processing of this ubiquitous self protein.