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Cryptic CTL Epitope on a Murine Sarcoma Meth A Generated by Exon Extension as a Novel Mechanism¹

Akiko Uenaka^*, Yoshiki Hirano^*, Hidenori Hata^*, Sanda Win^*, Toshiki Aji^*, Motoyuki Tanaka^*, Toshiro Ono^*, Jonathan C. A. Skipper, Kenji Shimizu and Eiichi Nakayama^2,*

Departments of ^* Immunology and Molecular Genetics, Okayama University Graduate School of Medicine and Dentistry, Okayama, Japan; and Ludwig Institute for Cancer Research, New York, NY 10058

Using the recently developed ELISPOT cloning methodology, we obtained cDNA clone S35 coding for the Ag epitope recognized by a murine sarcoma Meth A-specific CTL clone AT-1. Analysis of truncated S35 constructs and overlapping peptides revealed that the peptide epitope was LGAEAIFRL. AT-1 CTL lysed peptide-pulsed CMS8 cells at a nanomolar concentration, and the peptide strongly stimulated IFN- production in AT-1 CTL. Sequence homology indicated that the S35 was derived from a mouse homologue of human retinoic acid-regulated nuclear matrix-associated protein (ramp). The ramp gene consisted of 15 exons. The majority of the ramp mRNA was the transcript normally spliced between exons 14 and 15, but a minor population of mRNA with an extended exon 14 was also present in Meth A cells. The epitope was derived from the newly created open reading frame, which resulted from extension of exon 14 after splicing of the adjacent intronic sequence.

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