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Science 8 September 2006:
Vol. 313. no. 5792, pp. 1444 - 1447
DOI: 10.1126/science.1130660
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Reports

An Antigen Produced by Splicing of Noncontiguous Peptides in the Reverse Order

Edus H. Warren,1,2 Nathalie J. Vigneron,4,5* Marc A. Gavin,1,3 Pierre G. Coulie,5 Vincent Stroobant,4,5 Alexandre Dalet,4,5 Scott S. Tykodi,1,2 Suzanne M. Xuereb,1 Jeffrey K. Mito,1 Stanley R. Riddell,1,2 Benoît J. Van den Eynde4,5{dagger}

CD8-positive T lymphocytes recognize peptides that are usually derived from the degradation of cellular proteins and are presented by class I molecules of the major histocompatibility complex. Here we describe a human minor histocompatibility antigen created by a polymorphism in the SP110 nuclear phosphoprotein gene. The antigenic peptide comprises two noncontiguous SP110 peptide segments spliced together in reverse order to that in which they occur in the predicted SP110 protein. The antigenic peptide could be produced in vitro by incubation of precursor peptides with highly purified 20S proteasomes. Cutting and splicing probably occur within the proteasome by transpeptidation.

1 Program in Immunology, Clinical Research Division, Fred Hutchinson Cancer Research Center, Seattle, WA 98109, USA.
2 Department of Medicine, University of Washington, Seattle, WA 98195, USA.
3 Department of Immunology, University of Washington, Seattle, WA 98195, USA.
4 Ludwig Institute for Cancer Research, Brussels Branch, B-1200 Brussels, Belgium.
5 Cellular Genetics Unit, Institute of Cellular Pathology, Université Catholique de Louvain, B-1200 Brussels, Belgium.

* Present address: Yale University School of Medicine, Section of Immunobiology, New Haven, CT 06510, USA.

{dagger} To whom correspondence should be addressed. E-mail: benoit.vandeneynde{at}bru.licr.org

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