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Naturally Processed Tissue- and Differentiation Stage-Specific Autologous Peptides Bound by HLA Class I and II Molecules of Chronic Myeloid Leukemia Blasts
Kyriakos P. Papadopoulos,
Nicole Suciu-Foca,
Charles S. Hesdorffer,
Sorina Tugulea,
Antonella Maffei, and
Paul E. Harris
From the Division of Medical Oncology/Hematology, Department of Medicine and the Division of Immunogenetics, Department of Pathology, College of Physicians and Surgeons of Columbia University, New York, NY.
Structural analysis of naturally processed peptides bound to the HLA class I and class II molecules of chronic myeloid leukemia (CML) blast cells was performed to characterize the antigen processing and autoantigen repertoire in this hematopoietic malignancy. Self-peptides derived from the carboxy-terminal end of the breakpoint cluster region (bcr) protein, as well as several differentiation stage- and tissue-specific self-antigens characteristic of early stages of myeloid differentiation, such as c-fes, c-pim, granulocyte-macrophage colony-stimulating factor receptor  chain, proteinase 3, and cathepsin G, were identified. A common characteristic of several of the high copy-number self-peptides identified in this study is the participation of their parent proteins in signal transduction or myeloid effector function. Because bcr-abl junctional peptides bind to a limited number of major histocompatibility complex (MHC) class I alleles, an effective peptide-based immunotherapy strategy for CML requires identification of further tumor-associated or tissue-specific peptide antigens binding to common MHC alleles such as HLA-A2. The differentiation stage- and tissue-specific MHC-bound peptides found in this study, as well as the naturally processed proteins from which they are derived, may represent autoantigens towards which T-cell responses may potentially be developed for immunotherapy of hematopoietic malignancies such as CML.
Blood, Vol. 90 No. 12 (December 15), 1997:
pp. 4938-4946
© 1997 by The American Society of Hematology.
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