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Recognition of BCR-ABL positive leukemic blasts by human CD4+ T cells
elicited by primary in vitro immunization with a BCR-ABL breakpoint peptide
GJ Bosch, AM Joosten, JH Kessler, CJ Melief and OC Leeksma
Department of Immunohaematology and Bloodbank, Leiden University Hospital,
The Netherlands.
In chronic myeloid leukemia (CML) the classical 9;22 translocation results
in a BCR-ABL fusion gene, which encodes chimeric BCR-ABL fusion 210 kD
oncoproteins (p210BCR-ABL). The two main p210BCR-ABL fusion variants in
CML, b2a2 and b3a2 are examples of well characterized antigens expressed by
malignant cells. The possibility of an immunotherapeutic approach involving
the fusion part of p210BCR-ABL in CML has previously been illustrated by
observed peptide binding to major histocompatibility complex (MHC) class I
alleles and by demonstrating the immunogenicity of p210BCR-ABL breakpoint
peptides. In this report we show that in vitro immunization of human T
cells with a 17 amino acid (aa) peptide representing the p210BCR-ABL fusion
region resulted in peptide specific CD4+ T-cell lines designated P4, P6,
and P7. HLA DR4 (DRB1*0401) restricted T-cell line P4 and several
subsequently derived clones recognized HLA-DRB1*0401 and p210b3a2-mRNA
expressing blasts from an allogeneic patient with CML in blast crisis.
Recognition appeared DR expression-dependent. No responses were observed
with DR4 positive p210BCR-ABL negative cells or with p210b3a2 leukemic
cells with absent or insufficient expression of DR4. These observations
indicate that oncoprotein p210b3a2 can be degraded and processed for
presentation by MHC class II molecules at the surface of leukemic cells.
The BCR-ABL fusion region is in all likelihood presented as peptides by HLA
DR and thus capable to act as a distinctive tumor antigen to peptide
specific CD4+ T cells.
Volume 88,
Issue 9,
pp. 3522-3527,
11/01/1996
Copyright © 1996 by The American Society of Hematology
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