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Blood, Vol. 95 No. 9 (May 1), 2000:
pp. 2890-2896
Defensins are dominant HLA-DR-associated self-peptides from
CD34 peripheral blood mononuclear cells of different
tumor patients (plasmacytoma, chronic myeloid leukemia)
Thomas M. Halder,
Martin Blüggel,
Susanne Heinzel,
Graham Pawelec,
Helmut E. Meyer, and
Hubert Kalbacher
From the Medical and Natural Sciences Research Center, Section for
Transplantation Immunology and Immunohaematology, University of
Tübingen, Tübingen, Germany; Institute of Physiological
Chemistry, University of Bochum, Bochum, Germany.
The HLA-DR-associated peptides from peripheral blood mononuclear
cells of 2 patients with plasmacytoma and 1 with chronic myeloid
leukemia were isolated, identified, and compared. Several were
identified as derivatives of the defensin family. Defensins (or human
neutrophil peptides [HNP]) are antimicrobial, cationic peptides of 29 to 35 amino acids in length and are the major constituents of the
azurophilic granules of human neutrophils. Using peripheral blood cells
from leukapheresis, containing about 90% of polymorphonuclear cells,
we could identify HNP-1, -2, and -4 and propeptides of up to 49 amino
acids in length, eluted from HLA class II molecules. Binding of
isolated and synthetic defensin peptides to various HLA-DR alleles
using an in vitro binding/competition assay based on size exclusion
chromatography revealed that defensin may bind into the peptide-binding
groove. In a T-cell competition assay, defensins were able to reduce
the proliferation of an HLA-DR-restricted T-cell line after
preincubation of stimulating cells (CHO-DRB1*0401 transfectants) with
defensin. Therefore, binding of defensins might prevent T-cell
recognition of HLA class II molecules expressed on different blood
precursor cells (all of which are "nonprofessional" antigen-presenting cells) by blocking the HLA peptide-binding groove
or, alternatively, might protect defensin-expressing cells from
self-destruction.
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