International Immunology, Vol 10, 891-899, Copyright © 1998 by Oxford University Press
BJ Green, GJ Clark and DN Hart
The CMRF-35 mAb recognizes an antigen found on most leukocytes including
monocytes, neutrophils, macrophages, dendritic cells, and subpopulations of
lymphocytes and bone marrow cells. A cDNA expressing the CMRF-35 epitope
was isolated by expression cloning and this predicts for a type I cell
surface glycoprotein belonging to the Ig superfamily. Here we demonstrate
that the CMRF-35 mAb recognizes an epitope more widely distributed on
hemopoietic cells and cell lines than suggested by expression analysis of
the CMRF-35 mRNA. Furthermore, we have isolated a novel cDNA (CMRF-35-H9)
that encodes a protein product also recognized by the CMRF-35 mAb. This
cDNA product is a type I cell surface glycoprotein with a single Ig V-like
domain. Although the sequences of the extracellular V-like domains of the
two molecules are very similar, there is little similarity between the
remainder of their sequences. The two transcripts are expressed
independently of each other, and their presence accounts for the
discrepancy between CMRF-35 mAb binding and mRNA analysis. The cytoplasmic
tail of CMRF-35- H9 contains motifs similar to the inhibitory motifs found
in some leukocyte surface receptors. Their expression in hemopoietic cells
suggests that these two molecules may play distinct but related roles in
the regulation of leukocyte function.
ARTICLES
The CMRF-35 mAb recognizes a second leukocyte membrane molecule with a domain similar to the poly Ig receptor
Haematology/Immunology/Transfusion Medicine Research Group, Christchurch School of Medicine, New Zealand.
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