Mouse immunoglobulin (Ig) molecules have previously been shown to bind to t
he surface of CD5(+) B cells from patients with B-cell chronic lymphocytic
leukemia (B-CLL). The results indicated that surface IgM was involved in th
e interaction and suggested the phenomenon was an example of the polyreacti
ve binding capacity of the surface Ig (sIg) expressed by these malignant ce
lls. This article describes the further characterization of the interaction
between human IgM and mouse Ig molecules and subunits. Mouse Ig molecules
of both kappa and lambda light chain classes bound to the B-CLL cell surfac
e. The dissociation constant for the interaction of mouse IgG1 (K121) with
the B-CLL cell surface was 3.6 x 10(-7) m. To confirm the involvement of th
e human IgM expressed by the B-CLL cells in the interaction, the malignant
cells were stimulated in vitro to induce secretion of human IgM. Enzyme imm
unoassay was used to show that secreted human IgM bound to intact mouse Ig,
as occurred with the cell surface analysis. The mouse Ig epitope recognize
d by the purified secreted human IgM was shown by Western blot analysis to
be located on the light chain of the mouse Ig molecule and to be conformati
onally dependent. K121 light chain was cloned and expressed in E. coli and
the recombinant light chain bound to the surface of CLL B cells. The result
s confirm that human IgM is the reactive ligand in the interaction with mou
se Ig and indicate that the interaction of polyreactive IgM with mouse IgG
occurs via the light chain component of IgG. Copyright (C) 2001 John Wiley
& Sons, Ltd.