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Division of Molecular Immunology, Department of Internal Medicine III, Nikolaus-Fiebiger Center, University of Erlangen-Nürnberg, Erlangen, Germany
Signals initiated by the precursor B cell receptor (pre-BCR) are
critical for B cell progenitors to mature into precursor B cells. The
pre-BCR consists of a homodimer of µH chains, the covalently
associated surrogate L (SL) chain composed of VpreB and 
5, and the
transmembrane signal molecules Ig
and Ig
. One way to explain how
maturation signals are initiated in late progenitor B cells is that the
pre-BCR is transported to the cell surface and interacts from there
with a ligand on stroma cells. To address this hypothesis, we first
produced soluble Fab-like pre-BCR and BCR fragments, as well as SL
chain, in baculovirus-infected insect cells. Flow cytometry revealed
that, in contrast to Fab-like BCR fragments, the soluble pre-BCR binds
to the surface of stroma and several other adherent cell lines, but not
to B and T lymphoid suspension cells. The specific binding of the
soluble pre-BCR to stroma cells is saturable, sensitive to trypsin
digestion, and not dependent on bivalent cations. The binding of
pre-BCR seems to be independent of the H chain of IgM (µH chain),
because SL chain alone was able to interact with stroma cells. Finally,
soluble pre-BCR specifically precipitated a 135-kDa protein from ST2
cells. These findings not only demonstrate for the first time the
capacity of a pre-BCR to specifically bind to a structure on the
surface of adherent cells, but also suggest that the pre-BCR interacts
via its SL chain with a putative ligand on stroma
cells.
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