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Centre d’Immunologie de Marseille-Luminy, Marseille, France
The surrogate light chain (SL) composed of the 
-like and VpreB
polypeptides is organized as two Ig domains and an extra-loop
structure. It associates to the µ-chain in preB cells. We have
produced human VpreB, SL, two Fdµ (VH-CH1),
and the two corresponding Fab-like (Fdµ-SL) recombinant proteins in
baculovirus. The correctness of the general conformation of the
proteins was assessed by epitope mapping and affinity measurements
using a new batch of anti-VpreB mAbs. Plasmon resonance analysis
showed that both VpreB and the entire SL associated with the Fdµ
fragments, with Kd values of 3 x
10-8 M for VpreB-Fdµ and of 10-9 to
10-10 M, depending upon the VH, for SL-Fdµ.
These results indicate that the -like chain, in addition to be
covalently bound to the Cµ1 domain, also interacts with the
VH domain. Therefore, a dual role of the SL emerges: 1)
interaction of the C-domain of -like would release the
µ-chain from its interaction with binding protein in the
endoplasmic reticulum, and 2) interaction of a part of -like
and most of VpreB would bind to VH, ensuring a "quality
control" of the native heavy chain that represents the first step of
selection of the B cell repertoire. We also demonstrated that two
Fab-like fragments did not interact with each other, suggesting that
activation of the cell surface preB receptor does not involve
aggregation neither in cis nor in trans
of the Fab-like structures.
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