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Updated: Aug 9, 2026

Production of Disulfide-stabilized Transmembrane Peptide Complexes for Structural Studies
Published on: March 6, 2013
The human (PsiL+mu-) proB complex: cell surface expression and biochemical structure of a putative transducing
B Lemmers1, L Gauthier, V Guelpa-Fonlupt
1Centre d'Immunologie de Marseille-Luminy, Marseille, France.
Insights
New monoclonal antibodies reveal the surrogate light chain (PsiL) on proB cells, identifying a novel PsiL+mu- complex involved in early B-cell differentiation signaling.
Area of Science:
- Immunology
- Cell Biology
- Hematopoiesis
Background:
- The surrogate light chain (PsiL) is crucial for pre-B cell receptor formation and early B-cell differentiation.
- The presence of PsiL+mu- proB cells and the structure of their associated complex remain unclear in humans.
Purpose of the Study:
- To investigate the expression and biochemical characteristics of the surrogate light chain (PsiL) in proB cells.
- To identify novel monoclonal antibodies (MoAbs) for detecting PsiL on proB and preB cells.
Main Methods:
- Development and characterization of new antihuman VpreB monoclonal antibodies (gamma kappa isotype).
- Flow cytometry analysis of PsiL cell surface expression on normal bone marrow and proB leukemic cells.
- Biochemical analysis of PsiL-associated proteins in proB cells.
Main Results:
- Five gamma kappa MoAbs demonstrated high-affinity binding to VpreB protein, recognizing distinct epitopes.
- MoAbs detected PsiL on both proB and preB cells, including PsiL+mu- proB cells and TEL/AML1 type proB leukemic cells.
- Biochemical studies identified PsiL noncovalently associated with 105 and 130 kD proteins in proB cells, triggering Ca2+ flux upon complex activation.
Conclusions:
- PsiL is expressed on both proB and preB cells, challenging previous discrepancies.
- A novel PsiL+mu- proB cell complex exists, associated with specific proteins and potentially functioning as an early-stage receptor.
- These findings advance understanding of B-cell differentiation and identify potential targets for leukemia research.
Abstract:
The surrogate light chain (PsiL) associates with mu and Igalpha-Igbeta chains to form the preB-cell receptor that plays a critical role in early B-cell differentiation. Discrepancies exist in human concerning the existence of PsiL+mu- proB cells and the biochemical structure of such a proB-cell complex remains elusive. Among new antihuman VpreB monoclonal antibodies (MoAbs), 5 of the gamma kappa isotype bound to recombinant and native VpreB protein with high affinity. They recognized 4 discrete epitopes, upon which 2 were in the extra-loop fragment. Such MoAbs detected the PsiL at the cell surface of either preB or on both proB and preB cells. The previously reported SLC1/SLC2 MoAbs recognize a conformational epitope specific for the mu/PsiL association in accordance with their preB-cell reactivity. Using the proB/preB 4G7 MoAb, PsiL cell surface expression was detected on normal bone marrow, not only on CD34(-)CD19(+) preB but also on CD34(+)CD19(+) proB cells. Futhermore, this MoAb identified PsiL+mu- fresh proB leukemic cells of the TEL/AML1 type. Biochemical studies showed that, at the proB stage, the PsiL is associated noncovalently with two proteins of 105 and 130 kD. Triggering of this complex induces intracellular Ca2+ flux, suggesting that the PsiL may be involved in a new receptor at this early step of the B-cell differentiation.
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