The non-Ig parts of the VpreB and λ5 proteins of the surrogate light chain play opposite roles in the surface representation of the precursor B cell receptor

The Journal of Immunology : Official Journal of the American Association of Immunologists
Marko KnollKazuo Ohnishi

Abstract

The VpreB and λ5 proteins, together with Igμ-H chains, form precursor BCRs (preBCRs). We established λ5(-/-)/VpreB1(-/-)/VpreB2(-/-) Abelson virus-transformed cell lines and reconstituted these cells with λ5 and VpreB in wild-type form or with a deleted non-Ig part. Whenever preBCRs had the non-Ig part of λ5 deleted, surface deposition was increased, whereas deletion of VpreB non-Ig part decreased it. The levels of phosphorylation of Syk, SLP65, or PLC-γ2, and of Ca(2+) mobilization from intracellular stores, stimulated by μH chain crosslinking Ab were dependent on the levels of surface-bound preBCRs. It appears that VpreB probes the fitness of newly generated VH domains of IgH chains for later pairing with IgL chains, and its non-Ig part fixes the preBCRs on the surface. By contrast, the non-Ig part of λ5 crosslinks preBCRs for downregulation and stimulation.

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Citations

May 6, 2015·The Journal of Clinical Investigation·Fritz Melchers
Aug 23, 2012·Scandinavian Journal of Immunology·N Almqvist, I-L Mårtensson
Nov 6, 2012·The Journal of Biological Chemistry·Latifa ElantakClaudine Schiff
Dec 1, 2018·Frontiers in Immunology·Thomas H Winkler, Inga-Lill Mårtensson
Oct 27, 2020·Disease Markers·Muhammad Muaaz AslamM Ilyas Kamboh
May 27, 2020·Developmental and Comparative Immunology·Marek SinkoraJana Sinkorova
May 1, 2021·International Journal of Molecular Sciences·Ronny Petterson Dos Santos AraújoMarcelo Macedo Brigido

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