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Pivotal Advance: CD45RB glycosylation is specifically regulated during human peripheral B cell differentiation.

Journal article
Authors Susanne Koethe
Linda Zander
Sofia Köster
Adelaide Annan
Anders Ebenfelt
Jo Spencer
Mats Bemark
Published in Journal of leukocyte biology
Volume 90
Issue 1
Pages 5-19
ISSN 1938-3673
Publication year 2011
Published at Institute of Biomedicine, Department of Microbiology and Immunology
Institute of Clinical Sciences, Department of Otorhinolaryngology
Pages 5-19
Language en
Links dx.doi.org/10.1189/jlb.0710404
Subject categories Immunology in the medical area, Otorhinolaryngology

Abstract

A screen of cell surface markers differentially expressed during peripheral B cell differentiation identified that the CD45RB epitope detected by the mAb MEM-55 was highly expressed on CD27(+) memory B cells and absent on CD27(-) naïve B cells. IgG(+)CD27(-) memory and a previously unacknowledged CD27(-) population in blood also expressed high levels of CD45RB(MEM55). Naïve and memory B cells from tonsils followed the pattern observed in blood, and CD38(high) B cells had a bimodal expression pattern when analyzed using flow cytometry. No CD38(high) GC B cells, however, expressed the CD45RB(MEM55) epitope when assayed using immunohistochemistry. Rather, CD38(high)CD45RB(MEM55high) B cells had a distinct cellular phenotype and were localized outside of GCs. CD45RB epitopes, detected by other antibody clones, were expressed at high levels through B cell differentiation, and no changes in splicing of the CD45RB exon were observed during B cell differentiation. Instead, B cells regulated their expression of the CD45RB(MEM55) epitope through site-specific modifications of an O-linked glycochain. CD4(+) T cells differentially spliced CD45 but did not vary the glycosylation of the CD45RB(MEM55) epitope, and CD8(+) cells modified CD45RB(MEM55) expression in a similar manner as B cells. Monocytes expressed the CD45RB exon but not the CD45RB(MEM55) epitope. As CD45 is a highly expressed tyrosine phosphatase that regulates antigen receptor signaling strength in lymphocytes, we conclude that regulated O-linked glycosylation of CD45RB can be used to follow B cell differentiation and that this regulation may be involved in fine-tuning antigen signaling in the cell.

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