Pivotal advance : CD45RB glycosylation is specifically regulated during human peripheral B cell differentiation
Koethe, Susanne ; Zander, Linda ; Köster, Sofia ; Annan, Adelaide ; Ebenfelt, Anders ; Spencer, Jo and Bemark, Mats LU
(2011)
In Journal of Leukocyte Biology
90(1).
p.5-19
- 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 CD45RBMEM55. Naïve and memory B cells from tonsils followed the pattern observed in blood, and CD38high B cells had a bimodal expression pattern when analyzed using flow cytometry. No CD38high GC B cells, however, expressed the CD45RBMEM55 epitope when assayed using immunohistochemistry. Rather,... (More)
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 CD45RBMEM55. Naïve and memory B cells from tonsils followed the pattern observed in blood, and CD38high B cells had a bimodal expression pattern when analyzed using flow cytometry. No CD38high GC B cells, however, expressed the CD45RBMEM55 epitope when assayed using immunohistochemistry. Rather, CD38highCD45RBMEM55high 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 CD45RBMEM55 epitope through site-specific modifications of an O-linked glycochain. CD4+ T cells differentially spliced CD45 but did not vary the glycosylation of the CD45RBMEM55 epitope, and CD8+ cells modified CD45RBMEM55 expression in a similar manner as B cells. Monocytes expressed the CD45RB exon but not the CD45RBMEM55 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.
(Less)
- author
- Koethe, Susanne
; Zander, Linda
; Köster, Sofia
; Annan, Adelaide
; Ebenfelt, Anders
; Spencer, Jo
and Bemark, Mats
LU
- publishing date
- 2011-07
- type
- Contribution to journal
- publication status
- published
- keywords
- Cell surface marker, O-linked, Sialic acids
- in
- Journal of Leukocyte Biology
- volume
- 90
- issue
- 1
- pages
- 5 - 19
- publisher
- John Wiley & Sons Inc.
- external identifiers
-
- scopus:79959828123
- pmid:21278234
- ISSN
- 0741-5400
- DOI
- 10.1189/jlb.0710404
- language
- English
- LU publication?
- no
- id
- ff0715e2-e663-4766-9afd-e3c70283b95b
- date added to LUP
- 2023-12-06 16:36:57
- date last changed
- 2024-04-05 08:52:36
@article{ff0715e2-e663-4766-9afd-e3c70283b95b,
abstract = {{<p>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<sup>+</sup> memory B cells and absent on CD27<sup>-</sup> naïve B cells. IgG<sup>+</sup>CD27<sup>-</sup> memory and a previously unacknowledged CD27<sup>-</sup> population in blood also expressed high levels of CD45RB<sup>MEM55</sup>. Naïve and memory B cells from tonsils followed the pattern observed in blood, and CD38<sup>high</sup> B cells had a bimodal expression pattern when analyzed using flow cytometry. No CD38<sup>high</sup> GC B cells, however, expressed the CD45RB<sup>MEM55</sup> epitope when assayed using immunohistochemistry. Rather, CD38<sup>high</sup>CD45RB<sup>MEM55</sup>high 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<sup>MEM55</sup> epitope through site-specific modifications of an O-linked glycochain. CD4<sup>+</sup> T cells differentially spliced CD45 but did not vary the glycosylation of the CD45RB<sup>MEM55</sup> epitope, and CD8<sup>+</sup> cells modified CD45RB<sup>MEM55</sup> expression in a similar manner as B cells. Monocytes expressed the CD45RB exon but not the CD45RB<sup>MEM55</sup> 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.</p>}},
author = {{Koethe, Susanne and Zander, Linda and Köster, Sofia and Annan, Adelaide and Ebenfelt, Anders and Spencer, Jo and Bemark, Mats}},
issn = {{0741-5400}},
keywords = {{Cell surface marker; O-linked; Sialic acids}},
language = {{eng}},
number = {{1}},
pages = {{5--19}},
publisher = {{John Wiley & Sons Inc.}},
series = {{Journal of Leukocyte Biology}},
title = {{Pivotal advance : CD45RB glycosylation is specifically regulated during human peripheral B cell differentiation}},
url = {{http://dx.doi.org/10.1189/jlb.0710404}},
doi = {{10.1189/jlb.0710404}},
volume = {{90}},
year = {{2011}},
}