The IgD-binding domain of the Moraxella IgD-binding protein MID (MID962-1200) activates human B cells in the presence of T cell cytokines.
Nordström, Therése LU ; Jendholm, Johan LU ; Samuelsson, Martin LU ; Forsgren, Arne LU and Riesbeck, Kristian LU
(2006)
In Journal of Leukocyte Biology
79(2).
p.319-329
- Abstract
- Moraxella catarrhalis immunoglobulin D (IgD)-binding protein (MID) is an outer membrane protein with specific affinity for soluble and cell-bound human IgD. Here, we demonstrate that mutated M. catarrhalis strains devoid of MID show a 75% decreased activation of human B cells as compared with wild-type bacteria. In contrast to MID-expressing Moraxella, the MID-deficient Moraxella mutants did not bind to human CD19(+) IgD(+) B cells. The smallest MID fragment with preserved IgD-binding capacity comprises 238 amino acids (MID962-1200). To prove the specificity of MID962-1200 for IgD, a Chinese hamster ovary (CHO) cell line expressing membrane-anchored human IgD was manufactured. MID962-1200 bound strongly to the recombinant IgD on CHO cells.... (More)
- Moraxella catarrhalis immunoglobulin D (IgD)-binding protein (MID) is an outer membrane protein with specific affinity for soluble and cell-bound human IgD. Here, we demonstrate that mutated M. catarrhalis strains devoid of MID show a 75% decreased activation of human B cells as compared with wild-type bacteria. In contrast to MID-expressing Moraxella, the MID-deficient Moraxella mutants did not bind to human CD19(+) IgD(+) B cells. The smallest MID fragment with preserved IgD-binding capacity comprises 238 amino acids (MID962-1200). To prove the specificity of MID962-1200 for IgD, a Chinese hamster ovary (CHO) cell line expressing membrane-anchored human IgD was manufactured. MID962-1200 bound strongly to the recombinant IgD on CHO cells. Moreover, MID962-1200 stimulated peripheral blood lymphocyte (PBL) proliferation 5- and 15-fold at 0.1 and 1.0 mu g/ml, respectively. This activation could be blocked completely by antibodies directed against the CD40 ligand (CD154). MID962-1200 also activated purified B cells in the presence of interleukin (IL)-2 or IL-4. An increased IL-6 production was seen after stimulation with MID962-1200, as revealed by a human cytokine protein array. MID962-1200 fused to green fluorescent protein (GFP) bound to human B cells and activated PBL to the same degree as MID962-1200 Taken together, MID is the only IgD-binding protein in Moraxella. Furthermore, the novel T cell-independent antigen MID962-1200 may, together with MID962-1200-GFP, be considered as promising reagents in the study of IgD-dependent B cell activation. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/147820
- author
- Nordström, Therése
LU
; Jendholm, Johan
LU
; Samuelsson, Martin
LU
; Forsgren, Arne
LU
and Riesbeck, Kristian
LU
- organization
- publishing date
- 2006
- type
- Contribution to journal
- publication status
- published
- subject
- keywords
- Moraxella catarrhalis, GFP, B lymphocyte, immunoglobulin D
- in
- Journal of Leukocyte Biology
- volume
- 79
- issue
- 2
- pages
- 319 - 329
- publisher
- John Wiley & Sons Inc.
- external identifiers
-
- pmid:16415174
- wos:000243014900008
- scopus:33646451574
- ISSN
- 1938-3673
- DOI
- 10.1189/jlb.0205065
- language
- English
- LU publication?
- yes
- id
- d905291f-802a-46f3-a0b5-934ca0ca1806 (old id 147820)
- alternative location
- http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=16301327&dopt=Abstract
- date added to LUP
- 2016-04-01 11:44:21
- date last changed
- 2022-04-05 04:22:40
@article{d905291f-802a-46f3-a0b5-934ca0ca1806,
abstract = {{Moraxella catarrhalis immunoglobulin D (IgD)-binding protein (MID) is an outer membrane protein with specific affinity for soluble and cell-bound human IgD. Here, we demonstrate that mutated M. catarrhalis strains devoid of MID show a 75% decreased activation of human B cells as compared with wild-type bacteria. In contrast to MID-expressing Moraxella, the MID-deficient Moraxella mutants did not bind to human CD19(+) IgD(+) B cells. The smallest MID fragment with preserved IgD-binding capacity comprises 238 amino acids (MID962-1200). To prove the specificity of MID962-1200 for IgD, a Chinese hamster ovary (CHO) cell line expressing membrane-anchored human IgD was manufactured. MID962-1200 bound strongly to the recombinant IgD on CHO cells. Moreover, MID962-1200 stimulated peripheral blood lymphocyte (PBL) proliferation 5- and 15-fold at 0.1 and 1.0 mu g/ml, respectively. This activation could be blocked completely by antibodies directed against the CD40 ligand (CD154). MID962-1200 also activated purified B cells in the presence of interleukin (IL)-2 or IL-4. An increased IL-6 production was seen after stimulation with MID962-1200, as revealed by a human cytokine protein array. MID962-1200 fused to green fluorescent protein (GFP) bound to human B cells and activated PBL to the same degree as MID962-1200 Taken together, MID is the only IgD-binding protein in Moraxella. Furthermore, the novel T cell-independent antigen MID962-1200 may, together with MID962-1200-GFP, be considered as promising reagents in the study of IgD-dependent B cell activation.}},
author = {{Nordström, Therése and Jendholm, Johan and Samuelsson, Martin and Forsgren, Arne and Riesbeck, Kristian}},
issn = {{1938-3673}},
keywords = {{Moraxella catarrhalis; GFP; B lymphocyte; immunoglobulin D}},
language = {{eng}},
number = {{2}},
pages = {{319--329}},
publisher = {{John Wiley & Sons Inc.}},
series = {{Journal of Leukocyte Biology}},
title = {{The IgD-binding domain of the Moraxella IgD-binding protein MID (MID962-1200) activates human B cells in the presence of T cell cytokines.}},
url = {{https://lup.lub.lu.se/search/files/2619157/625150.pdf}},
doi = {{10.1189/jlb.0205065}},
volume = {{79}},
year = {{2006}},
}