Skip to main content

Lund University Publications

LUND UNIVERSITY LIBRARIES

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 orcid (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:
author
; ; ; and
organization
publishing date
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}},
}