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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)
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author
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
Society for Leukocyte Biology
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
2007-07-26 12:29:45
date last changed
2019-01-06 05:49:54
@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},
  keyword      = {Moraxella catarrhalis,GFP,B lymphocyte,immunoglobulin D},
  language     = {eng},
  number       = {2},
  pages        = {319--329},
  publisher    = {Society for Leukocyte Biology},
  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          = {http://dx.doi.org/10.1189/jlb.0205065},
  volume       = {79},
  year         = {2006},
}