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Isolation and characterization of a novel IgD-binding protein from Moraxella catarrhalis

Forsgren, Arne LU ; Brant, Marta LU ; Möllenkvist, Andrea LU ; Muyombwe, Anthony LU ; Janson, Håkan LU ; Woin, Nicolas and Riesbeck, Kristian LU orcid (2001) In Journal of Immunology 167(4). p.2112-2120
Abstract
A novel surface protein of the bacterial species Moraxella catarrhalis that displays a high affinity for IgD (MID) was solubilized in Empigen and isolated by ion exchange chromatography and gel filtration. The apparent molecular mass of monomeric MID was estimated to approximately 200 kDa by SDS-PAGE. The mid gene was cloned and expressed in Escherichia coli. The complete mid nucleotide gene sequence was determined, and the deduced amino acid sequence consists of 2123 residues. The sequence of MID has no similarity to other Ig-binding proteins and differs from all previously described outer membrane proteins of M. catarrhalis. MID was found to exhibit unique Ig-binding properties. Thus, in ELISA, dot blots, and Western blots, MID bound two... (More)
A novel surface protein of the bacterial species Moraxella catarrhalis that displays a high affinity for IgD (MID) was solubilized in Empigen and isolated by ion exchange chromatography and gel filtration. The apparent molecular mass of monomeric MID was estimated to approximately 200 kDa by SDS-PAGE. The mid gene was cloned and expressed in Escherichia coli. The complete mid nucleotide gene sequence was determined, and the deduced amino acid sequence consists of 2123 residues. The sequence of MID has no similarity to other Ig-binding proteins and differs from all previously described outer membrane proteins of M. catarrhalis. MID was found to exhibit unique Ig-binding properties. Thus, in ELISA, dot blots, and Western blots, MID bound two purified IgD myeloma proteins, four IgD myeloma sera, and finally one IgD standard serum. No binding of MID was detected to IgG, IgM, IgA, or IgE myeloma proteins. MID also bound to the surface-expressed B cell receptor IgD, but not to other membrane molecules on human PBLs. This novel Ig-binding reagent promises to be of theoretical and practical interest in immunological research. (Less)
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author
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organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Journal of Immunology
volume
167
issue
4
pages
2112 - 2120
publisher
American Association of Immunologists
external identifiers
  • pmid:11489995
  • scopus:0035881266
ISSN
1550-6606
language
English
LU publication?
yes
id
09281c59-aa1c-43cc-bdd9-9bcad90e300e (old id 1120781)
alternative location
http://www.ncbi.nlm.nih.gov/pubmed/11489995
date added to LUP
2016-04-01 16:45:36
date last changed
2022-04-30 23:33:30
@article{09281c59-aa1c-43cc-bdd9-9bcad90e300e,
  abstract     = {{A novel surface protein of the bacterial species Moraxella catarrhalis that displays a high affinity for IgD (MID) was solubilized in Empigen and isolated by ion exchange chromatography and gel filtration. The apparent molecular mass of monomeric MID was estimated to approximately 200 kDa by SDS-PAGE. The mid gene was cloned and expressed in Escherichia coli. The complete mid nucleotide gene sequence was determined, and the deduced amino acid sequence consists of 2123 residues. The sequence of MID has no similarity to other Ig-binding proteins and differs from all previously described outer membrane proteins of M. catarrhalis. MID was found to exhibit unique Ig-binding properties. Thus, in ELISA, dot blots, and Western blots, MID bound two purified IgD myeloma proteins, four IgD myeloma sera, and finally one IgD standard serum. No binding of MID was detected to IgG, IgM, IgA, or IgE myeloma proteins. MID also bound to the surface-expressed B cell receptor IgD, but not to other membrane molecules on human PBLs. This novel Ig-binding reagent promises to be of theoretical and practical interest in immunological research.}},
  author       = {{Forsgren, Arne and Brant, Marta and Möllenkvist, Andrea and Muyombwe, Anthony and Janson, Håkan and Woin, Nicolas and Riesbeck, Kristian}},
  issn         = {{1550-6606}},
  language     = {{eng}},
  number       = {{4}},
  pages        = {{2112--2120}},
  publisher    = {{American Association of Immunologists}},
  series       = {{Journal of Immunology}},
  title        = {{Isolation and characterization of a novel IgD-binding protein from Moraxella catarrhalis}},
  url          = {{http://www.ncbi.nlm.nih.gov/pubmed/11489995}},
  volume       = {{167}},
  year         = {{2001}},
}