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J. Biol. Chem., Vol. 277, Issue 38, 34692-34699, September 20, 2002
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From the Department of Medical Microbiology, Lund University,
University Hospital Malmö, S-205 02 Malmö, Sweden
Moraxella catarrhalis IgD-binding
protein (MID), a 200-kDa outer membrane protein comprising 2,139 amino
acids, has recently been isolated and shown to display a unique and
specific affinity for human IgD. To identify the IgD-binding region,
MID was digested with proteases. In addition, a series of truncated
fragments of MID were manufactured and expressed in Escherichia
coli followed by analysis for IgD binding in Western and dot
blots. The smallest fragment with essentially preserved IgD binding was
comprised of 238 amino acid residues (MID962-1200).
Shorter recombinant proteins gradually lost IgD-binding capacity, and
the shortest IgD-binding fragment comprising 157 amino acids (MID985-1142) displayed a 1,000-fold reduced IgD binding
compared with the full-length molecule. The truncated
MID962-1200 was efficiently attracted to a standard IgD
serum and to purified myeloma IgD(
The Immunoglobulin D-binding Part of the Outer Membrane Protein
MID from Moraxella catarrhalis Comprises 238 Amino
Acids and a Tetrameric Structure*
) and IgD(
) sera but not to
IgG, IgM, or IgA myeloma sera. Furthermore, the fragment specifically
bound to peripheral blood B lymphocytes, and the binding was inhibited
by preincubation with anti-IgD-Fab polyclonal antibodies. Results
obtained by introducing five amino acids randomly into
MID962-1200 using transposons suggested that 
-helix
structures were important for IgD binding. Ultracentrifugation
experiments and gel electrophoresis revealed that native
MID962-1200 was a tetramer. Interestingly,
tetrameric MID962-1200 attracted IgD more than 20-fold
more efficiently than the monomeric form. Thus, a tetrameric structure
of MID962-1200 is crucial for optimal IgD-binding capacity.
*
This work was supported by grants from the Alfred
Österlund Foundation, the Anna and Edwin Berger Foundation, the
Crafoord Foundation, the Greta and Johan Kock Foundation, the IngaBritt and Arne Lundberg Foundation, the Magnus Bergvall Foundation, the
Swedish Medical Research Council, the Swedish Society of Medicine, the Åke Wiberg foundation, and the Cancer Foundation at the
University Hospital in Malmö.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed: Dept. of Medical
Microbiology, University Hospital Malmö, Lund University,
S-205 02 Malmö, Sweden. Tel.: 46-40-331340; Fax:
46-40-336234; E-mail: kristian.riesbeck@mikrobiol.mas.lu.se.
Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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