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Department of Medical Microbiology, Malmö University Hospital, Lund University, Malmö, Sweden
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
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.
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