Abstract
To elucidate potential vaccine antigens, Moraxella catarrhalis outer membrane proteins (OMPs) were studied. We have previously shown an OMP to be a target for human IgG and have now further characterised this OMP which appears to have a molecular mass of 84 kDa and to be distinct from the 81-kDa OMP, CopB. Human transferrin was shown to bind the 84-kDa Chip alone. N-terminal sequencing of this OMP and purified M. catarrhalis transferrin binding protein B (TbpB) revealed homolog both with each other and with the TbpB of Haemophilus influenzae and Neisseria meningitidis. Adsorption of human anti-serum with purified TbpB from two M. catarrhalis strains abolished or reduced binding of IgG to the 84-kDa OMP from thee M. catarrhalis isolates. IgG binding to CopB was unaffected. It is clear that the 84-kDa OMP is distinct from CopB and is a likely homologue of TbpB.
Original language | English (US) |
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Pages (from-to) | 231-236 |
Number of pages | 6 |
Journal | FEMS Immunology and Medical Microbiology |
Volume | 19 |
Issue number | 3 |
DOIs | |
State | Published - Nov 1997 |
Keywords
- Immunoglobulin G
- Moraxella catarrhalis
- Outer membrane protein
- Transferrin binding protein
ASJC Scopus subject areas
- Immunology and Allergy
- Microbiology
- Immunology
- Microbiology (medical)
- Infectious Diseases