Open AccessCharacterisation of an outer membrane protein of Moraxella catarrhalis
Author(s) -
Mathers Kate E.,
Goldblatt David,
Aebi Christoph,
Yu Ronghua,
Schryvers Anthony B.,
Hansen Eric J.
Publication year - 1997
Publication title -
fems immunology & medical microbiology
Language(s) - English
Resource type - Journals
eISSN - 1574-695X
pISSN - 0928-8244
DOI - 10.1111/j.1574-695x.1997.tb01092.x
Subject(s) - moraxella catarrhalis , moraxella (branhamella) catarrhalis , bacterial outer membrane , biology , microbiology and biotechnology , moraxella , neisseriaceae , haemophilus influenzae , neisseria meningitidis , transferrin , neisseria , bacterial adhesin , molecular mass , antigen , biochemistry , bacteria , gene , escherichia coli , immunology , genetics , enzyme , antibiotics
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 OMP alone. N‐terminal sequencing of this OMP and purified M. catarrhalis transferrin binding protein B (TbpB) revealed homology 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 three 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.