FEMS Immunology & Medical Microbiology · 2006 · 23 citations · 21 references
Veterinary MedicineInfectious DiseasesMicrobiologyHost-pathogen InteractionsImmunology Of Infectious DiseasesMedical MicrobiologyBacterial ImmunologyBacterial InfectionsPathogen AdhesionPathogenesis Of Infectious DiseaseVaccine Antigen DesignVaccine Antigen DiscoveryBacterial Vaccine AntigensMembrane Protein Antigen DiscoveryN-terminal SequencingOuter Membrane ProteinsOuter Membrane StructurePurification Of Vaccine AntigensSubunit Vaccine Antigen DiscoveryVaccine Candidate Antigens
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.
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Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4
Ulrich K. Laemmli · Nature · 1970 · 251.6K citations
Basic local alignment search tool
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