Mathers K E, Goldblatt D, Aebi C, Yu R, Schryvers A B, Hansen E J
Immunobiology Unit, Institute of Child Health, London, UK.
FEMS Immunol Med Microbiol. 1997 Nov;19(3):231-6. doi: 10.1111/j.1574-695X.1997.tb01092.x.
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.
为了阐明潜在的疫苗抗原，我们对卡他莫拉菌外膜蛋白（OMPs）进行了研究。我们之前已证明一种OMP是人类IgG的靶点，现在我们进一步对这种OMP进行了表征，它的分子量似乎为84 kDa，且与81 kDa的OMP CopB不同。研究表明，人转铁蛋白仅与84 kDa的OMP结合。对该OMP和纯化的卡他莫拉菌转铁蛋白结合蛋白B（TbpB）进行N端测序后发现，它们彼此之间以及与流感嗜血杆菌和脑膜炎奈瑟菌的TbpB均具有同源性。用来自两株卡他莫拉菌的纯化TbpB吸附人抗血清后，可消除或降低IgG与来自三株卡他莫拉菌分离株的84 kDa OMP的结合。IgG与CopB的结合未受影响。显然，84 kDa的OMP与CopB不同，且可能是TbpB的同源物。
