Characterisation of an outer membrane protein of Moraxella catarrhalis.
Characterisation of an outer membrane protein of Moraxella catarrhalis.
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卡他莫拉菌外膜蛋白的表征。
DOI：
10.1111/j.1574-695x.1997.tb01092.x
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发表时间：
1997
影响因子：
--
通讯作者：
Hansen,EJ
中科院分区：
文献类型：
--
作者：
Mathers,KE;Goldblatt,D;Aebi,C;Yu,R;Schryvers,AB;Hansen,EJ
为了阐明潜在的疫苗抗原，研究了卡他莫拉氏菌外膜蛋白(OMPS)。我们之前已经证明OMP是人类免疫球蛋白的靶标，现在进一步描述了这种OMP的分子质量似乎为84 kDa，并与81 kDa的OMP CopB不同。人转铁蛋白仅与84 kDa的OMP结合。对该OMP和纯化的M进行N-末端测序。卡他司转铁蛋白结合蛋白B(TbpB)与流感嗜血杆菌和脑膜炎奈瑟菌的TbpB具有同源性。纯化的TbpB对人抗血清的吸附卡他沙门氏菌取消或减少了免疫球蛋白与84 kDa OMP的结合。卡他沙门氏剂。与CopB的结合不受影响。很明显，84 kDa的OMP不同于CopB，很可能是TbpB的同源物。
To elucidate potential vaccine antigens,Moraxella catarrhalisouter 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 purifiedM. catarrhalistransferrin binding protein B (TbpB) revealed homology both with each other and with the TbpB ofHaemophilus influenzaeandNeisseria meningitidis. Adsorption of human anti-serum with purified TbpB from twoM. catarrhalisstrains abolished or reduced binding of IgG to the 84-kDa OMP from threeM. catarrhalisisolates. 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.