Ala'Aldeen D A, Davies H A, Wall R A, Borriello S P
Microbial Pathogenicity Research Group, MRC Clinical Research Centre, Harrow, Middlesex, U.K.
FEMS Microbiol Lett. 1990 May;57(1-2):37-42. doi: 10.1016/0378-1097(90)90409-j.
Neisseria meningitidis is able to chelate iron from human transferrin (HTF), the main sequestrator of extracellular iron in vivo. Previous workers have reported that a ca. 70 kilodalton (kDa) iron regulated outer membrane protein (FeRP-70) is a highly specific receptor for HTF. We have examined the interaction between the iron regulated outer membrane proteins (OMP's) and HTF, using HTF and rabbit anti HTF, as well as gold labelled HTF (Au-HTF) to blot OMP's of various serogroups and serotypes of N. meningitidis. Also, we used monospecific rabbit anti FeRP-70 in competitive experiments to determine the role of FeRP-70 in HTF-binding. Single proteins (molecular weights range ca. 60 to ca. 90 kDa) were identified in the OMP's from each strain which reacted with HTF. HTF failed to block the reaction between FeRP-70 and the OMP's, conversely anti FeRP-70 failed to block the HTF-binding reaction. We believe that the 70 kDa iron regulated protein of N. meningitidis is not a human transferrin receptor.
脑膜炎奈瑟菌能够从人转铁蛋白（HTF）中螯合铁，HTF是体内细胞外铁的主要螯合剂。先前的研究人员报道，一种约70千道尔顿（kDa）的铁调节外膜蛋白（FeRP - 70）是HTF的高度特异性受体。我们使用HTF、兔抗HTF以及金标记的HTF（Au - HTF）对不同血清群和血清型的脑膜炎奈瑟菌的外膜蛋白（OMP）进行印迹分析，以研究铁调节外膜蛋白（OMP）与HTF之间的相互作用。此外，我们在竞争性实验中使用单特异性兔抗FeRP - 70来确定FeRP - 70在HTF结合中的作用。在每个菌株的OMP中鉴定出与HTF反应的单一蛋白质（分子量范围约为60至约90 kDa）。HTF未能阻断FeRP - 70与OMP之间的反应，相反，抗FeRP - 70未能阻断HTF结合反应。我们认为脑膜炎奈瑟菌的70 kDa铁调节蛋白不是人转铁蛋白受体。
