Naka Hiroaki, López Claudia S, Crosa Jorge H
Department of Molecular Microbiology and Immunology, Oregon Health and Science University, Portland, OR 97239, USA.
Environ Microbiol Rep. 2010 Feb 1;2(1):104-111. doi: 10.1111/j.1758-2229.2009.00110.x.
Vibrio anguillarum serotype O1 is part of the natural flora in the aquatic habitat, but under certain circumstances it can cause terminal haemorrhagic septicemia in marine and fresh water fish due to the action of the anguibactin iron uptake system encoded by the virulence plasmid pJM1. This plasmid harbours the genes for the biosynthesis of the siderophore anguibactin and the ferric anguibactin transport proteins FatD, C, B and A encoded in the iron transport operon. The FatA protein is the outer membrane receptor for the ferric siderophore complex and the FatB lipoprotein provides the periplasmic domain for its internalization, whereas the FatC and D proteins are located in the cytoplasmic membrane and might play a role as part of the ABC transporter for internalization of the ferric siderophore. In this work we demonstrate the essential role of these two inner membrane proteins in ferric anguibactin transport and that the lipo-protein nature of FatB is not necessary for ferric anguibactin transport.
鳗弧菌血清型O1是水生栖息地自然菌群的一部分，但在某些情况下，由于毒力质粒pJM1编码的anguibactin铁摄取系统的作用，它可导致海水和淡水鱼类发生终末出血性败血症。该质粒含有铁载体anguibactin生物合成基因以及铁转运操纵子中编码的铁螯合鳗弧菌素转运蛋白FatD、C、B和A。FatA蛋白是铁载体复合物的外膜受体，FatB脂蛋白为其内化提供周质结构域，而FatC和D蛋白位于细胞质膜中，可能作为铁载体内化ABC转运蛋白的一部分发挥作用。在这项研究中，我们证明了这两种内膜蛋白在铁螯合鳗弧菌素转运中的重要作用，并且FatB的脂蛋白性质对于铁螯合鳗弧菌素转运并非必需。
