Abstract
Bdellovibrio bacteriovorus invade Gram-negative bacteria in a predatory process requiring Type IV pili (T4P) at a single invasive pole, and also glide on surfaces to locate prey. Ras-like G-protein MglA, working with MglB and RomR in the deltaproteobacterium Myxococcus xanthus, regulates adventurous gliding and T4P-mediated social motility at both M. xanthus cell poles. Our bioinformatic analyses suggested that the GTPase activating protein (GAP)-encoding gene mglB was lost in Bdellovibrio, but critical residues for MglABd GTP-binding are conserved. Deletion of mglABd abolished prey-invasion, but not gliding, and reduced T4P formation. MglABd interacted with a previously uncharacterised tetratricopeptide repeat (TPR) domain protein Bd2492, which we show localises at the single invasive pole and is required for predation. Bd2492 and RomR also interacted with cyclic-di-GMP-binding receptor CdgA, required for rapid prey-invasion. Bd2492, RomRBd and CdgA localize to the invasive pole and may facilitate MglA-docking. Bd2492 was encoded from an operon encoding a TamAB-like secretion system. The TamA protein and RomR were found, by gene deletion tests, to be essential for viability in both predatory and non-predatory modes. Control proteins, which regulate bipolar T4P-mediated social motility in swarming groups of deltaproteobacteria, have adapted in evolution to regulate the anti-social process of unipolar prey-invasion in the “lone-hunter” Bdellovibrio. Thus GTP-binding proteins and cyclic-di-GMP inputs combine at a regulatory hub, turning on prey-invasion and allowing invasion and killing of bacterial pathogens and consequent predatory growth of Bdellovibrio.
Highlights
Bdellovibrio bacteriovorus is a small, predatory deltaproteobacterium which invades other Gram-negative bacteria wherein it replicates
A previously unidentified tetratricopeptide repeat (TPR) protein interacts with MglA and is essential for preyinvasion
We report a previously undescribed interacting protein partner of MglA, and show that MglABd and RomRBd interact with this tetratricopeptide repeat protein (TPR) which is required for predation
Summary
Bdellovibrio bacteriovorus is a small, predatory deltaproteobacterium which invades other Gram-negative bacteria wherein it replicates. Bdellovibrio can encounter their prey by fast motility, driven by rotation of a single flagellum in liquid environments [1,2], or by slow gliding motility on solid surfaces [3], but do not show social- or S-motility a process that is shown by other deltaproteobacteria (discussed below). On surfaces a flagellum is not present and the Bdellovibrio glide bidirectionally. This work led us to find that proteins known for surface motility control in a second deltaproteobacterium, Myxococcus xanthus, have evolved to control predatory invasion of bacteria by Bdellovibrio
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