Structural investigations of Adhesin-like proteins in the predatory bacterium Bdellovibrio Bacteriovorus

Bdellovibrio bacteriovorus is an extremely efficient predator of Gram-negative bacteria and carries out a predatory lifestyle which sees the predator invade the prey's periplasm and subsequently kill them from within. Bdellovibrio's ability to kill Gram-negative bacteria, including many antibiotic-resistant pathogens, has raised its possibility of being used as a 'living antibiotic' to treat bacterial infections in animals and crops. The therapeutic potential of Bdellovibrio has been illustrated by a number of studies where it has been observed to kill Klebsiella pneumoniae and Shigella in animal models of infection.

This project will study a currently uncharacterised element of Bdellovibrio's predatory lifecycle, the attachment of Bdellovibrio cells to its prey. The key focus of the project will be on predatory proteins which contain domains predicted to play a role in adhesion. The complexity and specificity of Bdellovibrio's predatory lifecycle is reflected within its genome and, as a result of this, its homology to other organisms is fairly low. Therefore, this project will utilise X-ray crystallography and complementary techniques to gain high resolution structures of the proposed adhesin-like proteins. Information gleaned from these structures will then be used to uncover the mechanisms of prey attachment at the molecular level. An in-depth understanding of potential interactions between multi-domain bdellovibrio proteins and exposed prey features will not only help uncover a key process of Bdellovibrio's lifecycle but may also open the possibility of manipulating the mechanism to increase the range of prey with which Bdellovibrio can interact.