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Infectious disease is a huge health burden globally and antibiotic resistance is an ever growing problem, currently attributable to ~700,000 deaths per year with projected figures rising to 10 million by the year 2050.  For this reason, new therapies to replace antibiotics are crucial. Due to their rapid doubling time, bacteria have the ability to quickly evolve mechanisms to overcome drugs targeted to them, for this reason, I believe the future for anti-infectives is to target infection at the human cell level. Bacteria enter our cells by "hijacking" parts of our own cell machinery (proteins).

Our cells are encased in a membrane consisting of water-repelling fatty acids and proteins. Bacteria have to attach to and breach this membrane in order to get inside our cells. They do this by "hijacking" the proteins within the membrane. Whilst there has been extensive research into how bacteria bind our cells, no universal mechanisms (used by all bacteria) are known. Different bacterial species have been shown to hijack different proteins, which causes problems with therapeutic design. I have discovered that a family of human cell membrane proteins, the tetraspanins, are extremely important in the binding of multiple bacterial species to our cells. Targeting tetraspanins using drugs reduces bacterial binding to multiple types of human cells by greater than 50%. The tetraspanins form part of our cell membranes and act as "organisers", bringing together lots of other proteins to form large protein "islands" in the cell membrane. Bacteria do not directly attach to the tetraspanins but I hypothesise that the tetraspanins organize the proteins required for bacterial binding and it is therefore the loss of this organization which results in reduced bacterial adhesion to our cells when the tetraspanins are blocked.

My lab is interested in investigating the role of these proteins and their interactors in bacterial infection.