Matthew's laboratory focuses on the incredibly multifunctional Omp85 protein superfamily which conduct essential processes in the outer membranes of all Gram-negative bacteria such as protein folding, insertion, and translocation reactions, as well as lipid transport reactions.

Throughout my PhD, I determined the transport mechanisms of two proteins that we show break the standard channel / transporter definitions and instead function as anion “chansporters” - proteins that exist somewhere on the spectrum between transporters and channels.

Heteromeric amino acid transporters (HATs) play essential roles in the transport of amino acids, thyroid hormones, and various amino acid–like drugs. Mutations in HATs are associated with several inherited disorders, including cystinuria, lysinuric protein intolerance, and autism spectrum disorders.

Autotransporters (ATs) are virulence factors found in Gram-negative bacteria that consist of three domains: an N-terminal signal peptide, a central passenger domain, and a C-terminal β-barrel domain. Here, we used RpeA from rabbit enteropathogenic Escherichia coli as a model AT.

The ability of Plasmodium falciparum to access and utilise vital nutrients, including riboflavin (vitamin B2), is essential for its growth and proliferation, positioning riboflavin metabolism as a promising target for antimalarial intervention.

My work studies how platelets control malarial infection, and through this has revealed the specific anti-plasmodial actions of platelets and molecules with novel mechanisms of parasite killing.