Stimulator of interferon genes, also known as STING, is a key facilitator of innate immunity. It is a membrane signalling protein, and functions as a small homodimer of 80 kDa whose C-terminal ligand binding domain is exposed in the cytosol. When the monomers come together to form the dimer, the C-terminal region of each monomer forms a butterfly-shaped ligand binding site [1].
STING has the ability to sense pathogen or damage-associated molecular patterns (PAMPs and DAMPs), which are conserved molecular motifs secreted upon pathogen infection or by stressed, damaged, dying, or cancerous cells. A broad range of dsDNA, cyclic dinucleotides, and cGAMP are responsible for STING activation triggering a downstream cascade of signalling events that lead to the production of interferons [2, 3]. Given its role in the first line of cell defense to maintain immune homeostasis, STING is very important in the context of disease. Its activation has been linked with pathogen neutralisation and cancer treatment with immunotherapy. On the other hand, prolonged or chronic stimulation of the STING pathway has been associated with hyperinflammation, autoimmune diseases and the detrimental effects observed in traumatic brain injury [2, 4]. Dampening the STING pathway might be beneficial in many cases. Unfortunately, few STING inhibitors have reached the pre-clinical stage, and none have made it to clinical trials [5, 6].
We aim to explore druggable pockets located in human STING with small molecule inhibitors and use direct binding assays and cryo-electron microscopy to confirm binding and guide structure-based drug design. Inhibitors of STING have been identified through in silico screening and confirmed with in vitro assays. Progress has been made towards the expression of full-length human STING with the BacMam system and I will report advances in the expression and purification of STING and its interactions with selected small molecule inhibitors.