A tale in two parts: how a search for antivirulence compounds led to the discovery of a shapeshifting copper resistance protein

Prof Jennifer Martin


Tuesday, 13 November, 2018 -
12:00 to 13:00


Room M17, Chemical Sciences Building


School of Chemistry

Type of event: 


2018 Jeffery Lecture (School of Chemistry)

Protein disulfide bonds form covalent links between sulfurs of cysteine sidechains and are critical for the folding and function of secreted proteins. There is now overwhelming evidence that these inter-residue bonds play a key role in Gram negative bacterial virulence. This presentation will describe the bacterial machinery that introduce disulfide bonds into folding proteins; explore how these have been used to search for a new class of antibacterial agent; and outline the serendipitous discovery of a shape-shifting foldase that is not only a target for drug discovery but also provides clues for potential plug-and-play bionanotechnology.


Prof Jennifer Martin is the Director for the Griffith Institute for Drug Discovery (GRIDD). She is an internationally renowned protein crystallographer and structural biologist. She has made seminal discoveries in bacterial redox biochemistry, including revealing how the DsbA enzyme assembles bacterial ‘weapons’, and has validated DsbA as a target for novel antibacterials that are now being developed. Through her role as a founding member of the Science and Gender Equity (SAGE) Steering Committee, Prof Martin helped implement the Athena SWAN pilot to address gender equity in science. Prof Martin is a strong public advocate for science with an inspirational and highly effective science communication record.