microLife Poster Prize: Jake Colautti

Congratulations to Jake Colautti, PhD Candidate at the Department of Biochemistry and Biomedical Sciences, McMaster University (Canada)  for winning a Poster Prize at the Gordon Research Conference on Microbial Adhesion and Signal Transduction (GRC-MAST). This conference took place at Salve Regina University (USA) on 16 – 21 July 2023.

This award is sponsored by our journal microLife and as well as receiving a cash prize, we interviewed Jake to find out more about his prize winning research:

What has been your journey through microbiology thus far?

My journey in microbiology began as a graduate student in John Whitney’s laboratory at McMaster University. Our research is interested in understanding the molecular mechanisms of interbacterial interactions and primarily focuses on two secretion systems that bacteria use to secrete toxins into competitor cells: the type VI secretion system in Gram-negative organisms and the type VIIb secretion system in Gram-positive organisms. Using genetic, biochemical, and structural approaches, we aim to determine how proteins are recognized for secretion by these systems and how these toxins kill target cells.

Could you provide a brief and simple overview of the topic your oral presentation covers?

In order to compete for limited resources in dense polymicrobial environments, bacteria frequently encode systems that export antimicrobial molecules. One such system, the type VI secretion system (T6SS), exports toxins directly into competitor cells. While the activity of several of these toxins has been well characterized, the mechanism by which structurally and functionally diverse toxins are recognized by conserved components of the system remains poorly understood. My project characterizes a family of chaperone proteins that physically interact with structurally unrelated toxins and recruit them to closely related T6SS components. In this way, these proteins allow conserved components of the system to recognize and export a diverse repertoire of toxins.

What encouraged you to perform research in this area of microbiology

I was drawn to this work because it exists at the interface between microbiology and biochemistry; while the biological system employing the proteins I work on is a bacterial one, the approaches we use to ascertain the function of these proteins employ tools from protein biochemistry and structural biology. This allows me to explore these two areas of personal interest, learn valuable skills from multiple fields, and integrate these skills to mechanistically investigate challenging questions.

What do you see as the next steps in this area of research?

I think it will be important to determine whether the chaperone proteins I am investigating dissociate from their cognate toxins before or during secretion and, if so, how this dissociation occurs. Furthermore, I am interested in understanding whether the secreted complex of toxin and structural components dissociate upon delivery to the target cells, how this dissociation may be regulated, and what the consequences of that disassembly are for the function of the system.

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