ACS Infectious Diseases Young Investigator Award Winners Announced - ACS Axial | ACS Publications

ACS Infectious Diseases Young Investigator Award Winners Announced

The ACS Infectious Diseases Young Investigator Award recognizes outstanding young investigators in the infectious diseases field who are within 10 years of their last training experience or at the Assistant Professor level. The 2019 ACS Infectious Diseases Young Investigator  awardees are:

  • Steve D. Townsend, Assistant Professor at Vanderbilt University
  • Jarrod French, Associate Professor at Stonybrook University
  • Megan Wright, University Academic Fellow at the University of Leeds.

The award is jointly presented by ACS Infectious Diseases and the ACS Division of Biological Chemistry.

As winners of the 2019 ACS Infectious Diseases Young Investigator Awards, Townsend, Wright, and French will each receive a plaque, an award of $1,000, and up to $500 in travel reimbursement to attend the Fall 2019 ACS National Meeting & Exposition in San Diego and present at an ACS Division of Biological Chemistry symposium in their honor.

I got the chance to chat with the award winners; read on to find out more about them:

Steve Townsend

How did you get into your field of study?

My primary interest and training are in synthetic organic chemistry. However, as a postdoc, I took an interest in maternal and child health. My goal over the past several years has been to leverage organic chemistry to make discoveries that would translate to reducing the burden of adverse pregnancy outcomes and improve the lives of women and children.

What is the most exciting discovery you have made in your career so far?

Our first big discovery was that human milk oligosaccharides (HMOs) possess potent antimicrobial and antibiofilm activity. The most exciting discovery, however, was that different mothers were producing HMOs with varying levels of potency.

What are you looking forward to most about your research?

The lab currently has two research focuses: Human milk glycoscience and small-molecule total synthesis. Regarding the milk program, I am most excited about deciphering novel interacting partners (perhaps proteins) that milk glycans might engage to provide protection against bacterial pathogens. In our small molecule program, we have recently completed the total synthesis of two natural products. Two others are close!  Therefore, it is an exciting time in the lab as we are displaying our synthetic chops and beginning to study the biology of several interesting molecules. Equal to my excitement about our research results is watching the continued growth of the graduate students in our lab who have entrusted me with helping them develop into independent researchers. Ultimately, I believe that their development, success, and well-being will be my greatest legacy.

Jarrod French

How did you get into your field of study?

Shortly after I started my independent career at Stony Brook in 2014, a colleague approached me from the department of molecular genetics and microbiology. His group works on host-pathogen interactions and the regulation of the immune response. They had recently discovered this exciting phenotype when studying a new class of phosphatase called the Suppressor of TCR Signaling (Sts). A Sts-knockout mouse model strain that they had generated displayed a profound level of resistance to infection by a number of pathogenic organisms. This result suggested that if you could down-regulate the activity of the Sts enzymes in a clinical setting, then you could potentially stimulate the immune response, enhancing the clearance of pathogens and improving outcomes for systemic infections. My colleague and I began to work together, first to characterize the structure and function of this class of protein, and then to search for inhibitors that could act as a basis for drug development. We have been collaborating on this project now for several years and have made tremendous progress, both in our understanding of how this interesting class of protein works and towards the identification of specific inhibitors.

What is the most exciting discovery you have made in your career so far?

I have been fortunate to be involved with a lot of great science over the years. I am proud of all of the work that my lab has done. However, one of the most exciting and rewarding elements of our work is getting to solve a new crystal structure of a protein. Even after dozens of structures, I still get super excited when we solve a new one. To me, it is akin to an explorer discovering a new world. You get to be the first person ever to lay eyes upon this particular arrangement of molecules. It is exciting to be a part of this process, and every new protein structure reveals critical details about function. On top of that, the excitement only just begins there. A new structure of a protein is a jumping-off point – the beginning of many new lines of inquiry.

What are you looking forward to most about your research?

What motivated me to become a scientist in the first place was a real desire to make discoveries and develop new drugs that could one day help to cure disease and save lives. In the beginning, however, I had no idea how difficult, time-consuming and expensive the drug discovery process really is. In spite of that, my group is finally at the point where we have characterized a great drug target, developed assays, completed screens and identified our first few inhibitors. While it may be many years down the road, what I really look forward to most is the opportunity that we may one-day start clinical trials on a compound that we developed. The best possible outcome would be the development of a new immunostimulatory treatment for infectious disease that could be used to save thousands of lives each year.

Megan Wright

How did you get into your field of study?

I did a degree in natural sciences, majoring in chemistry because I loved the creativity and analytical nature of this subject. However, I always had half an eye on biology, and during my degree I did a summer project in the lab of David Spring (University of Cambridge, UK), synthesizing potential inhibitors of bacterial quorum sensing. In the last two weeks of this project, I tested my compounds in a microbiology lab – and from then on, I was hooked on chemical biology! I did a Ph.D. with Ed Tate at Imperial College London developing a chemical approach to identifying lipidated proteins, in collaboration with parasitologists working on different protozoa. This completely opened my eyes to these fascinating organisms and to what you can accomplish working in collaborative teams across disciplines. Then when I was writing postdoctoral fellowship proposals to work with Stephan Sieber (TU Munich) I took inspiration from my initial summer experience to delve back into microbiology. There is something about using chemistry to identify interactions in their native environment — to unravel the inner workings of cells and communication between cells — that really captures my imagination.

What’s the most exciting discovery you’ve made in your career so far?

I find it fascinating that we as chemists can design a tool that closely mimics a molecule yet contains functionality that allows us to understand the fate and interactions of that molecule in a living system. For example, during my postdoctoral fellowship, I wanted to understand how a human peptide triggers virulence in the opportunistic pathogen Pseudomonas aeruginosa. I designed chemical probes based on this peptide to search for the hypothesized bacterial receptor. By combining these probes with proteomics, we discovered a protein sensor that alerts bacteria to the presence of antimicrobial peptides. This is exciting, firstly because no one had shown direct binding of these peptides to proteins in live bacterial cells and so the chemist in me appreciates this technical achievement, but secondly because this sensor seems to be allowing bacteria to mount their defenses in order to thrive in the host. Perhaps this mechanism could be manipulated to help clear bacterial infection? Or maybe these tools will allow us to better understand how Pseudomonas can adapt to different environments? My lab is now developing this chemical approach and applying it to identify other signal-sensor interactions that mediate host-microbe communication.

What are you looking forward to most about your research?

I am most excited about using chemical probes as discovery tools to reveal molecular interactions in live cells and in complex, heterogeneous, cellular systems. I see my lab focusing in two main areas. First, using chemical tools to discover new mechanisms of communication between microbes and their hosts; there must be a huge number of molecules, receptors, and pathways operating in complex multispecies environments that we know nothing about and I think chemical biology can really contribute to this area. Secondly, I want to develop methods that can interrogate dynamic protein function in cells. We are just starting a new project developing probes that can label or trap proteins in specific states in living cells and with spatial and temporal control. This will allow us to start to unravel how cells integrate signals and respond to changing conditions. This is a fundamental biological question, but also one that is central to infectious disease.

The journal and the Division encourage you to attend the ACS Infectious Diseases Young Investigator Awards Symposium at the 2019 ACS National Fall Meeting in San Diego

  • Global Health: Biology and Chemistry of Waterborne Diseases
    • Tuesday, August 27, 8:30 am
    • Marriott Marquis San Diego Marina, Marriott Grand Ballroom Section 6
  • ACS Infectious Diseases Young Investigators Award Symposium
    • Tuesday, August 27, 1:00 pm
    • Marriott Marquis San Diego Marina, Marriott Grand Ballroom Section 6

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