26 Oct 2016

Understanding the path of syphilis

Research team uses the Canadian Light Source to help discover new information about how syphilis infections work

In 2001, new cases of syphilis around the world hit at an all-time low. Since then, the number of new cases has kept growing.

“It’s a highly invasive pathogen,” says Dr. Martin Boulanger, a structural biologist from the University of Victoria in British Columbia, “and unfortunately, it’s exploding worldwide.”

syphilis protein image
A recreation of the syphilis protein Tp0751
Photo courtesy Dr. Martin Boulanger

According to the Centres for Disease Control and Prevention (CDC), the rate of new syphilis cases skyrocketed by 19 per cent between 2014 and 2015. According to the World Health Organization, there are 36 million cases around the world and 11 million new infections each year. Alarming numbers like these are driving the race to discover and test viable preventative interventions. The problem is that this isn’t always as easy to do as it sounds.

“The syphilis bacterium Treponema pallidum is extremely difficult to work with,” says Boulanger. “You can’t just grow it in a lab and run standard experiments. As a result, we focus on characterizing its proteins.”

Using research facilities at the CLS, Boulanger and his team, including leading T. pallidum specialist Dr. Caroline Cameron (UVic), discovered that the syphilis protein Tp0751 adopts a similar structure to a family of proteins known for their role in immune response and pheromone transport. This discovery helps to outline – at a molecular level – how the bacterium, and resulting infection, spreads through the body.

“By understanding these molecular interactions we gain valuable insight into the biology of the organism and move one step closer to disease prevention,” says Boulanger.

Boulanger says this research wouldn’t have been successful if weren’t for the support of his research collaborators and the dedicated work of the team at the CLS.

“Access to the sophisticated infrastructure at CLS allows us to obtain high resolution data that is essential for our detailed structural studies,” says Boulanger. “The CLS staff are outstanding and having a facility like CLS in Canada is an enormous benefit to the national research community.” 

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Parker, Michelle L., Simon Houston, Helena P?trošová, Karen V. Lithgow, Rebecca Hof, Charmaine Wetherell, Wei-Chien Kao et al. "The Structure of Treponema pallidum Tp0751 (Pallilysin) Reveals a Non-canonical Lipocalin Fold That Mediates Adhesion to Extracellular Matrix Components and Interactions with Host Cells." PLoS Pathog 12, no. 9 (2016): e1005919. DOI: 10.1371/journal.ppat.1005919

Story by Jane Caulfield

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