Probing function and structure of trehalose-6-phosphate phosphatases from pathogenic organisms suggests distinct molecular groupings

  • Megan Cross, Romain Lepage, Siji Rajan, Sonja Biberacher, Neil D. Young, Bo-Na Kim, Mark J. Coster, Robin B. Gasser, Jeong-Sun Kim, Andreas Hofmann
  • The FASEB Journal, November 2016, Federation of American Societies For Experimental Biology (FASEB)
  • DOI: 10.1096/fj.201601149r

What is it about?

Many pathogens require the disaccharide, trehalose, yet it isn't required or synthesized in mammals. Hence, the biochemical pathways to trehalose are of great interest in the development of new and novel therapeutics. This paper looks at the topology of trehalose-6-phosphate phosphatases (TPPs) and classifies them into 3 groups.

Why is it important?

New therapeutics for parasitic diseases are greatly needed and are generally not highly prioritized by the pharmaceutical industry. Inhibition of TPP could be a novel approach to new anti-parasitic compounds.


Associate Professor Mark J Coster
Griffith University

This work is led by my colleague, Andreas Hofmann. It is a highly fruitful, multi-disciplinary collaboration across structural chemistry, parasitology and synthetic medicinal chemistry. It is an exciting area to be working in, due to the untapped nature of the TPPs for anti-parasitic drugs.

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The following have contributed to this page: Dr Andreas Hofmann and Associate Professor Mark J Coster