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Activity-Based Protein Profiling for the Study of Parasite Biology

Part of the Current Topics in Microbiology and Immunology book series (CT MICROBIOLOGY,volume 420)

Abstract

Parasites exist within most ecological niches, often transitioning through biologically and chemically complex host environments over the course of their parasitic life cycles. While the development of technologies for genetic engineering has revolutionised the field of functional genomics, parasites have historically been less amenable to such modification. In light of this, parasitologists have often been at the forefront of adopting new small-molecule technologies, repurposing drugs into biological tools and probes. Over the last decade, activity-based protein profiling (ABPP) has evolved into a powerful and versatile chemical proteomic platform for characterising the function of enzymes. Central to ABPP is the use of activity-based probes (ABPs), which covalently modify the active sites of enzyme classes ranging from serine hydrolases to glycosidases. The application of ABPP to cellular systems has contributed vastly to our knowledge on the fundamental biology of a diverse range of organisms and has facilitated the identification of potential drug targets in many pathogens. In this chapter, we provide a comprehensive review on the different forms of ABPP that have been successfully applied to parasite systems, and highlight key biological insights that have been enabled through their application.

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  • DOI: 10.1007/82_2018_123
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Fig. 1: Major types of infection exhibited by human-infective parasites.
Fig. 2: Representative activity-based probes (ABPs) used to interrogate the function of major enzyme classes in parasites.

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Correspondence to Matthew A. Child .

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Benns, H.J., Tate, E.W., Child, M.A. (2018). Activity-Based Protein Profiling for the Study of Parasite Biology. In: Cravatt, B., Hsu, KL., Weerapana, E. (eds) Activity-Based Protein Profiling. Current Topics in Microbiology and Immunology, vol 420. Springer, Cham. https://doi.org/10.1007/82_2018_123

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