Reductive evolution during the adaptation to obligate parasitism and expansions of gene families encoding virulence factors are characteristics evident to greater or lesser degrees in all parasitic protists studied to date. Large evolutionary distances separate many parasitic protists from the yeast and animal models upon which classic views of eukaryotic biochemistry are often based. Thus a combination of evolutionary divergence, niche adaptation and reductive evolution means the biochemistry of parasitic protists is often very different from their hosts and to other eukaryotes generally, making parasites intriguing subjects for those interested in the phenomenon of moonlighting proteins. In common with other organisms, the contribution of protein moonlighting to parasite biology is only just emerging, and it is not without controversy. Here, an overview of recently identified moonlighting proteins in parasitic protists is provided, together with discussion of some of the controversies.
- glyceraldehyde-3-phosphate dehydrogenase (GAPDH)
- Plasmodium falciparum
- Trichomonas vaginalis
- Trypanosoma brucei
The Biological and Biomedical Consequences of Protein Moonlighting: A Biochemical Society Focused Meeting held at Charles Darwin House, London, U.K., 29–30 July 2014. Organized and Edited by Brian Henderson and Andrew Martin (University College London, U.K.).
Abbreviations: EBP, enolase-binding protein; GAPDH, glyceraldehyde-3-phosphate dehydrogenase; α-KDE2, α-ketoglutarate dehydrogenase complex subunit 2; PFO, pyruvate:ferredoxin oxidoreductase; ROS, reactive oxygen species; SCoAS, succinyl-CoA synthetase; TAC, tripartite attachment complex
- © The Authors Journal compilation © 2014 Biochemical Society