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Title: Proteome mapping of Plasmodium: identification of the P. yoelii remodellome
Authors: Siau, Anthony
Huang, Ximei
Weng, Mei
Sze, Siu Kwan
Preiser, Peter R.
Keywords: Parasite biology
Mass spectrometry
Issue Date: 2016
Source: Siau, A., Huang, X., Weng, M., Sze, S. K., & Preiser, P. R. (2016). Proteome mapping of Plasmodium: identification of the P. yoelii remodellome. Scientific Reports, 6, 31055-.
Series/Report no.: Scientific Reports
Abstract: Plasmodium associated virulence in the host is linked to extensive remodelling of the host erythrocyte by parasite proteins that form the “remodellome”. However, without a common motif or structure available to identify these proteins, little is known about the proteins that are destined to reside in the parasite periphery, the host-cell cytoplasm and/or the erythrocyte membrane. Here, the subcellular fractionation of erythrocytic P. yoelii at trophozoite and schizont stage along with label-free quantitative LC-MS/MS analysis of the whole proteome, revealed a proteome of 1335 proteins. Differential analysis of the relative abundance of these proteins across the subcellular compartments allowed us to map their locations, independently of their predicted features. These results, along with literature data and in vivo validation of 61 proteins enabled the identification of a remodellome of 184 proteins. This approach identified a significant number of conserved remodelling proteins across plasmodium that likely represent key conserved functions in the parasite and provides new insights into parasite evolution and biology.
ISSN: 2045-2322
DOI: 10.1038/srep31055
Schools: School of Biological Sciences 
Rights: © The Author(s) 2016. This work is licensed under a Creative Commons Attribution 4.0 International License. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder to reproduce the material. To view a copy of this license, visit
Fulltext Permission: open
Fulltext Availability: With Fulltext
Appears in Collections:SBS Journal Articles

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