Proteome mapping of Plasmodium: identification of the P. yoelii remodellome

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 i...

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Main Authors: Siau, Anthony, Huang, Ximei, Weng, Mei, Sze, Siu Kwan, Preiser, Peter R.
Other Authors: School of Biological Sciences
Format: Article
Language:English
Published: 2017
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Online Access:https://hdl.handle.net/10356/83086
http://hdl.handle.net/10220/42416
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Institution: Nanyang Technological University
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spelling sg-ntu-dr.10356-830862023-02-28T17:00:18Z Proteome mapping of Plasmodium: identification of the P. yoelii remodellome Siau, Anthony Huang, Ximei Weng, Mei Sze, Siu Kwan Preiser, Peter R. School of Biological Sciences Parasite biology Mass spectrometry 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. NMRC (Natl Medical Research Council, S’pore) Published version 2017-05-15T05:15:29Z 2019-12-06T15:11:35Z 2017-05-15T05:15:29Z 2019-12-06T15:11:35Z 2016 Journal Article 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-. 2045-2322 https://hdl.handle.net/10356/83086 http://hdl.handle.net/10220/42416 10.1038/srep31055 27503796 en Scientific Reports © 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 http://creativecommons.org/licenses/by/4.0/ 12 p. application/pdf
institution Nanyang Technological University
building NTU Library
continent Asia
country Singapore
Singapore
content_provider NTU Library
collection DR-NTU
language English
topic Parasite biology
Mass spectrometry
spellingShingle Parasite biology
Mass spectrometry
Siau, Anthony
Huang, Ximei
Weng, Mei
Sze, Siu Kwan
Preiser, Peter R.
Proteome mapping of Plasmodium: identification of the P. yoelii remodellome
description 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.
author2 School of Biological Sciences
author_facet School of Biological Sciences
Siau, Anthony
Huang, Ximei
Weng, Mei
Sze, Siu Kwan
Preiser, Peter R.
format Article
author Siau, Anthony
Huang, Ximei
Weng, Mei
Sze, Siu Kwan
Preiser, Peter R.
author_sort Siau, Anthony
title Proteome mapping of Plasmodium: identification of the P. yoelii remodellome
title_short Proteome mapping of Plasmodium: identification of the P. yoelii remodellome
title_full Proteome mapping of Plasmodium: identification of the P. yoelii remodellome
title_fullStr Proteome mapping of Plasmodium: identification of the P. yoelii remodellome
title_full_unstemmed Proteome mapping of Plasmodium: identification of the P. yoelii remodellome
title_sort proteome mapping of plasmodium: identification of the p. yoelii remodellome
publishDate 2017
url https://hdl.handle.net/10356/83086
http://hdl.handle.net/10220/42416
_version_ 1759858062591524864