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Mol Cell Proteomics. 2015 Jul;14(7):1977-88. doi: 10.1074/mcp.M114.045146. Epub 2015 May 11.

Cell Surface Proteomics Provides Insight into Stage-Specific Remodeling of the Host-Parasite Interface in Trypanosoma brucei.

Author information

1
From the ‡Department of Microbiology, Immunology, and Molecular Genetics, University of California Los Angeles, Los Angeles, California, 90095;
2
§Department of Biological Chemistry, University of California Los Angeles, Los Angeles, California 90095;
3
§Department of Biological Chemistry, University of California Los Angeles, Los Angeles, California 90095; ¶Molecular Biology Institute, University of California Los Angeles, Los Angeles, California 90095 kenthill@mednet.ucla.edu jwohl@mednet.ucla.edu.
4
From the ‡Department of Microbiology, Immunology, and Molecular Genetics, University of California Los Angeles, Los Angeles, California, 90095; ¶Molecular Biology Institute, University of California Los Angeles, Los Angeles, California 90095 kenthill@mednet.ucla.edu jwohl@mednet.ucla.edu.

Abstract

African trypanosomes are devastating human and animal pathogens transmitted by tsetse flies between mammalian hosts. The trypanosome surface forms a critical host interface that is essential for sensing and adapting to diverse host environments. However, trypanosome surface protein composition and diversity remain largely unknown. Here, we use surface labeling, affinity purification, and proteomic analyses to describe cell surface proteomes from insect-stage and mammalian bloodstream-stage Trypanosoma brucei. The cell surface proteomes contain most previously characterized surface proteins. We additionally identify a substantial number of novel proteins, whose functions are unknown, indicating the parasite surface proteome is larger and more diverse than generally appreciated. We also show stage-specific expression for individual paralogs within several protein families, suggesting that fine-tuned remodeling of the parasite surface allows adaptation to diverse host environments, while still fulfilling universally essential cellular needs. Our surface proteome analyses complement existing transcriptomic, proteomic, and in silico analyses by highlighting proteins that are surface-exposed and thereby provide a major step forward in defining the host-parasite interface.

PMID:
25963835
PMCID:
PMC4587323
DOI:
10.1074/mcp.M114.045146
[Indexed for MEDLINE]
Free PMC Article

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