A Protein Complex Map of Trypanosoma brucei
Author(s) -
Vahid Gazestani,
Najmeh Nikpour,
Vaibhav Mehta,
Hamed S. Najafabadi,
Houtan Moshiri,
Armando Jardim,
Reza Salavati
Publication year - 2016
Publication title -
plos neglected tropical diseases
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.99
H-Index - 135
eISSN - 1935-2735
pISSN - 1935-2727
DOI - 10.1371/journal.pntd.0004533
Subject(s) - trypanosoma brucei , biology , african trypanosomiasis , computational biology , function (biology) , rna binding protein , proteomics , identification (biology) , genetics , microbiology and biotechnology , rna , trypanosomiasis , gene , virology , botany
The functions of the majority of trypanosomatid-specific proteins are unknown, hindering our understanding of the biology and pathogenesis of Trypanosomatida . While protein-protein interactions are highly informative about protein function, a global map of protein interactions and complexes is still lacking for these important human parasites. Here, benefiting from in-depth biochemical fractionation, we systematically interrogated the co-complex interactions of more than 3354 protein groups in procyclic life stage of Trypanosoma brucei , the protozoan parasite responsible for human African trypanosomiasis. Using a rigorous methodology, our analysis led to identification of 128 high-confidence complexes encompassing 716 protein groups, including 635 protein groups that lacked experimental annotation. These complexes correlate well with known pathways as well as for proteins co-expressed across the T . brucei life cycle, and provide potential functions for a large number of previously uncharacterized proteins. We validated the functions of several novel proteins associated with the RNA-editing machinery, identifying a candidate potentially involved in the mitochondrial post-transcriptional regulation of T . brucei . Our data provide an unprecedented view of the protein complex map of T . brucei , and serve as a reliable resource for further characterization of trypanosomatid proteins. The presented results in this study are available at: www.TrypsNetDB.org .
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