Shotgun proteomics of detergent-solubilized membrane proteins from Trypanosoma evansi

Trypanosoma evansi, the etiological agent of Surra, is the most widespread pathogenic salivarian trypanosomes and affects most livestock and wild animals in endemic regions. Knowledge of the molecular and cell biology of the parasite is limited. The study of proteins through a proteomic-based approach contributes to biochemical, molecular, and epidemiological studies. In this work, high-throughput proteomic analysis of Triton X-114-extracted surface-enriched proteins of bloodstream forms of T. evansi was carried out by gel-free approach (LC-ESI-MS/MS). Proteins resolved by SDS-PAGE revealed major proteins bands between 35 kDa and 100 kDa. After MS analysis of three biological and technical replicates, 385 proteins were identified. From these proteins, xx (0.77 %) were predicted to have GPI-anchor, 137 (35.5 %) were predicted to have transmembrane domains by (TMHMM), and 154 (40 %) were predicted as membrane-bound proteins. Membrane proteins typical of each organelle were found, some of which were already studied in other trypanosomatids. Two proteins, a and b, were considered T. evansi singletons, one of them, a, with two predicted epitopes, a putative 75 kDa invariant surface glycoprotein.