Differential expression of peptidases in Strigomonas culicis wild-type and aposymbiotic strains: from proteomic data to proteolytic activity.

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Strigomonas culicis is a monoxenic trypanosomatid parasite of insects that naturally contains an endosymbiotic bacterium. The aposymbiotic strain can be obtained, making this strain a model for evolutive research about organelle origins. In addition, S. culicis contains homologues of virulence factors of pathogenic trypanosomatids, which functions are waiting for further analysis. In this sense, the publication of S. culicis proteome makes feasible additional investigations regarding the differential expression of peptidases from the wild-type (WT) and the aposymbiotic (APO) strains. Here, we analysed two proteomic data from S. culicis WT and APO strains screening for peptidases differentially expressed and assessed the differential expression of cysteine and metallopeptidases. A comparative proteomic screening between WT and APO identified 43 modulated peptidases. Cysteine and metallopeptidases, such as calpains and GP63, were the major classes, highlighting their significance. GP63 exhibited an increased proteolysis in a specific metallopeptidase substrate, an up-modulation gene expression in RT-PCR, and a higher protein identification by flow cytometry in the aposymbiotic strain. Notwithstanding, the wild-type strain showed enhanced cysteine peptidase activity. Our study highlighted the endosymbiont influence in S. culicis peptidase expression, with GP63 expression and activity raised in the aposymbiotic strain, whereas cysteine peptidase levels were reduced.