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Proteomic Analysis Reveals Differential Protein Expression Induced by Inhibition of Prolyl Oligopeptidase in Filarial Parasites

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Abstract

Prolyl oligopeptidase (POP) plays a crucial role in the processing and degradation of neuropeptides and regulates inositol trisphosphate (IP3) signaling in mammals. We have reported that POP inhibition leads to IP3-mediated calcium efflux leading to mitochondrial-mediated apoptosis in the filarial parasite Setaria cervi. This study further elucidates the effect of altered calcium homeostasis on the proteome of filarial parasites. Adult parasites were treated with POP’s specific inhibitor, Z-Pro-prolinal (ZPP), for 7 h. Cytosolic and mitochondrial proteome was analyzed using 2D gel electrophoresis coupled with MALDI-MS/MS. Phosphoproteins were also analyzed in the cytosolic fraction of the parasites. The phosphoprotein analysis revealed 7, and 9 spots in the cytosolic fraction of control and ZPP-treated parasites, respectively. The two identified protein spots in the treated set were found to be involved in G protein signaling. In cytosolic fraction, 109 and 112 protein spots were observed in control and treated parasites, respectively. Of these, 56 upregulated and 32 downregulated protein spots were observed in the treated set. On the other hand, 50 and 47 protein spots were detected in the mitochondrial fraction of control and treated parasites, respectively. Of these spots, 18 upregulated and 12 down-regulated protein spots were found in treated parasites. In silico analysis showed that the identified proteins were involved in energy metabolism, calcium signaling, stress response, and cytoskeleton organization. These findings correlate with our previous results suggesting the important regulatory role of POP in signaling and different metabolic pathways of filarial parasites.

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Data Availability

The datasets generated during and/or analyzed during the current study are available from the corresponding author on reasonable request.

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Acknowledgements

We acknowledge the Interdisciplinary School of Life Sciences (ISLS), Banaras Hindu University (BHU) for IEF, MALDI-MS/MS, and fluorescence imager facility. The authors also acknowledge Ms. Ritu Chauhan, CSIR-Institute of Genomics and Integrative Biology, New Delhi, India, for preparing KEGG pathway scatter plot using R software.

Funding

This study was supported by Banaras Hindu University (BHU), Varanasi, India, in the form of a UGC research fellowship to MW [R/Dev/IX-Sch (BHU Res. Sch.)/2013-14/65134], FA [R/Dev/IX-Sch (BHU Res. Sch.)/2016-17/15562] and SY [R/Dev/IX-Sch (BHU Res. Sch.)/2015-16/00889].

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  1. Department of Biochemistry, Institute of Science, Banaras Hindu University, 221005, Varanasi, India

    Mohit Wadhawan, Faiyaz Ahmad, Smita Yadav & Sushma Rathaur

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  1. Mohit Wadhawan
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MW performed the experiments, analyzed the data, and drafted the manuscript. FA and SY participated in study implementation, and manuscript revision. SR conceived and designed the study, and critically revised the manuscript. All authors read and approved the final manuscript.

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Wadhawan, M., Ahmad, F., Yadav, S. et al. Proteomic Analysis Reveals Differential Protein Expression Induced by Inhibition of Prolyl Oligopeptidase in Filarial Parasites. Protein J 41, 613–624 (2022). https://doi.org/10.1007/s10930-022-10080-7

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