ACS Infectious DiseasesMolecular BiologyPeer-reviewed journal article
Functional study of Leishmania braziliensis protein arginine methyltransferases (PRMTs) reveals that PRMT1 and PRMT5 are required for macrophage infection
Lucas B. LorenzoniD, José Carlos Quilles JunioriD, Gustavo D. CampagnaroiD, Lissur Azevedo OrsineiD, Letícia de AlmeidaiD, Flavio Protasio VerasiD, Rubens Daniel Miserani MagalhãesiD, Juliana Alcoforado DiniziD, Tiago Rodrigues FerreiraiD, Ângela K. CruziD
Abstract
In trypanosomatids, regulation of gene expression occurs mainly at the posttranscriptional level, and RNA-binding proteins (RBPs) are key players in determining the fates of transcripts. RBPs are major targets of protein arginine methyltransferases (PRMTs), which posttranslationally regulate the RNA-binding capacity and other macromolecular interactions of RBPs by transferring methyl groups to protein arginine residues. Herein, we present the results of a study that functionally characterized the five predicted PRMTs in Leishmania braziliensis by gene knockout and endogenous protein HA tagging using CRISPR/Cas9 gene editing. We report that arginine methylation profiles vary among Leishmania species and that target protein methylation changes across different L. braziliensis life cycle stages, with higher PRMT expression in the promastigote stages than in the axenic amastigote stage. Knockout of some of the L. braziliensis PRMTs led to significant changes in global arginine methylation patterns without affecting promastigote axenic growth. Deletion of either PRMT1 or PRMT3 disrupted most type I PRMT activity, resulting in a global increase in monomethyl arginine (MMA) levels, which is mainly catalyzed by PRMT7. Putative targets and/or PRMT-interacting proteins were identified by coimmunoprecipitation using HA-tagged PRMTs, revealing a network of target RBPs and suggesting functional interactions between them and a relevant participation in epigenetic control of gene expression. Finally, we demonstrate that L. braziliensis PRMT1 and PRMT5 are required for efficient macrophage infection in vitro, and that in the absence of PRMT1 and PRMT5, axenic amastigote proliferation is impaired. The results indicate that arginine methylation is modulated across life cycle stages in L. braziliensis and show possible functional overlap and cooperation among the different PRMTs in targeting proteins. Overall, our data suggest important regulatory roles of these proteins throughout the L. braziliensis life cycle, showing that arginine methylation is important for parasite-host cell interactions.
- Citations
- 19
- FWCI
- 3.75
- Field percentile
- top 7%
Reproducibility ledger
Nobody has reported trying to reproduce this paper yet. Did you replicate an experiment or run the code? Your report saves the next lab a week.
Sign in to file a reproducibility report.
Related papers
- Post-translational epigenetics: PRMT7 regulates RNA-binding capacity and protein stability to control Leishmania parasite virulence
Tiago Rodrigues Ferreira, Adam Dowle, … Pegine B. Walrad·bioRxiv·Aug 15, 2019
- Polyamines shift expression of macrophage L-arginine metabolism related-genes during Leishmania amazonensis infection
Jonathan Miguel Zanatta, Stephanie Maia Acuña, … Sandra Márcia Muxel·bioRxiv·May 27, 2022
- A systematic survey of PRMT interactomes reveals the key roles of arginine methylation in the global control of RNA splicing and translation
Huanhuan Y. Wei, Xiaojuan Fan, … Zefeng Wang·中国科学通报:英文版Peer-reviewed·Jan 14, 2021
- The mRNA-bound proteome of Leishmania mexicana: novel genetic insight into an ancient parasite
Luis Miguel De Pablos, Tiago Rodrigues Ferreira, … Pegine B. Walrad·Molecular & Cellular ProteomicsPeer-reviewed·Apr 4, 2019
- LC-MS profiling of prmt-1 and prmt-5 knockout C. elegans reveals PRMT-1 substrates and global proteome remodeling
Ali Basirattalab, Dylan C Wallis, … Nicholas Alexander Graham·bioRxiv·Feb 16, 2026
- RNA-binding proteins and regulatory networks involved in life-stage, stress temperature, and drug resistance in Leishmania parasites
Eduardo Martínez, Víctor Aliaga-Tobar, … Alberto J. M. Martín·bioRxiv·Feb 17, 2026