SUMOylation of Paraflagellar Rod Protein, PFR1, and Its Stage-specific Localization in Trypanosoma Cruzi

Overview

Journal PLoS One

Specialties General Medicine
Science

Date 2012 May 23

PMID 22615934

Citations 7

Authors

Takeshi Annoura

Takashi Makiuchi

Idalia Sariego

Takashi Aoki

Takeshi Nara

Affiliations

Soon will be listed here.

Abstract

Background: The flagellate protozoan parasite, Trypanosoma cruzi, is a causative agent of Chagas disease that is transmitted by reduviid bugs to humans. The parasite exists in multiple morphological forms in both vector and host, and cell differentiation in T. cruzi is tightly associated with stage-specific protein synthesis and degradation. However, the specific molecular mechanisms responsible for this coordinated cell differentiation are unclear.

Methodology/principal Findings: The SUMO conjugation system plays an important role in specific protein expression. In T. cruzi, a subset of SUMOlylated protein candidates and the nuclear localization of SUMO have been shown. Here, we examined the biological roles of SUMO in T. cruzi. Site-directed mutagenesis analysis of SUMO consensus motifs within T. cruzi SUMO using a bacterial SUMOylation system revealed that T. cruzi SUMO can polymerize. Indirect fluorescence analysis using T. cruzi SUMO-specific antibody showed the extra-nuclear localization of SUMO on the flagellum of epimastigote and metacyclic and bloodstream trypomastigote stages. In the short-flagellate intracellular amastigote, an extra-nuclear distribution of SUMO is associated with basement of the flagellum and becomes distributed along the flagellum as amastigote transforms into trypomastigote. We examined the flagellar target protein of SUMO and show that a paraflagellar rod protein, PFR1, is SUMOylated.

Conclusions: These findings indicate that SUMOylation is associated with flagellar homeostasis throughout the parasite life cycle, which may play an important role in differentiation of T. cruzi.

Citing Articles

Ubiquitination and the Proteasome as Drug Targets in Trypanosomatid Diseases.

Bijlmakers M Front Chem. 2021; 8:630888.

PMID: 33732684 PMC: 7958763. DOI: 10.3389/fchem.2020.630888.

The SENP Protease Is Required for SUMO Processing but Not for Viability.

Bea A, Krober-Boncardo C, Sandhu M, Brinker C, Clos J Genes (Basel). 2020; 11(10).

PMID: 33066659 PMC: 7602377. DOI: 10.3390/genes11101198.

Ubiquitin-Like Modifiers: Emerging Regulators of Protozoan Parasites.

Karpiyevich M, Artavanis-Tsakonas K Biomolecules. 2020; 10(10).

PMID: 33022940 PMC: 7600729. DOI: 10.3390/biom10101403.

Characterization and Diagnostic Application of Trypanosoma cruzi Trypomastigote Excreted-Secreted Antigens Shed in Extracellular Vesicles Released from Infected Mammalian Cells.

Bautista-Lopez N, Ndao M, Vasquez Camargo F, Nara T, Annoura T, Hardie D J Clin Microbiol. 2016; 55(3):744-758.

PMID: 27974541 PMC: 5328442. DOI: 10.1128/JCM.01649-16.

Biosynthesis of SUMOylated Proteins in Bacteria Using the Trypanosoma brucei Enzymatic System.

Iribarren P, Berazategui M, Cazzulo J, Alvarez V PLoS One. 2015; 10(8):e0134950.

PMID: 26258470 PMC: 4530879. DOI: 10.1371/journal.pone.0134950.

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