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Article

Trypanosoma cruzi Presenilin-Like Transmembrane Aspartyl Protease: Characterization and Cellular Localization

by
Guilherme C. Lechuga
1,2,
Paloma Napoleão-Pêgo
1,
Carolina C. G. Bottino
1,
Rosa T. Pinho
4,
David W. Provance-Jr
1,3 and
Salvatore G. De-Simone
1,5,*
1
Center for Technological Development in Health/National Institute of Science and Technology for Innovation on Diseases of Neglected Population (INCT-IDPN), FIOCRUZ, Rio de Janeiro 21040-900, Brazil
2
Cellular Ultrastructure Laboratory, FIOCRUZ, Oswaldo Cruz Institute, Rio de Janeiro 21040-900, Brazil
3
Interdisciplinary Medical Research Laboratory, FIOCRUZ, Oswaldo Cruz Institute, Rio de Janeiro 21040-900, Brazil
4
Clinical Immunology Laboratory, FIOCRUZ, Oswaldo Cruz Institute, Rio de Janeiro 21040-900, Brazil
5
Department of Molecular and Cellular Biology, Federal Fluminense University, Niterói 24220-008, Brazil
*
Author to whom correspondence should be addressed.
Biomolecules 2020, 10(11), 1564; https://doi.org/10.3390/biom10111564
Submission received: 30 September 2020 / Revised: 6 November 2020 / Accepted: 9 November 2020 / Published: 17 November 2020
(This article belongs to the Section Cellular Biochemistry)
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Abstract

The increasing detection of infections of Trypanosoma cruzi, the etiological agent of Chagas disease, in non-endemic regions beyond Latin America has risen to be a major public health issue. With an impact in the millions of people, current treatments rely on antiquated drugs that produce severe side effects and are considered nearly ineffective for the chronic phase. The minimal progress in the development of new drugs highlights the need for advances in basic research on crucial biochemical pathways in T. cruzi to identify new targets. Here, we report on the T. cruzi presenilin-like transmembrane aspartyl enzyme, a protease of the aspartic class in a unique phylogenetic subgroup with T. vivax separate from protozoans. Computational analyses suggest it contains nine transmembrane domains and an active site with the characteristic PALP motif of the A22 family. Multiple linear B-cell epitopes were identified by SPOT-synthesis analysis with Chagasic patient sera. Two were chosen to generate rabbit antisera, whose signal was primarily localized to the flagellar pocket, intracellular vesicles, and endoplasmic reticulum in parasites by whole-cell immunofluorescence. The results suggest that the parasitic presenilin-like enzyme could have a role in the secretory pathway and serve as a target for the generation of new therapeutics specific to the T. cruzi.
Keywords: Trypanosoma cruzi; presenilin; aspartic protease; SPOT-synthesis; anti-peptide antibodies; immunolocalization; transmembrane domains Trypanosoma cruzi; presenilin; aspartic protease; SPOT-synthesis; anti-peptide antibodies; immunolocalization; transmembrane domains
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MDPI and ACS Style

Lechuga, G.C.; Napoleão-Pêgo, P.; Bottino, C.C.G.; Pinho, R.T.; Provance-Jr, D.W.; De-Simone, S.G. Trypanosoma cruzi Presenilin-Like Transmembrane Aspartyl Protease: Characterization and Cellular Localization. Biomolecules 2020, 10, 1564. https://doi.org/10.3390/biom10111564

AMA Style

Lechuga GC, Napoleão-Pêgo P, Bottino CCG, Pinho RT, Provance-Jr DW, De-Simone SG. Trypanosoma cruzi Presenilin-Like Transmembrane Aspartyl Protease: Characterization and Cellular Localization. Biomolecules. 2020; 10(11):1564. https://doi.org/10.3390/biom10111564

Chicago/Turabian Style

Lechuga, Guilherme C., Paloma Napoleão-Pêgo, Carolina C. G. Bottino, Rosa T. Pinho, David W. Provance-Jr, and Salvatore G. De-Simone. 2020. "Trypanosoma cruzi Presenilin-Like Transmembrane Aspartyl Protease: Characterization and Cellular Localization" Biomolecules 10, no. 11: 1564. https://doi.org/10.3390/biom10111564

APA Style

Lechuga, G. C., Napoleão-Pêgo, P., Bottino, C. C. G., Pinho, R. T., Provance-Jr, D. W., & De-Simone, S. G. (2020). Trypanosoma cruzi Presenilin-Like Transmembrane Aspartyl Protease: Characterization and Cellular Localization. Biomolecules, 10(11), 1564. https://doi.org/10.3390/biom10111564

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