VERONICA ARANDA CHAN

RESEARCH, TEACHING, or OTHER INTERESTS

Biochemistry, Genetics and Molecular Biology, Biotechnology, Molecular Medicine, Structural Biology

Scopus Publications

Trichocystatin-2 from Trichomonas vaginalis: role of N-terminal cysteines in aggregation, protease inhibition, and trichomonal cysteine protease-dependent cytotoxicity on HeLa cells
Verónica Aranda-Chan, Montserrat Gutiérrez-Soto, Claudia Ivonne Flores-Pucheta, Octavio Montes-Flores, Rossana Arroyo, Jaime Ortega-López
Frontiers in Parasitology, 2025
Trichomonas vaginalis is a protozoan parasite that causes trichomoniasis, the most common nonviral neglected sexually transmitted disease worldwide. Biomarkers and therapeutic targets, including specific trichomonad cysteine proteases (CPs) and their endogenous inhibitors, have been identified to diagnose and treat this disease. Trichocystatin 2 (TC-2) was previously identified as one of the three endogenous inhibitors of the parasite’s cathepsin L-like CPs, including TvCP39, which is involved in T. vaginalis cytotoxicity and is a potential therapeutic target. TC-2 contains five cysteines, including four located in the N-terminal sequence. These cysteines may be responsible for the formation of multimers of the recombinant protein expressed in E. coli. To determine whether these cysteines are responsible for the formation of TC-2 multimers and the effect of the N-terminus on CP inhibition, a recombinant TC-2 mutant was expressed, purified, characterized, and compared with the recombinant wild-type TC-2 protein. In silico and experimental analyses revealed that wild-type and mutant TC-2 proteins presented similar results in terms of secondary and tertiary structure prediction and high thermal stability. However, compared with that of wild-type TC-2, multimer formation was significantly reduced in the mutant lacking the four N-terminal cysteines, leading to a significant reduction in papain inhibition but not in trichomonal CP activity. These results support the hypothesis that the four cysteines located in the N-terminal region are responsible for aggregation, and their deletion affected the interaction of TC-2 with papain without affecting its inhibitory activity on homologous target proteases that are crucial for T. vaginalis virulence. Our results provide essential data supporting the use of TC-2 as a potential therapeutic target.
Insights into Peptidyl-Prolyl cis-trans Isomerases from Clinically Important Protozoans: From Structure to Potential Biotechnological Applications
Verónica Aranda-Chan, Rosa Elena Cárdenas-Guerra, Alejandro Otero-Pedraza, Esdras Enoc Pacindo-Cabrales, Claudia Ivonne Flores-Pucheta, Octavio Montes-Flores, Rossana Arroyo, Jaime Ortega-López
Pathogens, 2024
Peptidyl-prolyl cis/trans isomerases (PPIases) are present in a wide variety of microorganisms, including protozoan parasites such as Trypanosoma cruzi, Trypanosoma brucei, Trichomonas vaginalis, Leishmania major, Leishmania donovani, Plasmodium falciparum, Plasmodium vivax, Entamoeba histolytica, Giardia intestinalis, Cryptosporidium parvum, and Cryptosporidium hominis, all of which cause important neglected diseases. PPIases are classified as cyclophilins, FKBPs, or parvulins and play crucial roles in catalyzing the cis-trans isomerization of the peptide bond preceding a proline residue. This activity assists in correct protein folding. However, experimentally, the biological structure–function characterization of PPIases from these protozoan parasites has been poorly addressed. The recombinant production of these enzymes is highly relevant for this ongoing research. Thus, this review explores the structural diversity, functions, recombinant production, activity, and inhibition of protozoan PPIases. We also highlight their potential as biotechnological tools for the in vitro refolding of other recombinant proteins from these parasites. These applications are invaluable for the development of diagnostic and therapeutic tools.

RECENT SCHOLAR PUBLICATIONS

Trichocystatin-2 from Trichomonas vaginalis : role of N-terminal cysteines in aggregation, protease inhibition, and trichomonal cysteine protease-dependent …
V Aranda-Chan, M Gutiérrez-Soto, CI Flores-Pucheta, O Montes-Flores, ...
Frontiers in Parasitology 4, 1512012 , 2025
2025.0
Citations: 3
Insights into Peptidyl-Prolyl cis - trans Isomerases from Clinically Important Protozoans: From Structure to Potential Biotechnological Applications
V Aranda-Chan, RE Cárdenas-Guerra, A Otero-Pedraza, ...
Pathogens 13 (8), 644 , 2024
2024.0
Citations: 12
Estudio de replegamiento in vitro de proteínas de parásitos de difícil expresión en E. coli, utilizando peptidil-prolil-cis/trans-isomerasas de parásito y chaperones moleculares
VS Aranda Chan
Tesis (DC)--Centro de Investigación y de Estudios Avanzados del IPN … , 2024
2024.0
XX Congreso Nacional de Biotecnología y Bioingeniería
V Aranda-Chan, R Arroyo-Verástegui, A Meneses, R Marsch, ...

MOST CITED SCHOLAR PUBLICATIONS

Insights into Peptidyl-Prolyl cis - trans Isomerases from Clinically Important Protozoans: From Structure to Potential Biotechnological Applications
V Aranda-Chan, RE Cárdenas-Guerra, A Otero-Pedraza, ...
Pathogens 13 (8), 644 , 2024
2024.0
Citations: 12
Trichocystatin-2 from Trichomonas vaginalis : role of N-terminal cysteines in aggregation, protease inhibition, and trichomonal cysteine protease-dependent …
V Aranda-Chan, M Gutiérrez-Soto, CI Flores-Pucheta, O Montes-Flores, ...
Frontiers in Parasitology 4, 1512012 , 2025
2025.0
Citations: 3
Estudio de replegamiento in vitro de proteínas de parásitos de difícil expresión en E. coli, utilizando peptidil-prolil-cis/trans-isomerasas de parásito y chaperones moleculares
VS Aranda Chan
Tesis (DC)--Centro de Investigación y de Estudios Avanzados del IPN … , 2024
2024.0
XX Congreso Nacional de Biotecnología y Bioingeniería
V Aranda-Chan, R Arroyo-Verástegui, A Meneses, R Marsch, ...