Version 1
: Received: 11 June 2024 / Approved: 11 June 2024 / Online: 12 June 2024 (08:58:44 CEST)
How to cite:
Aranda-Chan, V.; Cárdenas-Guerra, R. E.; Otero-Peraza, A.; Pacindo-Cabrales, E. E.; Flores-Pucheta, C. I.; Montes-Flores, O.; Arroyo, R.; Ortega-López, J. Insights Into Peptidyl-Prolyl Cis-Trans Isomerases From Clinically Important Protozoans: From Structure to Potential Biotechnological Applications. Preprints2024, 2024060718. https://doi.org/10.20944/preprints202406.0718.v1
Aranda-Chan, V.; Cárdenas-Guerra, R. E.; Otero-Peraza, A.; Pacindo-Cabrales, E. E.; Flores-Pucheta, C. I.; Montes-Flores, O.; Arroyo, R.; Ortega-López, J. Insights Into Peptidyl-Prolyl Cis-Trans Isomerases From Clinically Important Protozoans: From Structure to Potential Biotechnological Applications. Preprints 2024, 2024060718. https://doi.org/10.20944/preprints202406.0718.v1
Aranda-Chan, V.; Cárdenas-Guerra, R. E.; Otero-Peraza, A.; Pacindo-Cabrales, E. E.; Flores-Pucheta, C. I.; Montes-Flores, O.; Arroyo, R.; Ortega-López, J. Insights Into Peptidyl-Prolyl Cis-Trans Isomerases From Clinically Important Protozoans: From Structure to Potential Biotechnological Applications. Preprints2024, 2024060718. https://doi.org/10.20944/preprints202406.0718.v1
APA Style
Aranda-Chan, V., Cárdenas-Guerra, R. E., Otero-Peraza, A., Pacindo-Cabrales, E. E., Flores-Pucheta, C. I., Montes-Flores, O., Arroyo, R., & Ortega-López, J. (2024). Insights Into Peptidyl-Prolyl Cis-Trans Isomerases From Clinically Important Protozoans: From Structure to Potential Biotechnological Applications. Preprints. https://doi.org/10.20944/preprints202406.0718.v1
Chicago/Turabian Style
Aranda-Chan, V., Rossana Arroyo and Jaime Ortega-López. 2024 "Insights Into Peptidyl-Prolyl Cis-Trans Isomerases From Clinically Important Protozoans: From Structure to Potential Biotechnological Applications" Preprints. https://doi.org/10.20944/preprints202406.0718.v1
Abstract
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, and Giardia intestinalis, 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, the biological structure‒function characterization of PPIases from these protozoan parasites is still incomplete. The recombinant production of these enzymes is highly relevant for this ongoing research. In this review, we explore the structural diversity, functions, recombinant production, and 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.
Copyright:
This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
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