PreprintArticleVersion 1This version is not peer-reviewed
Exploration of COX-Like Activity in Wild-Type gp63 Recombinant Protein from Leishmania mexicana; Identification of Orthologous Proteins in Clinically Significant Parasites, and Investigation of Arachidonic Acid Binding Sites
Version 1
: Received: 29 July 2024 / Approved: 30 July 2024 / Online: 31 July 2024 (08:57:23 CEST)
How to cite:
Hernández-Ramírez, V.-I.; Matus-Meza, A.-S.; Oviedo, N.; Magos-Castro, M. A.; Osorio-Trujillo, C.; Salazar-Villatoro, L.; Constantino-Jonapa, L. A.; Talamás-Rohana, P. Exploration of COX-Like Activity in Wild-Type gp63 Recombinant Protein from Leishmania mexicana; Identification of Orthologous Proteins in Clinically Significant Parasites, and Investigation of Arachidonic Acid Binding Sites. Preprints2024, 2024072496. https://doi.org/10.20944/preprints202407.2496.v1
Hernández-Ramírez, V.-I.; Matus-Meza, A.-S.; Oviedo, N.; Magos-Castro, M. A.; Osorio-Trujillo, C.; Salazar-Villatoro, L.; Constantino-Jonapa, L. A.; Talamás-Rohana, P. Exploration of COX-Like Activity in Wild-Type gp63 Recombinant Protein from Leishmania mexicana; Identification of Orthologous Proteins in Clinically Significant Parasites, and Investigation of Arachidonic Acid Binding Sites. Preprints 2024, 2024072496. https://doi.org/10.20944/preprints202407.2496.v1
Hernández-Ramírez, V.-I.; Matus-Meza, A.-S.; Oviedo, N.; Magos-Castro, M. A.; Osorio-Trujillo, C.; Salazar-Villatoro, L.; Constantino-Jonapa, L. A.; Talamás-Rohana, P. Exploration of COX-Like Activity in Wild-Type gp63 Recombinant Protein from Leishmania mexicana; Identification of Orthologous Proteins in Clinically Significant Parasites, and Investigation of Arachidonic Acid Binding Sites. Preprints2024, 2024072496. https://doi.org/10.20944/preprints202407.2496.v1
APA Style
Hernández-Ramírez, V. I., Matus-Meza, A. S., Oviedo, N., Magos-Castro, M. A., Osorio-Trujillo, C., Salazar-Villatoro, L., Constantino-Jonapa, L. A., & Talamás-Rohana, P. (2024). Exploration of COX-Like Activity in Wild-Type gp63 Recombinant Protein from Leishmania mexicana; Identification of Orthologous Proteins in Clinically Significant Parasites, and Investigation of Arachidonic Acid Binding Sites. Preprints. https://doi.org/10.20944/preprints202407.2496.v1
Chicago/Turabian Style
Hernández-Ramírez, V., Luis Alejandro Constantino-Jonapa and Patricia Talamás-Rohana. 2024 "Exploration of COX-Like Activity in Wild-Type gp63 Recombinant Protein from Leishmania mexicana; Identification of Orthologous Proteins in Clinically Significant Parasites, and Investigation of Arachidonic Acid Binding Sites" Preprints. https://doi.org/10.20944/preprints202407.2496.v1
Abstract
Recently, we published that the monoclonal antibody (D12 mAb) recognizes gp63 of L. mexicana, it is responsible for COX activity. This D12 mAb exhibited cross-reactivity with Trypanosoma cruzi, Entamoeba histolytica, Acanthamoeba castellanii, and Naegleria fowleri. COX activity assays performed in these parasites suggested the potential presence of such enzymatic activity. In our investigation, we confirmed that wild-type recombinant gp63 exhibits COX-like activity, in contrast to a mutated recombinant gp63 variant. Consequently, our objective was to identify sequences orthologous to gp63 and subsequently analyze the binding of arachidonic acid (AA) to the putative active sites of these proteins. Given the absence of a crystallized structure for this protein in the Protein Data Bank (PDB), it was imperative to first obtain a three-dimensional structure by homology modeling, using leishmanolysin (PDB ID: LML1) as a template in the Swiss model. Database. The results obtained through molecular docking simulations revealed the primary interactions of AA close to the Zinc atom present in the catalytic site of gp63-like molecules of several parasites, predominantly mediated by hydrogen bonds with HIS264, HIS268 and HIS334. Furthermore, COX activity was evaluated in commensal species such as E. dispar and during the encystment process of E. invadens.
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