Bicistronic Vector Expression of Recombinant Jararhagin-C and Its Effects on Endothelial Cells

How to cite: Ferraz, K. F.; Caetano de Luca, L. H.; Orefice, D. P.; Calabria, P. A. L.; Della-Casa, M. S.; Freitas-de-Sousa, L. A.; Beraldo-Neto, E.; Sanabani, S. S.; Magalhaes, G. S.; Clissa, P. B. Bicistronic Vector Expression of Recombinant Jararhagin-C and Its Effects on Endothelial Cells. Preprints 2024, 2024100320. https://doi.org/10.20944/preprints202410.0320.v1 Ferraz, K. F.; Caetano de Luca, L. H.; Orefice, D. P.; Calabria, P. A. L.; Della-Casa, M. S.; Freitas-de-Sousa, L. A.; Beraldo-Neto, E.; Sanabani, S. S.; Magalhaes, G. S.; Clissa, P. B. Bicistronic Vector Expression of Recombinant Jararhagin-C and Its Effects on Endothelial Cells. Preprints 2024, 2024100320. https://doi.org/10.20944/preprints202410.0320.v1

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MDPI and ACS Style

Ferraz, K. F.; Caetano de Luca, L. H.; Orefice, D. P.; Calabria, P. A. L.; Della-Casa, M. S.; Freitas-de-Sousa, L. A.; Beraldo-Neto, E.; Sanabani, S. S.; Magalhaes, G. S.; Clissa, P. B. Bicistronic Vector Expression of Recombinant Jararhagin-C and Its Effects on Endothelial Cells. Preprints 2024, 2024100320. https://doi.org/10.20944/preprints202410.0320.v1

APA Style

Ferraz, K. F., Caetano de Luca, L. H., Orefice, D. P., Calabria, P. A. L., Della-Casa, M. S., Freitas-de-Sousa, L. A., Beraldo-Neto, E., Sanabani, S. S., Magalhaes, G. S., & Clissa, P. B. (2024). Bicistronic Vector Expression of Recombinant Jararhagin-C and Its Effects on Endothelial Cells. Preprints. https://doi.org/10.20944/preprints202410.0320.v1

Chicago/Turabian Style

Ferraz, K. F., Geraldo Santana Magalhaes and Patricia Bianca Clissa. 2024 "Bicistronic Vector Expression of Recombinant Jararhagin-C and Its Effects on Endothelial Cells" Preprints. https://doi.org/10.20944/preprints202410.0320.v1

Abstract

Jararhagin-C (JarC) is a protein from the venom of Bothrops jararaca consisting of disintegrin-like and cysteine-rich domains. JarC shows a modulating effect on angiogenesis and remodeling of extracellular matrix constituents improving wound healing in mice experimental model. JarC is purified from crude venom and the yield is less than 1 %. The aim of this work was to obtain the recombinant form of JarC and to test its biological activity. For this purpose, the bicistronic vector pSUMOUlp1 was used. This vector allowed the expression of the recombinant toxin JarC (rJarC) in fusion with the small ubiquitin-related modifier (SUMO) as well as the SUMO protease Ulp1. After expression, this protease was able to efficiently remove SUMO from rJarC inside the bacteria. rJarC free from SUMO was purified at the expected molecular mass, and recognized by polyclonal anti-Jararhagin antibodies. In terms of biological activity, both the native and recombinant forms showed no toxicity to the HUVEC cell line CRL1730 and were effective in modulating cell migration activity in experimental in vitro model. These results demonstrate the successful production of rJarC and the preservation of its biological activity, which may facilitate further investigations into the therapeutic potential of this snake venom-derived protein.

Keywords

snake venom disintegrins; recombinant protein; Jararhagin-C; endothelial cells

Subject

Biology and Life Sciences, Biology and Biotechnology

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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