Vitor de Freitas
Current Organizations / Institutes
The organizations/institutes from the scholar's latest article
Research Subjects
Research Interests
Vitor de Freitas has a total of 15 co-authors. Here are the top co-authors by number of shared publications:
- Alessandra Monteiro Rosini
Laboratory of Immunophysiology of Reproduction, Institute of Biomedical Science, Universidade Federal de Uberlândia, Campus Umuarama, Av. Pará, 1720, Uberlândia 38405-318, MG, Brazil
1 shared publication - Aryani Felixa Fajardo Martínez
Laboratory of Immunophysiology of Reproduction, Institute of Biomedical Science, Universidade Federal de Uberlândia, Campus Umuarama, Av. Pará, 1720, Uberlândia 38405-318, MG, Brazil
1 shared publication - Bellisa Freitas Barbosa
Laboratory of Immunophysiology of Reproduction, Institute of Biomedical Sciences, Universidade Federal de Uberlândia, Uberlândia 38405-318, MG, Brazil
1 shared publication - Daiana Silva Lopes
Institute Multidisciplinary in Health, Universidade Federal da Bahia (UFBA), Vitória da Conquista 45029-094, BA, Brazil
1 shared publication - Eloisa Amália Vieira Ferro
Laboratory of Immunophysiology of Reproduction, Institute of Biomedical Sciences, Universidade Federal de Uberlândia, Uberlândia 38405-318, MG, Brazil
1 shared publication - Guilherme de Souza
Laboratory of Immunophysiology of Reproduction, Institute of Biomedical Sciences, Universidade Federal de Uberlândia, Uberlândia 38405-318, MG, Brazil
1 shared publication
Latest Publications
- Open Access
Insights into the Role of Proteolytic and Adhesive Domains of Snake Venom Metalloproteinases from Bothrops spp. in the Control of Toxoplasma gondii Infection
Toxoplasmosis is an alarming public health problem that affects more than one-third of the world’s population. In our work, we investigated the antiparasitic effects of catalytically active [BpMP-I and Jararhagin (Jar)] and catalytically inactive [Jararhagin-C (Jar-C)] snake venom metalloproteinases (SVMPs) in human HeLa cells. These toxins impaired the parasite invasion and intracellular growth, and modulated IL-6, IL-8, and MIF cytokines that control the cell susceptibility and response against T. gondii. Furthermore, we verified that the antiprotozoal activities are not restricted to the presence of the proteolytic domain, and the adhesive domains participate in the control of T. gondii infection. Also, by analyzing the structures of Jar and Jar-C through molecular modeling and dynamics, we observed that the adhesive domains in Jar-C are more exposed due to the absence of the proteolytic domain, which could favor the interaction with different targets. Our investigation on the role of SVMP domains in combating T. gondii infection highlights their potential application as biotechnological tools for creating more effective treatments for toxoplasmosis.
Open AccessInsights into the Role of Proteolytic and Adhesive Domains of Snake Venom Metalloproteinases from Bothrops spp. in the Control of Toxoplasma gondii Infection
Toxoplasmosis is an alarming public health problem that affects more than one-third of the world’s population. In our work, we investigated the antiparasitic effects of catalytically active [BpMP-I and Jararhagin (Jar)] and catalytically inactive [Jararhagin-C (Jar-C)] snake venom metalloproteinases (SVMPs) in human HeLa cells. These toxins impaired the parasite invasion and intracellular growth, and modulated IL-6, IL-8, and MIF cytokines that control the cell susceptibility and response against T. gondii. Furthermore, we verified that the antiprotozoal activities are not restricted to the presence of the proteolytic domain, and the adhesive domains participate in the control of T. gondii infection. Also, by analyzing the structures of Jar and Jar-C through molecular modeling and dynamics, we observed that the adhesive domains in Jar-C are more exposed due to the absence of the proteolytic domain, which could favor the interaction with different targets. Our investigation on the role of SVMP domains in combating T. gondii infection highlights their potential application as biotechnological tools for creating more effective treatments for toxoplasmosis.