He attended the University of Sao Paulo (Bacharel Degree in Biology, 1987; Ph.D. in 1992, under the guidance of Dr. Ohara Augusto). Later (from December 1992 to May 1996), I was a NIH Postdoctoral Fellow in the Laboratory of Biochemistry National Heart, Lung and Blood Institute in collaboration with Dr. Stadtman, E.R. Currently he is full professor at the Department of Genetics and Evolutionary Biology, Institute of Biosciences, University of São Paulo. He is interested in studying the mechanisms by which cells defend themselves against the toxic effects of free radicals and related species, with emphasis on a class of proteins called peroxiredoxin, which includes thioredoxin peroxidases. Therefore, their lines of research are focused on the redox chemistry and biology of thiols such as thioredoxin, glutaredoxin, peroxiredoxin and glutathione. Saccharomyces cerevisiae has been used as a model organism. The antioxidant defense mechanisms of pathogenic bacteria are also studied especially those from the phytopathogen Xylella fastidiosa, but also from Chromobacterium violaceum and Pseudomonas aeruginosa. His group has characterized for the first time the role of a new class of antioxidant enzymes, called Ohr ("Organic hydroperoxide Resistance protein). Such investigations have gained prominence as a result of the human microbiota metagenomic projects. It is noteworthy that Ohr enzymes are abundant in bacteria that colonize the gastrointestinal tract (Molecular & Cellular Proteomics 11: 1-13, 2012). As animals and plants generate oxidants in an attempt to kill pathogens, Ohr may play a role in the pathogenicity of bacteria. In this context, his group also performs structural biology analyzes of antioxidant proteins, elucidating Ohr structure. So far, the coordinates of eight protein structures were deposited at the Protein Data Bank. He is a member of the steering committee of the CEPID Redoxoma (http://redoxoma.iq.usp.br/); editorial board of the Free Radical Biology and Medicine and academic editor of PLoS One (Source: Lattes Curriculum)
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Mitochondria are not only the powerhouses of the cell, but also play central roles in biological processes such as aging, cancer and neurodegenerative diseases. H2O2 is a byproduct of oxidative phosphorylation that is now also recognized to mediate signaling pathways underlying physiology and pathology. Therefore, the comprehension of the mechanisms that degrade H2O2 generated inside the …
The study of redox processes has high potential to elucidate integrative mechanisms, due to the ubiquity and strength of their effects. Many studies involve the role of redox mechanisms in diseases. However, the complexity of this field has increased concerning structures, structure-function relations, methods, molecular and sub-cellular pathology of redox-regulated proteins, genomics, pr…
The classical concept of oxidative stress is "a disturbance in the pro-oxidant-antioxidant balance in favor of the former". However, the accumulation of data indicates that a more useful definition is a "disruption of redox signaling and control" [...]. The tri-peptide glutathione plays a central role in the redox homeostasis, but there are also other thiols that participate in redox sign…
Plants and animals respond to infections by pathogenic agents using among other mechanisms an oxidative burst. In this way, Xylella fastidiosa and other pathogenic agents have to overcome the oxidative burst generated by plants to be successful in the infection. Our objective in this project is the search for potential inhibitors of antioxidant enzymes of Xyllela fastidiosa in banks of ex…
(Only some records are available in English at this moment)
Ohr enzymes are thiol-dependent peroxidases, characterized by two highly conserved cysteine residues and efficient organic peroxide detoxification. The first Ohr enzyme was discovered in the phytopathogen Xanthomonas campestris, then followed by the identification of many Ohr proteins in prokaryotes, which were considered the only type of organisms having this enzyme. However, a recent st…
Pseudomonas aeruginosa is a ubiquitous, gamma-proteobacteria, which are the main cause of nosocomial infection among all pathogens related to Pneumonia in the Intensive Care Unit. Among the various host's defense mechanisms, we are interested in the release of reactive oxygen and nitrogen species by phagocytes. LsfA belongs to the peroxiredoxin (Prx) family and to the subgroup that contai…
Reactive oxygen species (ROS) are mainly formed during aerobic metabolism and their production is intensified when cells are under chemical, physical and mechanical stresses, generating molecules such as hydrogen peroxide, hydroxyl radical and superoxide anion. These compounds can cause damage to cellular machinery, such as lipid peroxidation and dismantling of the membrane when there is …
(Only some records are available in English at this moment)
At low levels, ROS and especially H2O2 can trigger thiol-based signaling pathways that underlie important physiological processes. In plants, the 1-Cys PRX (PER1) is an enzyme that is highly efficient in H2O2 reduction that is mainly present in the nucleus of cells that take part of seeds. PER1 expression spatially and temporally follows events associated with seed germination. Recently, …
Pseudomonas aeruginosa is a ubiquitous and opportunistic pathogen that is exposed to an oxidative burst among other stresses during host invasion. To overcome this challenge, bacteria use a set of antioxidant proteins, including LsfA, a peroxiredoxin involved with the bacterial virulence that is capable to reduce H2O2 and other hydroperoxides at extremely fast rates. Thereby, LsfA protect…
VAPB is a transmembrane protein located in the endoplasmic reticulum (ER) due to the presence of a transmembrane domains (TMD) in its C-terminal region, besides a MSP (Major Sperm Protein) domain in its N-terminal region. The mutation of a proline by a serine at the position 56 of the MSP domain is involved with the familial type 8 of Amyotrophic Lateral Sclerosis (ALS). ALS is a neurodeg…
Peroxiredoxins (Prxs) are Cys-based thiol-dependent peroxidases that contain one (1-Cys Prx) or two (2-Cys Prx) Cys residues involved in catalysis. To date, all characterized Prxs display the universal motif PxxxT/SxxC and can reduce hydroperoxides with extraordinary rates, ranging from 106 to 108 M-1 s-1. In spite of being a heterogeneous family, all Prxs present the peroxidase activity …
(Only some records are available in English at this moment)
| 2 / 2 | Ongoing research grants |
| 10 / 7 | Completed research grants |
| 3 / 3 | Ongoing scholarships in Brazil |
| 56 / 23 | Completed scholarships in Brazil |
| 1 / 1 | Ongoing scholarships abroad |
| 4 / 4 | Completed scholarships abroad |
| 76 / 40 | All research grants and scholarships |
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CV Lattes
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