A5010809600- Venomous Animal Envenomation and Studies
- Rabies epidemiology and control
- Biochemical and Structural Characterization
- Antimicrobial Peptides and Activities
- Blood Coagulation and Thrombosis Mechanisms
- Marine Invertebrate Physiology and Ecology
- Healthcare and Venom Research
- Parasitic infections in humans and animals
- Amphibian and Reptile Biology
- Cell Adhesion Molecules Research
- Protease and Inhibitor Mechanisms
- Mosquito-borne diseases and control
- Echinoderm biology and ecology
- Cellular transport and secretion
- Bioinformatics and Genomic Networks
- Advanced Proteomics Techniques and Applications
- Viral Infections and Vectors
- Antifungal resistance and susceptibility
- Bioactive Natural Diterpenoids Research
- Parasitic Infections and Diagnostics
- Vector-borne infectious diseases
- Leptospirosis research and findings
- Coagulation, Bradykinin, Polyphosphates, and Angioedema
- Oil Palm Production and Sustainability
- Toxin Mechanisms and Immunotoxins
Instituto Butantan
2016-2025
University Medical Center Freiburg
2020
University of Freiburg
2020
Fundação de Amparo à Pesquisa do Estado de São Paulo
2005-2014
University of Papua New Guinea
2014
Universidade de São Paulo
2008-2012
Universidade Federal de São Paulo
2010
Instituto Vital Brazil (Brazil)
2005
University of Virginia
2003
The complexity of Viperid venoms has long been appreciated by investigators in the fields toxinology and medicine. However, it is only recently that depth become somewhat quantitatively qualitatively appreciated. With resurgence two-dimensional gel electrophoresis (2-DE) advances mass spectrometry virtually all venom components can be visualized identified given sufficient effort resources. Here we present use 2-DE for examining as well demonstrating interesting approaches to selectively...
Previous studies have demonstrated that the pharmacological activities displayed by Bothrops jararaca venom undergo a significant ontogenetic shift. Variation in proteome is well-documented phenomenon; however, variation peptidome poorly understood. We report comparative proteomic and peptidomic analysis of venoms from newborn adult specimens B. correlate it with evaluation important features. demonstrate similar hemorrhagic activities, while has slightly higher lethal activity mice;...
We investigated the putative toxins of Philodryas olfersii (Colubridae), a representative family snakes neglected in venom studies despite their growing medical importance. Transcriptomic data gland complemented by proteomic analysis secretion revealed presence major toxin classes from Viperidae family, including serine proteases, metalloproteases, C‐type lectins, Crisps, and natriuretic peptide (CNP). Interestingly, phylogenetic CNP precursor showed it as linker between two related...
Snake venom proteomes/peptidomes are highly complex and maintenance of their integrity within the gland lumen is crucial for expression toxin activities. There has been considerable progress in field proteomics, however, peptidomics does not as fast, because lack comprehensive sequence databases analysis MS data. Therefore, many cases peptides have to be sequenced manually by MS/MS or Edman degradation. This critical rare snake species, case Bothrops cotiara (BC) B. fonsecai (BF), which...
Background Snake bite is a neglected public health problem in communities rural areas of several countries. Bothrops jararaca causes many snake bites Brazil and previous studies have demonstrated that the pharmacological activities displayed by its venom undergo significant ontogenetic shift. Similarly, proteome B. exhibits considerable variation upon neonate to adult transition, which associated with changes diet from ectothermic prey early life endothermic adulthood. Moreover, it has been...
Comparisons between venoms from snakes kept under captivity or collected at the natural environment are of fundamental importance in order to obtain effective antivenoms treat human victims snakebites. In this study, we compared composition and biological activities Bothrops atrox venom Tapajós National Forest (Pará State, Brazil) maintained for more than 10 years Instituto Butantan herpetarium after have been mostly Maranhão Brazil. Venoms captive wild were similar except small quantitative...
Snake venom metalloproteinases (SVMPs) are major components in most viperid venoms that induce disturbances the hemostatic system and tissues of animals envenomated by snakes. These involved human pathology snake bites appear to be essential for capture digestion snake's prey avoidance predators. SVMPs a versatile family toxins acting on different targets which present distinct structural forms. However, reason why large number expressed some is still unclear. In this study, we evaluated...
Venom is a key adaptive innovation in snakes, and how nonvenom genes were co-opted to become part of the toxin arsenal significant evolutionary question. While this process has been investigated through phylogenetic reconstruction sequences, evidence provided by genomic context remains less explored. To investigate recruitment, we sequenced genome
ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTPurification, Characterization, and Amino Acid Sequence of a Serine Proteinase, PA-BJ, with Platelet-Aggregating Activity from the Venom Bothrops jararacaSolange M. T. Serrano, Reinhardt Mentele, Claudio A. Sampaio, Edwin FinkCite this: Biochemistry 1995, 34, 21, 7186–7193Publication Date (Print):May 30, 1995Publication History Published online1 May 2002Published inissue 30...
Abstract Variation in the snake venom proteome is well documented and it a ubiquitous phenomenon at all taxonomical levels. However, variation peptidome so far not described. In this work we used mass spectrometry [liquid chromatography/mass (LC/MS) matrix‐assisted laser desorption/ionization time‐of‐flight (MALDI‐TOFMS)] to explore sex‐based differences among peptides of eighteen sibling specimens Bothrops jararaca single litter born raised laboratory. MALDI‐TOFMS analyses showed individual...
The pharmacological activities displayed by Bothrops jararaca venom undergo a significant ontogenetic shift. Similarly, the diet of this species changes from ectothermic prey in early life to endothermic adulthood. In study we used large and representative newborn adult samples consisting pools 694 110 specimens, respectively, demonstrate shift proteome complexity B. jararaca. 2-DE coupled MS protein identification showed clear rearrangement toxin arsenal both terms total proteome, as...
Bj-BPP-10c is a bioactive proline-rich decapeptide, part of the C-type natriuretic peptide precursor, expressed in brain and venom gland Bothrops jararaca. We recently showed that displays strong, sustained anti-hypertensive effect spontaneous hypertensive rats (SHR), without causing any normotensive rats, by pharmacological independent angiotensin-converting enzyme inhibition. Therefore, we hypothesized another mechanism should be involved activity. Here used affinity chromatography to...