Solange M T Serrano

Instituto Butantan, San Paulo, São Paulo, Brazil

Are you Solange M T Serrano?

Claim your profile

Publications (105)276.05 Total impact

  • Source
    [Show abstract] [Hide abstract]
    ABSTRACT: Here we present a proteomic characterization of Phoneutria nigriventer venom. A shotgun proteomic approach allowed the identification, for the first time, of O-glycosyl hydrolases (chitinases) in P. nigriventer venom. The electrophoretic profiles under nonreducing and reducing conditions, and protein identification by mass spectrometry, indicated the presence of oligomeric toxin structures in the venom. Complementary proteomic approaches allowed for a qualitative and semi-quantitative profiling of P. nigriventer venom complexity, expanding its known venom proteome diversity.
    Full-text · Article · Jan 2016 · Amino Acids
  • [Show abstract] [Hide abstract]
    ABSTRACT: Plasminogen is a single-chain glycoprotein found in human plasma as the inactive precursor of plasmin. When converted to proteolytically active plasmin, plasmin(ogen) regulates both complement and coagulation cascades, thus representing an important target for pathogenic microorganisms. Leptospira interrogans binds plasminogen, which is converted to active plasmin. Leptospiral immunoglobulin-like (Lig) proteins are surface exposed molecules that interact with extracellular matrix components and complement regulators, including proteins of the FH family and C4BP. In this work, we demonstrate that these multifunctional molecules also bind plasminogen through both N- and C-terminal domains. These interactions are dependent on lysine residues and are affected by ionic strength. Competition assays suggest that plasminogen does not share binding sites with C4BP or FH on Lig proteins at physiological molar ratios. Plasminogen bound to Lig proteins is converted to proteolytic active plasmin in the presence of urokinase-type plasminogen activator (uPA). Lig-bound plasmin is able to cleave the physiological substrates fibrinogen and the complement proteins C3b and C5. Taken together, our data point to a new role of LigA and LigB in leptospiral invasion and complement immune evasion. Plasmin(ogen) acquisition by these versatile proteins may contribute to Leptospira infections, favoring bacterial survival and dissemination inside the host.
    No preview · Article · Jan 2016 · Immunobiology
  • Source
    [Show abstract] [Hide abstract]
    ABSTRACT: Lance-headed snakes are found in Central and South America, and they account for most snakebites in Brazil. The phylogeny of South American pitvipers has been reviewed, and the presence of natural and non-natural hybrids between different species of Bothrops snakes demonstrates that reproductive isolation of several species is still incomplete. The present study aimed to analyze the biological features, particularly the thrombin-like activity, of venoms from hybrids born in captivity, from the mating of a female Bothrops erythromelas and a male Bothrops neuwiedi, two species whose venoms are known to display ontogenetic variation. Proteolytic activity on azocoll and amidolytic activity on N-benzoyl-DL-arginine-p-nitroanilide hydrochloride (BAPNA) were lowest when hybrids were 3 months old, and increased over body growth, reaching values similar to those of the father when hybrids were 12 months old. The clotting activity on plasma diminished as hybrids grew; venoms from 3- and 6-months old hybrids showed low clotting activity on fibrinogen (i.e., thrombin-like activity), like the mother venom, and such activity was detected only when hybrids were older than 1 year of age. Altogether, these results point out that venom features in hybrid snakes are genetically controlled during the ontogenetic development. Despite the presence of the thrombin-like enzyme gene(s) in hybrid snakes, they are silenced during the first six months of life.
    Full-text · Article · Dec 2015 · PLoS ONE
  • Source
    [Show abstract] [Hide abstract]
    ABSTRACT: Comparisons between venoms from snakes kept under captivity or collected at the natural environment are of fundamental importance in order to obtain effective antivenoms to treat human victims of snakebites. In this study, we compared composition and biological activities of Bothrops atrox venom from snakes collected at Tapaj�os National Forest (Par�a State, Brazil) or maintained for more than 10 years under captivity at Instituto Butantan herpetarium after have been collected mostly at Maranh~ao State, Brazil. Venoms from captive or wild snakes were similar except for small quantitative differences detected in peaks correspondent to phospholipases A2 (PLA2), snake venom metalloproteinases (SVMP) class PI and serine proteinases (SVSP), which did not correlate with fibrinolytic and coagulant activities (induced by PI-SVMPs and SVSPs). In both pools, the major toxic component corresponded to PIII-SVMPs, which were isolated and characterized. The characterization by mass spectrometry of both samples identified peptides that matched with a single PIII-SVMP cDNA characterized by transcriptomics, named Batroxrhagin. Sequence alignments show a strong similarity between Batroxrhagin and Jararhagin (96%). Batroxrhagin samples isolated from venoms of wild or captive snakes were not pro-coagulant, but inhibited collagen-induced platelet-aggregation, and induced hemorrhage and fibrin lysis with similar doses. Results suggest that in spite of environmental differences, venom variability was detected only among the less abundant components. In opposition, the most abundant toxin, which is a PIII-SVMP related to the key effects of the venom, is structurally conserved in the venoms. This observation is relevant for explaining the efficacy of antivenoms produced with venoms from captive snakes in human accidents inflicted at distinct natural environments.
    Full-text · Conference Paper · Aug 2015
  • Source
    [Show abstract] [Hide abstract]
    ABSTRACT: Comparisons between venoms from snakes kept under captivity or collected at the natural environment are of fundamental importance in order to obtain effective antivenoms to treat human victims of snakebites. In this study, we compared composition and biological activities of Bothrops atrox venom from snakes collected at Tapajós National Forest (Pará State, Brazil) or maintained for more than 10 years under captivity at Instituto Butantan herpetarium after have been collected mostly at Maranhão State, Brazil. Venoms from captive or wild snakes were similar except for small quantitative differences detected in peaks correspondent to phospholipases A2 (PLA2), snake venom metalloproteinases (SVMP) class PI and serine proteinases (SVSP), which did not correlate with fibrinolytic and coagulant activities (induced by PI-SVMPs and SVSPs). In both pools, the major toxic component corresponded to PIII-SVMPs, which were isolated and characterized. The characterization by mass spectrometry of both samples identified peptides that matched with a single PIII-SVMP cDNA characterized by transcriptomics, named Batroxrhagin. Sequence alignments show a strong similarity between Batroxrhagin and Jararhagin (96%). Batroxrhagin samples isolated from venoms of wild or captive snakes were not pro-coagulant, but inhibited collagen-induced platelet-aggregation, and induced hemorrhage and fibrin lysis with similar doses. Results suggest that in spite of environmental differences, venom variability was detected only among the less abundant components. In opposition, the most abundant toxin, which is a PIII-SVMP related to the key effects of the venom, is structurally conserved in the venoms. This observation is relevant for explaining the efficacy of antivenoms produced with venoms from captive snakes in human accidents inflicted at distinct natural environments. Copyright © 2015. Published by Elsevier B.V.
    Full-text · Article · Aug 2015 · Biochimie
  • Source
    [Show abstract] [Hide abstract]
    ABSTRACT: Comparisons between venoms from snakes kept under captivity or collected at the natural environment are of fundamental importance in order to obtain effective antivenoms to treat human victims of snakebites. In this study, we compared composition and biological activities of Bothrops atrox venom from snakes collected at Tapaj�os National Forest (Par�a State, Brazil) or maintained for more than 10 years under captivity at Instituto Butantan herpetarium after have been collected mostly at Maranh~ao State, Brazil. Venoms from captive or wild snakes were similar except for small quantitative differences detected in peaks correspondent to phospholipases A2 (PLA2), snake venom metalloproteinases (SVMP) class PI and serine proteinases (SVSP), which did not correlate with fibrinolytic and coagulant activities (induced by PI-SVMPs and SVSPs). In both pools, the major toxic component corresponded to PIII-SVMPs, which were isolated and characterized. The characterization by mass spectrometry of both samples identified peptides that matched with a single PIII-SVMP cDNA characterized by transcriptomics, named Batroxrhagin. Sequence alignments show a strong similarity between Batroxrhagin and Jararhagin (96%). Batroxrhagin samples isolated from venoms of wild or captive snakes were not pro-coagulant, but inhibited collagen-induced platelet-aggregation, and induced hemorrhage and fibrin lysis with similar doses. Results suggest that in spite of environmental differences, venom variability was detected only among the less abundant components. In opposition, the most abundant toxin, which is a PIII-SVMP related to the key effects of the venom, is structurally conserved in the venoms. This observation is relevant for explaining the efficacy of antivenoms produced
    Full-text · Article · Aug 2015 · Biochimie
  • Source
    [Show abstract] [Hide abstract]
    ABSTRACT: The snakes from the Bitis genus are some of the most medically important venomous snakes in sub Saharan Africa, however little is known about the composition and effects of these snake venoms peptides. Considering that the victims with Bitis genus snakes have exacerbate hypotension and cardiovascular disorders, we investigated here the presence of angiotensin-converting enzyme modulators on four different species venoms. The peptide fractions from B. g. gabonica, B. nasicornis, B. g. rhinoceros and B. arietans which showed inhibitory activity on angiotensin-converting enzyme were subjected to mass spectrometry analysis. Eight proline-rich peptides were synthetized and their potencies were evaluated in vitro and in vivo. The MS analysis resulted in over 150 sequences, out of which 32 are new proline-rich oligopeptides, and eight were selected for syntheses. For some peptides, inhibition assays showed inhibitory potentials of cleavage of angiotensin I ten times greater when compared to bradykinin. In vivo tests showed that all peptides decreased mean arterial pressure, followed by tachycardia in 6 out of 8 of the tests. We describe here some new and already known proline-rich peptides, also known as bradykinin-potentiating peptides. Four synthetic peptides indicated a preferential inhibition of angiotensin-converting enzyme C-domain. In vivo studies show that the proline-rich oligopeptides are hypotensive molecules GENERAL SIGNIFICANCES: Although proline-rich oligopeptides are known molecules, we present here 32 new sequences that are inhibitors of the angiotensin-converting enzyme and consistent with the symptoms of the victims of Bitis spp, who display severe hypotension. Copyright © 2015. Published by Elsevier B.V.
    Full-text · Article · Feb 2015 · Biochimica et Biophysica Acta (BBA) - General Subjects
  • Source
    [Show abstract] [Hide abstract]
    ABSTRACT: Snake venom metalloproteinases (SVMPs) are major components in most viperid venoms that induce disturbances in the hemostatic system and tissues of animals envenomated by snakes. These disturbances are involved in human pathology of snake bites and appear to be essential for the capture and digestion of snake's prey and avoidance of predators. SVMPs are a versatile family of venom toxins acting on different hemostatic targets which are present in venoms in distinct structural forms. However, the reason why a large number of different SVMPs are expressed in some venoms is still unclear. In this study, we evaluated the interference of five isolated SVMPs in blood coagulation of humans, birds and small rodents. P-III class SVMPs (fractions Ic, IIb and IIc) possess gelatinolytic and hemorrhagic activities, and, of these, two also show fibrinolytic activity. P-I class SVMPs (fractions IVa and IVb) are only fibrinolytic. P-III class SVMPs reduced clotting time of human plasma. Fraction IIc was characterized as prothrombin activator and fraction Ic as factor X activator. In the absence of Ca2+, a firm clot was observed in chicken blood samples with fractions Ic, IIb and partially with fraction IIc. In contrast, without Ca2+, only fraction IIc was able to induce a firm clot in rat blood. In conclusion, functionally distinct forms of SVMPs were found in B. neuwiedi venom that affect distinct mechanisms in the coagulation system of humans, birds and small rodents. Distinct SVMPs appear to be more specialized to rat or chicken blood, strengthening the current hypothesis that toxin diversity enhances the possibilities of the snakes for hunting different prey or evading different predators. This functional diversity also impacts the complexity of human envenoming since different hemostatic mechanisms will be targeted by SVMPs accounting for the complexity of the response of humans to venoms.
    Full-text · Article · Oct 2014 · PLoS ONE
  • [Show abstract] [Hide abstract]
    ABSTRACT: Unlabelled: Many snake venom toxins are serine proteases but their specific in vivo targets are mostly unknown. Various act on components of the coagulation cascade, and fibrinolytic and kallikrein-kinin systems to trigger various pathological effects observed in the envenomation. Despite showing high similarity in terms of primary structure snake venom serine proteinases (SVSPs) show exquisite specificity towards macromolecular substrates. Therefore, the characterization of their peptide bond specificity is important for understanding the active site preference associated with effective proteolysis as well as for the design of peptide substrates and inhibitors. Bothrops jararaca contains various SVSPs among which Bothrops protease A is a specific fibrinogenolytic agent and PA-BJ is a platelet-activating enzyme. In this study we used proteome derived peptide libraries in the Proteomic Identification of protease Cleavage Sites (PICS) approach to explore the peptide bond specificity of Bothrops protease A and PA-BJ in order to determine their individual peptide cleavage sequences. A total of 371 cleavage sites (208 for Bothrops protease A and 163 for PA-BJ) were detected and both proteinases displayed a clear preference for arginine at the P1 position. Moreover, the analysis of the specificity profiles of Bothrops protease A and PA-BJ revealed subtle differences in the preferences along P6-P6', despite a common yet unusual preference for Pro at P2. Taken together, these results map the subsite specificity of both SVSPs and shed light in the functional differences between these proteinases. Biological significance: Proteolysis is key to various pathological effects observed upon envenomation by viperid snakes. The use of the Proteomic Identification of protease Cleavage Sites (PICS) approach for the easy mapping of proteinase subsite preferences at both the prime- and non-prime sides concurrently gives rise to a fresh understanding of the interaction of the snake venom serine proteinases with peptide and macromolecular substrates and indicates that their hydrolytic activity is influenced by the amino acid sequences adjacent to the scissile bond.
    No preview · Article · Oct 2014 · Journal of Proteomics
  • [Show abstract] [Hide abstract]
    ABSTRACT: Accidents caused by scorpions represent a relevant public health issue in Brazil, being more recurring than incidents with snakes and spiders. The main species responsible for this situation is the yellow scorpion, Tityus serrulatus, due especially to the great frequency with which accidents occur and the potential of its venom to induce severe clinical manifestations, even death, mainly among children. Although neurotoxins are well characterized, little information is known about other components of scorpion venoms, such as peptidases, and their effect on envenomation. Previous results from our group showed that the metallopeptidases present in this venom are capable of hydrolyzing the neuropeptide dynorphin 1-13 in vitro, releasing Leu-enkephalin, which may interact with ion channels and promote indirect neurotoxicity. Thus, this study aims to get more information about the effect of toxic peptidase activity present in the venom on biologically active peptides, and to evaluate the in vitro neutralizing potential of commercial antivenoms produced by the Butantan Institute. A set of human bioactive peptides were studied as substrates for the peptidases, and the members of the neuropeptide Y family were found to be the most susceptible ones. All new substrate hydrolyses were totally inhibited by EDTA and not blocked by PMSF, indicating that metallopeptidases were responsible for the peptidase activity. Also, peptidase activities were only partially inhibited by therapeutic Brazilian scorpion antivenom (SAV) and arachnid antivenom (AAV). The dose-response inhibition by both antivenoms indicates that AAV neutralizes better than SAV at the used doses. These characterizations, unpublished until now, can contribute to the improvement of our knowledge about the venom and envenomation processes by T. serrulatus.
    No preview · Article · Sep 2014 · Toxicological Sciences
  • Source
    [Show abstract] [Hide abstract]
    ABSTRACT: Snake venoms contain serine proteinases that are functionally similar to thrombin and specifically cleave fibrinogen to convert it into fibrin or activate platelets to aggregation. PA-BJ is a serine proteinase from Bothrops jararaca venom that promotes platelet aggregation and this effect is mediated by the G-coupled protein receptors PAR1 and PAR4. In this study we describe an improved procedure to obtain PA-BJ from B. jararaca venom that uses less chromatographic steps, and, interestingly, results in the isolation of eight proteoforms showing slightly different pIs and molecular masses due to variations in their glycosylation levels. The identity of the isolated PA-BJ forms (1-8) was confirmed by mass spectrometry, and they showed similar platelet-activating activity on washed platelet suspensions. N- and O-deglycosylation of PA-BJ 1-8 under denaturing conditions generated variable electrophoretic profiles and showed that some forms were resistant to complete deglycosylation. Furthermore, N- and O-deglycosylation under non-denaturing conditions also showed different electrophoretic profiles between the PA-BJ forms and caused partial loss of their ability to cleave a recombinant exodomain of PAR1 receptor. In parallel, three cDNAs encoding PA-BJ-like enzymes were identified by pyrosequencing of a B. jararaca venom gland library constructed with RNA from a single specimen. Taken together, our results suggest that PA-BJ occurs in the B. jararaca venom in multiple proteoforms displaying similar properties upon platelets regardless of their variable isoelectric points, molecular masses, carbohydrate moieties and susceptibility to the activity of glycosidases, and highlight that variability of specific venom components contributes to venom proteome complexity.
    Full-text · Article · Sep 2014 · Biochimica et Biophysica Acta (BBA) - Proteins & Proteomics
  • Source
    [Show abstract] [Hide abstract]
    ABSTRACT: Antivenoms manufactured by bioCSL Limited (Australia) and Instituto Clodomiro Picado (Costa Rica) against the venom of the taipan snakes (Oxyuranus scutellatus) from Australia and Papua New Guinea (PNG), respectively, were compared using antivenomics, an analytical approach that combines proteomics with immunoaffinity chromatography. Both antivenoms recognized all venom proteins present in venom from PNG O. scutellatus, although a pattern of partial recognition was observed for some components. In the case of the Australian O. scutellatus venom, both antivenoms immunorecognized the majority of the components, but the CSL antivenom showed a stronger pattern of immunoreactivity, which was revealed by the percentage of retained proteins in the immunoaffinity column. Antivenoms interacted with taipoxin in surface plasmon resonance. These observations on antivenomics agree with previous neutralization studies.
    Full-text · Article · Aug 2014 · The American journal of tropical medicine and hygiene
  • [Show abstract] [Hide abstract]
    ABSTRACT: Few virulence factors have been identified for Paracoccidioides brasiliensis, the agent of paracoccidioidomycosis. In this study, we quantitatively evaluated the protein composition of P. brasiliensis in the yeast phase using minimal and rich media to obtain a better understanding of its virulence and to gain new insights into pathogen adaptation strategies. This analysis was performed on two isolates of the Pb18 strain showing distinct infection profiles in B10.A mice. Using liquid chromatography/tandem mass spectrometry (LC-MS/MS) analysis, we identified and quantified 316 proteins in minimal medium, 29 of which were overexpressed in virulent Pb18. In rich medium, 29 out of 295 proteins were overexpressed in the virulent fungus. Three proteins were found up-regulated in both media, suggesting potential roles of these proteins in virulence regulation in P. brasiliensis. Moreover, genes up-regulated in virulent Pb18 showed increase in its expression after the recovery of virulence of attenuated Pb18. Proteins up-regulated in both isolates were grouped according to their functional categories. Virulent Pb18 undergoes metabolic reorganization and increased expression of proteins involved in fermentative respiration. This approach allowed us to identify potential virulence regulators and provided a foundation for achieving a molecular understanding of how Paracoccidioides modulates the host-pathogen interaction to its advantage.
    No preview · Article · Aug 2014 · Journal of Proteome Research
  • Source
    [Show abstract] [Hide abstract]
    ABSTRACT: Background / Purpose: The Center of Toxins, Immune-response and Cell Signaling (CeTICS) is an emerging center that studies biochemical, molecular, and cellular mechanisms of toxins that have therapeutic potential. That aims to understand the short-term and long-term behavior of biological systems based on analysis of signaling networks. This is an interdisciplinary project, coupled to the heterogeneous, high-throughput data produced by modern large scale techniques in genomics and proteomics, which implies the necessity of data organization and integration to carry out scientific knowledge. Based on the project goals, we are developing a platform to provide a uniform conceptual schema to minimize -omics data representation. As well as a suitable semantics for interdisciplinary research that allows quantitative and qualitative -omics integrative analyses and mathematical modeling of signaling networks. Main conclusion: The CeTICSdb platform, in its present conceptual database model, allows different integration approaches, construction and simulation of dynamic models based on high-throughput omics data. In addition, it also allows retrieval, storage, management, and integration of experimental and simulated results. Further development of CeTICSdb’ database structure and data integration tools is planned to reduce gaps between behavior of experimental models and virtual simulated models.
    Full-text · Conference Paper · Jul 2014
  • Source
    Solange M. T. Serrano · Ana K. Oliveira · Milene C. Menezes · André Zelanis
    [Show abstract] [Hide abstract]
    ABSTRACT: By catalyzing limited proteolysis or extensive degradation, proteolytic enzymes determine the fate of most proteins in an organism. In the evolutionary process of snake venoms, genes encoding proteinases were tailored to generate potent toxins to target key physiological proteins and thereby play a critical role in prey capture, immobilization and defense against predators. In Bothrops jararaca, metalloproteinases and serine proteinases are among the most abundant toxins both in newborn and adult venoms. In this review, we examine the proteinase-rich venom proteome of B. jararaca and how the proteinases act in a complex and heterogeneous fashion to exert their deleterious local and systemic effects.
    Full-text · Article · Jun 2014 · Toxin Reviews
  • Source
    [Show abstract] [Hide abstract]
    ABSTRACT: Background / Purpose: The Center of Toxins, Immune-response and Cell Signaling (CeTICS) is an emerging center that studies biochemical, molecular, and cellular mechanisms of toxins that have therapeutic potential, aiming to develop proofs of concept based on analyses of molecular signaling networks. Once those studies and analyses involve boundary crossing between Biology, Mathematics, Statistics, and Computer Science, the research developed in CeTICS is intrinsically interdisciplinary. This fact, coupled to the huge amount of data produced by modern high-throughput methods in genomics and proteomics, implies the necessity of data organization and integration to yield scientific knowledge. To this end, we are developing CeTICSdb, a platform to provide a uniform conceptual schema to minimize -omics data representation, as well as a suitable semantics for interdisciplinary research that allows quantitative and qualitative -omics integrative analyses and mathematical modeling of signaling networks. Main conclusion: The CeTICSdb conceptual database model supports high-throughput -omics data and also the management, access and integration of such results. However, further development of the database structure and data integration tools are required to reduce the gap between the experimental models and the actual data representation. Having those requirements properly addressed, a mid-term objective is to make the CeTICSdb platform available to the scientific community as a dry lab, in which high-throughput -omics data could be used to design and validate reaction kinetics models.
    Full-text · Conference Paper · May 2014
  • Source
    [Show abstract] [Hide abstract]
    ABSTRACT: Snake venom metalloproteinases (SVMPs) play important roles in the local and systemic hemorrhage observed upon envenomation. In a previous study on the structural elements important for the activities of HF3 (highly hemorrhagic, P-III-SVMP), bothropasin (hemorrhagic, P-III-SVMP) and BJ-PI (non-hemorrhagic, P-I-SVMP), from Bothrops jararaca, it was demonstrated that they differ in their proteolysis profile of plasma and extracellular matrix proteins. In this study, we evaluated the ability of proteins DM43 and α2-macroglobulin to interfere with the proteolytic activity of these SVMPs on fibrinogen and collagen VI and with their ability to induce hemorrhage. DM43 inhibited the proteolytic activity of bothropasin and BJ-PI but not that of HF3, and was not cleaved the three proteinases. On the other hand, α2-macroglobulin did not inhibit any of the proteinases and was rather cleaved by them. In agreement with these findings, binding analysis showed interaction of bothropasin and BJ-PI but not HF3 to DM43 while none of the proteinases bound to α2-macroglobulin. Moreover, DM43 promoted partial inhibition of the hemorrhagic activity of bothropasin but not that of HF3. Our results demonstrate that metalloproteinases of B. jararaca venom showing different domain composition, glycosylation level and hemorrhagic potency show variable susceptibilities to protein inhibitors.
    Full-text · Article · Jan 2014 · Toxicon

  • No preview · Article · Jan 2014 · Angiogenesis
  • Article: Bothropasin
    [Show abstract] [Hide abstract]
    ABSTRACT: This chapter discusses the structural chemistry and the biological aspects of bothropasin. Bothropasin is active on casein. The pH optimum of the endopeptidase is 8.8 and the assay system includes 4 mM CaCl2. It causes hemorrhage on rabbit skin with a minimum hemorrhagic dose of 1 μg. Bothropasin is an acidic glycoprotein that belongs to class III of reprolysins. This metalloendopeptidase is a medium-sized enzyme of 48 kDa. By sedimentation equilibrium a relative molecular mass of 49,870 was calculated. The native tertiary structure of the protein is dependent on disulfide and metal bonds. In the presence of EDTA, the denatured and reduced protein shows a relative molecular mass of 37,300 by sedimentation equilibrium. MPB presents two protein bands corresponding to MT values of 65,000 and 55,000, which stain with Schiffs reagent. It causes hemorrhage followed by myonecrosis and arterial necrosis after intramuscular injection of doses of 20 μg in mice. Myonecrosis is still observed with lower doses down to 1μg. Doses of 50 ng of jararhagin produce similar lesions. It is found that Bothropasin differs immunologically from hemorrhagic factors isolated from the same venom.
    No preview · Article · Dec 2013
  • Solange M.T. Serrano

    No preview · Article · Dec 2013

Publication Stats

3k Citations
276.05 Total Impact Points

Institutions

  • 1995-2016
    • Instituto Butantan
      • • Laboratório de Bacteriologia
      • • Laboratório de Imunoquímica
      • • Laboratório Especial de Toxinologia Aplicada (LETA)
      • • Laboratório de Bioquímica e Biofísica
      San Paulo, São Paulo, Brazil
  • 2014
    • São Paulo Research Foundation – FAPESP
      San Paulo, São Paulo, Brazil
  • 2011-2012
    • University of São Paulo
      • Department of Biochemistry (IQ)
      San Paulo, São Paulo, Brazil
    • Instituto Adolfo Lutz
      • Divisão de Biologia Médica
      San Paulo, São Paulo, Brazil
  • 2006-2012
    • Instituto Vital Brazil
      SRA, Rio Grande do Sul, Brazil
  • 2007
    • University of Cologne
      Köln, North Rhine-Westphalia, Germany
  • 2003-2005
    • University of Virginia
      • Microbiology, Immunology and Cancer Biology (MIC)
      Charlottesville, Virginia, United States
  • 2001-2005
    • CEP America
      Емеривил, California, United States