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A.R.B. Prieto-Da-Silva
Laboratory of Genetics, Butantan Institute, Sao Paulo 05503-900, Brazil

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Journal article
Published: 30 June 2021 in Toxins
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Osteoclasts (OCs) are important for bone maintenance, calcium balance, and tissue regeneration regulation and are involved in different inflammatory diseases. Our study aimed to evaluate the effect of Bothrops moojeni’s venom and its low and high molecular mass (HMM and LMM) fractions on human peripheral blood mononuclear cell (PBMC)-derived OCs’ in vitro differentiation. Bothrops moojeni, a Brazilian lanced-head viper, presents a rich but not well-explored, venom composition. This venom is a potent inducer of inflammation, which can be used as a tool to investigate the inflammatory process. Human PBMCs were isolated and induced to OC differentiation following routine protocol. On the fourth day of differentiation, the venom was added at different concentrations (5, 0.5, and 0.05 µg/mL). We observed a significant reduction of TRAP+ (tartrate-resistant acid phosphatase) OCs at the concentration of 5 µg/mL. We evaluated the F-actin-rich OCs structure’s integrity; disruption of its integrity reflects bone adsorption capacity. F-actin rings phalloidin staining demonstrated that venom provoked their disruption in treated OCs. HMM, fraction reduces TRAP+ OCs at a concentration of 5 µg/mL and LMM fraction at 1 µg/mL, respectively. Our results indicate morphological changes that the venom induced cause in OCs. We analyzed the pattern of soluble proteins found in the conditioned cell culture medium OCs treated with venom and its fractions using mass spectrometry (LC-MS/IT-Tof). The proteomic analyses indicate the possible pathways and molecular mechanisms involved in OC reduction after the treatment.

ACS Style

Fernanda D’Amélio; Hugo Vigerelli; Álvaro Prieto-Da-Silva; Eduardo Osório Frare; Isabel Batista; Daniel Pimenta; Irina Kerkis. Bothrops moojeni Venom and Its Components Strongly Affect Osteoclasts’ Maturation and Protein Patterns. Toxins 2021, 13, 459 .

AMA Style

Fernanda D’Amélio, Hugo Vigerelli, Álvaro Prieto-Da-Silva, Eduardo Osório Frare, Isabel Batista, Daniel Pimenta, Irina Kerkis. Bothrops moojeni Venom and Its Components Strongly Affect Osteoclasts’ Maturation and Protein Patterns. Toxins. 2021; 13 (7):459.

Chicago/Turabian Style

Fernanda D’Amélio; Hugo Vigerelli; Álvaro Prieto-Da-Silva; Eduardo Osório Frare; Isabel Batista; Daniel Pimenta; Irina Kerkis. 2021. "Bothrops moojeni Venom and Its Components Strongly Affect Osteoclasts’ Maturation and Protein Patterns." Toxins 13, no. 7: 459.

Journal article
Published: 29 July 2019 in Toxins
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Ant species have specialized venom systems developed to sting and inoculate a biological cocktail of organic compounds, including peptide and polypeptide toxins, for the purpose of predation and defense. The genus Dinoponera comprises predatory giant ants that inoculate venom capable of causing long-lasting local pain, involuntary shaking, lymphadenopathy, and cardiac arrhythmias, among other symptoms. To deepen our knowledge about venom composition with regard to protein toxins and their roles in the chemical–ecological relationship and human health, we performed a bottom-up proteomics analysis of the crude venom of the giant ant D. quadriceps, popularly known as the “false” tocandiras. For this purpose, we used two different analytical approaches: (i) gel-based proteomics approach, wherein the crude venom was resolved by denaturing sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and all protein bands were excised for analysis; (ii) solution-based proteomics approach, wherein the crude venom protein components were directly fragmented into tryptic peptides in solution for analysis. The proteomic data that resulted from these two methodologies were compared against a previously annotated transcriptomic database of D. quadriceps, and subsequently, a homology search was performed for all identified transcript products. The gel-based proteomics approach unequivocally identified nine toxins of high molecular mass in the venom, as for example, enzymes [hyaluronidase, phospholipase A1, dipeptidyl peptidase and glucose dehydrogenase/flavin adenine dinucleotide (FAD) quinone] and diverse venom allergens (homologous of the red fire ant Selenopsis invicta) and venom-related proteins (major royal jelly-like). Moreover, the solution-based proteomics revealed and confirmed the presence of several hydrolases, oxidoreductases, proteases, Kunitz-like polypeptides, and the less abundant inhibitor cysteine knot (ICK)-like (knottin) neurotoxins and insect defensin. Our results showed that the major components of the D. quadriceps venom are toxins that are highly likely to damage cell membranes and tissue, to cause neurotoxicity, and to induce allergic reactions, thus, expanding the knowledge about D. quadriceps venom composition and its potential biological effects on prey and victims.

ACS Style

Douglas Oscar Ceolin Mariano; Úrsula Castro De Oliveira; André Junqueira Zaharenko; Daniel Carvalho Pimenta; Gandhi Rádis-Baptista; Álvaro Rossan De Brandão Prieto-Da-Silva. Bottom-Up Proteomic Analysis of Polypeptide Venom Components of the Giant Ant Dinoponera Quadriceps. Toxins 2019, 11, 448 .

AMA Style

Douglas Oscar Ceolin Mariano, Úrsula Castro De Oliveira, André Junqueira Zaharenko, Daniel Carvalho Pimenta, Gandhi Rádis-Baptista, Álvaro Rossan De Brandão Prieto-Da-Silva. Bottom-Up Proteomic Analysis of Polypeptide Venom Components of the Giant Ant Dinoponera Quadriceps. Toxins. 2019; 11 (8):448.

Chicago/Turabian Style

Douglas Oscar Ceolin Mariano; Úrsula Castro De Oliveira; André Junqueira Zaharenko; Daniel Carvalho Pimenta; Gandhi Rádis-Baptista; Álvaro Rossan De Brandão Prieto-Da-Silva. 2019. "Bottom-Up Proteomic Analysis of Polypeptide Venom Components of the Giant Ant Dinoponera Quadriceps." Toxins 11, no. 8: 448.

Journal article
Published: 20 April 2018 in Molecules
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Crotamine is a highly cationic; cysteine rich, cross-linked, low molecular mass cell penetrating peptide (CPP) from the venom of the South American rattlesnake. Potential application of crotamine in biomedicine may require its large-scale purification. To overcome difficulties related with the purification of natural crotamine (nCrot) we aimed in the present study to synthesize and characterize a crotamine analog (sCrot) as well investigate its CPP activity. Mass spectrometry analysis demonstrates that sCrot and nCrot have equal molecular mass and biological function—the capacity to induce spastic paralysis in the hind limbs in mice. sCrot CPP activity was evaluated in a wide range of tumor and non-tumor cell tests performed at different time points. We demonstrate that sCrot-Cy3 showed distinct co-localization patterns with intracellular membranes inside the tumor and non-tumor cells. Time-lapse microscopy and quantification of sCrot-Cy3 fluorescence signalss in living tumor versus non-tumor cells revealed a significant statistical difference in the fluorescence intensity observed in tumor cells. These data suggest a possible use of sCrot as a molecular probe for tumor cells, as well as, for the selective delivery of anticancer molecules into these tumors.

ACS Style

Nicole Caroline Mambelli-Lisboa; Juliana Mozer Sciani; Alvaro Rossan Brandão Prieto Da Silva; Irina Kerkis. Co-Localization of Crotamine with Internal Membranes and Accentuated Accumulation in Tumor Cells. Molecules 2018, 23, 968 .

AMA Style

Nicole Caroline Mambelli-Lisboa, Juliana Mozer Sciani, Alvaro Rossan Brandão Prieto Da Silva, Irina Kerkis. Co-Localization of Crotamine with Internal Membranes and Accentuated Accumulation in Tumor Cells. Molecules. 2018; 23 (4):968.

Chicago/Turabian Style

Nicole Caroline Mambelli-Lisboa; Juliana Mozer Sciani; Alvaro Rossan Brandão Prieto Da Silva; Irina Kerkis. 2018. "Co-Localization of Crotamine with Internal Membranes and Accentuated Accumulation in Tumor Cells." Molecules 23, no. 4: 968.

Research article
Published: 20 October 2014 in PLOS ONE
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We propose the technique of biogeochemical typing (BGC typing) as a novel methodology to set forth the sub-systems of organismal communities associated to the correlated chemical profiles working within a larger complex environment. Given the intricate characteristic of both organismal and chemical consortia inherent to the nature, many environmental studies employ the holistic approach of multi-omics analyses undermining as much information as possible. Due to the massive amount of data produced applying multi-omics analyses, the results are hard to visualize and to process. The BGC typing analysis is a pipeline built using integrative statistical analysis that can treat such huge datasets filtering, organizing and framing the information based on the strength of the various mutual trends of the organismal and chemical fluctuations occurring simultaneously in the environment. To test our technique of BGC typing, we choose a rich environment abounding in chemical nutrients and organismal diversity: the surficial freshwater from Japanese paddy fields and surrounding waters. To identify the community consortia profile we employed metagenomics as high throughput sequencing (HTS) for the fragments amplified from Archaea rRNA, universal 16S rRNA and 18S rRNA; to assess the elemental content we employed ionomics by inductively coupled plasma optical emission spectroscopy (ICP-OES); and for the organic chemical profile, metabolomics employing both Fourier transformed infrared (FT-IR) spectroscopy and proton nuclear magnetic resonance (1H-NMR) all these analyses comprised our multi-omics dataset. The similar trends between the community consortia against the chemical profiles were connected through correlation. The result was then filtered, organized and framed according to correlation strengths and peculiarities. The output gave us four BGC types displaying uniqueness in community and chemical distribution, diversity and richness. We conclude therefore that the BGC typing is a successful technique for elucidating the sub-systems of organismal communities with associated chemical profiles in complex ecosystems.

ACS Style

Diogo M. O. Ogawa; Shigeharu Moriya; Yuuri Tsuboi; Yasuhiro Date; Alvaro Prieto; Gandhi Rádis-Baptista; Tetsuo Yamane; Jun Kikuchi. Biogeochemical Typing of Paddy Field by a Data-Driven Approach Revealing Sub-Systems within a Complex Environment - A Pipeline to Filtrate, Organize and Frame Massive Dataset from Multi-Omics Analyses. PLOS ONE 2014, 9, e110723 .

AMA Style

Diogo M. O. Ogawa, Shigeharu Moriya, Yuuri Tsuboi, Yasuhiro Date, Alvaro Prieto, Gandhi Rádis-Baptista, Tetsuo Yamane, Jun Kikuchi. Biogeochemical Typing of Paddy Field by a Data-Driven Approach Revealing Sub-Systems within a Complex Environment - A Pipeline to Filtrate, Organize and Frame Massive Dataset from Multi-Omics Analyses. PLOS ONE. 2014; 9 (10):e110723.

Chicago/Turabian Style

Diogo M. O. Ogawa; Shigeharu Moriya; Yuuri Tsuboi; Yasuhiro Date; Alvaro Prieto; Gandhi Rádis-Baptista; Tetsuo Yamane; Jun Kikuchi. 2014. "Biogeochemical Typing of Paddy Field by a Data-Driven Approach Revealing Sub-Systems within a Complex Environment - A Pipeline to Filtrate, Organize and Frame Massive Dataset from Multi-Omics Analyses." PLOS ONE 9, no. 10: e110723.

Journal article
Published: 14 August 2014 in Cell Death & Disease
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Endostatin (ES) inhibits angiogenesis, reducing tumor growth in animal models. However, it has low therapeutic effect in human clinical trials. BAX is a member of the BCL-2 family of proteins; its proapoptotic (BH3) domain interacts with other members of the family in the cytoplasm, to induce apoptosis. Here, we fused the BAX BH3 domain with murine ES, to enhance ES potency. Endothelial cells specifically internalize the fusion protein ES-BAX. The presence of the BAX domain enhances endothelial cell death by apoptosis by 1.8-fold and diminishes microvessel outgrowth in the rat aortic ring assay by 6.5-fold. Daily injections of 15 μg of ES-BAX/g in tumor-bearing mice reduce tumor weight by 86.9% as compared with ES-treated animals. Co-immunoprecipitation assays confirmed that ES-BAX interacts with members of the BCL-2 family. Also, ES interacts with BCL-2, BCL-XL, and BAK in endothelial cell lysates, suggesting a potential new mechanism for the apoptosis induction by ES. The superiority of the ES-BAX antiangiogenic effect indicates that this fusion protein could be a promising therapeutic alternative to treat cancer.

ACS Style

Rosa M Churachambi; Maria Helena Bellini; Jacqueline F Jacysyn; Luciana Andrade; L P Medina; Alvaro Prieto; Gustavo P. Amarante-Mendes; Ligia Morganti. Improving the therapeutic potential of endostatin by fusing it with the BAX BH3 death domain. Cell Death & Disease 2014, 5, e1371 -e1371.

AMA Style

Rosa M Churachambi, Maria Helena Bellini, Jacqueline F Jacysyn, Luciana Andrade, L P Medina, Alvaro Prieto, Gustavo P. Amarante-Mendes, Ligia Morganti. Improving the therapeutic potential of endostatin by fusing it with the BAX BH3 death domain. Cell Death & Disease. 2014; 5 (8):e1371-e1371.

Chicago/Turabian Style

Rosa M Churachambi; Maria Helena Bellini; Jacqueline F Jacysyn; Luciana Andrade; L P Medina; Alvaro Prieto; Gustavo P. Amarante-Mendes; Ligia Morganti. 2014. "Improving the therapeutic potential of endostatin by fusing it with the BAX BH3 death domain." Cell Death & Disease 5, no. 8: e1371-e1371.

Research article
Published: 31 January 2014 in PLOS ONE
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Dinoponera quadriceps is a predatory giant ant that inhabits the Neotropical region and subdues its prey (insects) with stings that deliver a toxic cocktail of molecules. Human accidents occasionally occur and cause local pain and systemic symptoms. A comprehensive study of the D. quadriceps venom gland transcriptome is required to advance our knowledge about the toxin repertoire of the giant ant venom and to understand the physiopathological basis of Hymenoptera envenomation. We conducted a transcriptome analysis of a cDNA library from the D. quadriceps venom gland with Sanger sequencing in combination with whole-transcriptome shotgun deep sequencing. From the cDNA library, a total of 420 independent clones were analyzed. Although the proportion of dinoponeratoxin isoform precursors was high, the first giant ant venom inhibitor cysteine-knot (ICK) toxin was found. The deep next generation sequencing yielded a total of 2,514,767 raw reads that were assembled into 18,546 contigs. A BLAST search of the assembled contigs against non-redundant and Swiss-Prot databases showed that 6,463 contigs corresponded to BLASTx hits and indicated an interesting diversity of transcripts related to venom gene expression. The majority of these venom-related sequences code for a major polypeptide core, which comprises venom allergens, lethal-like proteins and esterases, and a minor peptide framework composed of inter-specific structurally conserved cysteine-rich toxins. Both the cDNA library and deep sequencing yielded large proportions of contigs that showed no similarities with known sequences. To our knowledge, this is the first report of the venom gland transcriptome of the New World giant ant D. quadriceps. The glandular venom system was dissected, and the toxin arsenal was revealed; this process brought to light novel sequences that included an ICK-folded toxins, allergen proteins, esterases (phospholipases and carboxylesterases), and lethal-like toxins. These findings contribute to the understanding of the ecology, behavior and venomics of hymenopterans.

ACS Style

Alba F. C. Torres; Chen Huang; Cheong-Meng Chong; Siu Wai Leung; Alvaro Prieto; Alexandre Havt; Yves P. Quinet; Alice M. C. Martins; Simon M. Y. Lee; Gandhi Rádis-Baptista. Transcriptome Analysis in Venom Gland of the Predatory Giant Ant Dinoponera quadriceps: Insights into the Polypeptide Toxin Arsenal of Hymenopterans. PLOS ONE 2014, 9, e87556 .

AMA Style

Alba F. C. Torres, Chen Huang, Cheong-Meng Chong, Siu Wai Leung, Alvaro Prieto, Alexandre Havt, Yves P. Quinet, Alice M. C. Martins, Simon M. Y. Lee, Gandhi Rádis-Baptista. Transcriptome Analysis in Venom Gland of the Predatory Giant Ant Dinoponera quadriceps: Insights into the Polypeptide Toxin Arsenal of Hymenopterans. PLOS ONE. 2014; 9 (1):e87556.

Chicago/Turabian Style

Alba F. C. Torres; Chen Huang; Cheong-Meng Chong; Siu Wai Leung; Alvaro Prieto; Alexandre Havt; Yves P. Quinet; Alice M. C. Martins; Simon M. Y. Lee; Gandhi Rádis-Baptista. 2014. "Transcriptome Analysis in Venom Gland of the Predatory Giant Ant Dinoponera quadriceps: Insights into the Polypeptide Toxin Arsenal of Hymenopterans." PLOS ONE 9, no. 1: e87556.

Journal article
Published: 01 August 2012 in Toxicon
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ACS Style

Poliana G. Corrêa; Taís Machado; Valdir J. Germano; Daniela P.T. Gennari; Álvaro R.B. Prieto-Da-Silva; Nancy Oguiura. 66. β-defensin-like genes in Brazilian Poisonous Snakes. Toxicon 2012, 60, 127 .

AMA Style

Poliana G. Corrêa, Taís Machado, Valdir J. Germano, Daniela P.T. Gennari, Álvaro R.B. Prieto-Da-Silva, Nancy Oguiura. 66. β-defensin-like genes in Brazilian Poisonous Snakes. Toxicon. 2012; 60 (2):127.

Chicago/Turabian Style

Poliana G. Corrêa; Taís Machado; Valdir J. Germano; Daniela P.T. Gennari; Álvaro R.B. Prieto-Da-Silva; Nancy Oguiura. 2012. "66. β-defensin-like genes in Brazilian Poisonous Snakes." Toxicon 60, no. 2: 127.

Journal article
Published: 31 August 2009 in Toxicon
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Gyroxin is one of main serine proteases of Crotalus durissus terrificus venom, representing about 2% of the protein content in the crude venom. It is a 33 kDa glycoprotein with 3.8% by weight of sugar moiety. This toxin induces hemotoxicity in mice and a neurological condition called barrel rotation syndrome. In the present work, we report the molecular cloning of five new nucleotide sequences from a cDNA library of the venom glands of a single specimen of C. d. terrificus. These sequences have been analyzed in silico with respect to their cDNA organization and similarity with other snake venom serine proteases (SVSPs). We also describe a rapid and efficient method for screening vectors for mammalian cell expression, based on the fact that SVSPs are difficult-to-express toxins due to the presence of several disulfide bonds and glycosylation in their structures. Thus, one of the Gyroxin cDNAs was subcloned into pSectag2 HygroA and pED vectors and used to transfect COS-7 cells. Expression of the functional recombinant Gyroxin isoform was achieved with this cell line with esterase activity in the conditioned culture medium, as revealed by immunoblot of secreted protein and standard anti-crotalic serum from Butantan Institute.

ACS Style

C.M. Yonamine; A.R.B. Prieto-Da-Silva; G.S. Magalhães; G. Rádis-Baptista; L. Morganti; F.C. Ambiel; R.M. Chura-Chambi; T. Yamane; M.A.P. Camillo. Cloning of serine protease cDNAs from Crotalus durissus terrificus venom gland and expression of a functional Gyroxin homologue in COS-7 cells. Toxicon 2009, 54, 110 -120.

AMA Style

C.M. Yonamine, A.R.B. Prieto-Da-Silva, G.S. Magalhães, G. Rádis-Baptista, L. Morganti, F.C. Ambiel, R.M. Chura-Chambi, T. Yamane, M.A.P. Camillo. Cloning of serine protease cDNAs from Crotalus durissus terrificus venom gland and expression of a functional Gyroxin homologue in COS-7 cells. Toxicon. 2009; 54 (2):110-120.

Chicago/Turabian Style

C.M. Yonamine; A.R.B. Prieto-Da-Silva; G.S. Magalhães; G. Rádis-Baptista; L. Morganti; F.C. Ambiel; R.M. Chura-Chambi; T. Yamane; M.A.P. Camillo. 2009. "Cloning of serine protease cDNAs from Crotalus durissus terrificus venom gland and expression of a functional Gyroxin homologue in COS-7 cells." Toxicon 54, no. 2: 110-120.

Journal article
Published: 15 December 2008 in Toxicon
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Snake venom metalloproteases encompass a large family of toxins, with approximately 200 members already catalogued, which exhibit a diversity of structures and biological functions. From this relatively large number, only a dozen examples of apoptosis-inducing metalloproteases, like VAP1 and 2 from the venom of Crotalus atrox, are known. Since most VAP1-like toxins ever characterized were purified from the venom of Viperidae species inhabiting diverse places on earth, we investigate the expression of VAP-like metalloproteases in the venom gland of three representative pit vipers of the Brazilian territory. By molecular cloning and quantitative real-time polymerase chain reaction, using as calibrator gene the Crotalus durissus terrificus homolog of VAP1, named crotastatin, it is reported here that VAP1/crotastatin-like homologues in the venom gland of Bothrops atrox, C. d. cascavella and Lachesis m. rhombeata are expressed at different levels. Hence, batroxstatins, the crotastatin-like precursors from B. atrox, are expressed 87 times more than crotastatin-1, from C. d. cascavella, and 7.5-fold that lachestatins, from L. m. rhombeata. Moreover, in silico structural analysis of amino acid sequences indicates that batroxstatin-2, crotastatins and lachestatin-1 and -2 which share the archetypal motifs and metal- binding sites of VAP1, are subgrouped in a branch that comprises some apoptosis-inducing toxins.

ACS Style

N.A.C. Tavares; J.M. Correia; M.C. Guarnieri; J.L. Lima-Filho; Alvaro Prieto; Gandhi Radis-Baptista. Expression of mRNAs coding for VAP1/crotastatin-like metalloproteases in the venom glands of three South American pit vipers assessed by quantitative real-time PCR. Toxicon 2008, 52, 897 -907.

AMA Style

N.A.C. Tavares, J.M. Correia, M.C. Guarnieri, J.L. Lima-Filho, Alvaro Prieto, Gandhi Radis-Baptista. Expression of mRNAs coding for VAP1/crotastatin-like metalloproteases in the venom glands of three South American pit vipers assessed by quantitative real-time PCR. Toxicon. 2008; 52 (8):897-907.

Chicago/Turabian Style

N.A.C. Tavares; J.M. Correia; M.C. Guarnieri; J.L. Lima-Filho; Alvaro Prieto; Gandhi Radis-Baptista. 2008. "Expression of mRNAs coding for VAP1/crotastatin-like metalloproteases in the venom glands of three South American pit vipers assessed by quantitative real-time PCR." Toxicon 52, no. 8: 897-907.