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Celebrating 120 Years of Butantan Institute Contributions for Toxinology
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Celebrating 120 Years of Butantan Institute Contributions for Toxinology

A special issue of Toxins (ISSN 2072-6651). This special issue belongs to the section "Animal Venoms".

Deadline for manuscript submissions: closed (15 October 2021) | Viewed by 69722

Printed Edition Available!
A printed edition of this Special Issue is available here.

Special Issue Editor

Dr. Ana Maria Moura-Da-Silva

E-Mail Website
Guest Editor
Laboratório de Imunopatologia, Instituto Butantan, São Paulo 05503-900, Brazil
Interests: snake venoms; metalloproteinases; hemostasis; venom composition; venom variability; antivenoms; immunoassays
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

The Butantan Institute was founded by the Brazilian physician and scientist Vital Brazil in 1901, combining, in the same institution, medical research and the transfer of results to society in the form of health products. More than a century after its foundation, Butantan is today an outstanding biomedical research center, which integrates basic research, technological development, production of immunobiologicals, and technical and scientific dissemination, seeking the permanent contribution to Public Health systems. When celebrating Butantan's 120th anniversary, we acknowledge its international relevance and continuous contributions to Toxinology. Butantan houses one of the largest collections of venomous animals in the world, its scientists are involved in countless studies on the characterization of the composition of venoms, mechanisms of action of toxins, and the use of toxins as lead molecules for drug development. The Butantan Institute also operates the "Hospital Vital Brazil", which is specialized in accidents involving venomous animals and is one of the most renowned antivenom producers. This Special Issue of Toxins celebrates the 120th anniversary of the Butantan Institute in recognition of its contribution to global Toxinology and control of neglected tropical diseases. To attend to these goals, we aim to include in this Special Issue recent and advanced contributions to the knowledge of plant, microorganisms, and animal venom toxins. The subjects include toxins characterization, evolution, and mechanisms of action, the venomous animals and toxic plants or microorganisms, highlighting human accidents and antivenoms.

Dr. Ana M. Moura-da-Silva
Guest Editor

Manuscript Submission Information

Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All submissions that pass pre-check are peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.

Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a double-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. Toxins is an international peer-reviewed open access monthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. The Article Processing Charge (APC) for publication in this open access journal is 2700 CHF (Swiss Francs). Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.

Keywords

  • Venom composition and evolution
  • Plant and microbial toxins
  • Mechanism of action of venom toxins
  • Human accidents
  • Antivenoms
  • Venomous animals
  • Toxins and drug development

Published Papers (23 papers)

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Editorial

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2 pages, 212 KiB  
Editorial
Celebrating 120 Years of Butantan Institute Contributions for Toxinology
by Ana M. Moura-da-Silva
Toxins 2022, 14(2), 76; https://0-doi-org.brum.beds.ac.uk/10.3390/toxins14020076 - 21 Jan 2022
Viewed by 1907
Abstract
A hundred and twenty years ago, the Butantan Institute was founded by the Brazilian physician and scientist Vital Brazil, combining, in the same institution, medical research, and the transfer of results to society in the form of health products [...] Full article
(This article belongs to the Special Issue Celebrating 120 Years of Butantan Institute Contributions for Toxinology)

Research

Jump to: Editorial, Review

18 pages, 9470 KiB  
Article
Molecular Characterization and Functional Analysis of the Nattectin-like Toxin from the Venomous Fish Thalassophryne maculosa
by Monica Lopes-Ferreira, Ines Sosa-Rosales, Pedro Ismael Silva Junior, Katia Conceicao, Adolfo Luis Almeida Maleski, Leticia Balan-Lima, Geonildo Rodrigo Disner and Carla Lima
Toxins 2022, 14(1), 2; https://0-doi-org.brum.beds.ac.uk/10.3390/toxins14010002 - 21 Dec 2021
Cited by 4 | Viewed by 2794
Abstract
TmC4-47.2 is a toxin with myotoxic activity found in the venom of Thalassophryne maculosa, a venomous fish commonly found in Latin America whose envenomation produces an injury characterized by delayed neutrophil migration, production of major pro-inflammatory cytokines, and necrosis at the wound [...] Read more.
TmC4-47.2 is a toxin with myotoxic activity found in the venom of Thalassophryne maculosa, a venomous fish commonly found in Latin America whose envenomation produces an injury characterized by delayed neutrophil migration, production of major pro-inflammatory cytokines, and necrosis at the wound site, as well as a specific systemic immune response. However, there are few studies on the protein structure and functions associated with it. Here, the toxin was identified from the crude venom by chromatography and protein purification systems. TmC4-47.2 shows high homology with the Nattectin from Thalassophryne nattereri venom, with 6 cysteines and QPD domain for binding to galactose. We confirm its hemagglutinating and microbicide abilities independent of carbohydrate binding, supporting its classification as a nattectin-like lectin. After performing the characterization of TmC4-47.2, we verified its ability to induce an increase in the rolling and adherence of leukocytes in cremaster post-capillary venules dependent on the α5β1 integrin. Finally, we could observe the inflammatory activity of TmC4-47.2 through the production of IL-6 and eotaxin in the peritoneal cavity with sustained recruitment of eosinophils and neutrophils up to 24 h. Together, our study characterized a nattectin-like protein from T. maculosa, pointing to its role as a molecule involved in the carbohydrate-independent agglutination response and modulation of eosinophilic and neutrophilic inflammation. Full article
(This article belongs to the Special Issue Celebrating 120 Years of Butantan Institute Contributions for Toxinology)
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14 pages, 871 KiB  
Article
Antimicrobial Activity of Snake β-Defensins and Derived Peptides
by Nancy Oguiura, Poliana Garcia Corrêa, Isabella Lemos Rosmino, Ana Olívia de Souza and Kerly Fernanda Mesquita Pasqualoto
Toxins 2022, 14(1), 1; https://0-doi-org.brum.beds.ac.uk/10.3390/toxins14010001 - 21 Dec 2021
Cited by 5 | Viewed by 3295
Abstract
β-defensins are antimicrobial peptides presenting in vertebrate animals. They participate in innate immunity, but little is known about them in reptiles, including snakes. Although several β-defensin genes were described in Brazilian snakes, their function is still unknown. The peptide sequence from these genes [...] Read more.
β-defensins are antimicrobial peptides presenting in vertebrate animals. They participate in innate immunity, but little is known about them in reptiles, including snakes. Although several β-defensin genes were described in Brazilian snakes, their function is still unknown. The peptide sequence from these genes was deduced, and synthetic peptides (with approximately 40 amino acids and derived peptides) were tested against pathogenic bacteria and fungi using microbroth dilution assays. The linear peptides, derived from β-defensins, were designed applying the bioisosterism strategy. The linear β-defensins were more active against Escherichia coli, Micrococcus luteus, Citrobacter freundii, and Staphylococcus aureus. The derived peptides (7–14 mer) showed antibacterial activity against those bacteria and on Klebsiella pneumoniae. Nonetheless, they did not present activity against Candida albicans, Cryptococcus neoformans, Trychophyton rubrum, and Aspergillus fumigatus showing that the cysteine substitution to serine is deleterious to antifungal properties. Tryptophan residue showed to be necessary to improve antibacterial activity. Even though the studied snake β-defensins do not have high antimicrobial activity, they proved to be attractive as template molecules for the development of antibiotics. Full article
(This article belongs to the Special Issue Celebrating 120 Years of Butantan Institute Contributions for Toxinology)
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24 pages, 43533 KiB  
Article
rDromaserpin: A Novel Anti-Hemostatic Serpin, from the Salivary Glands of the Hard Tick Hyalomma dromedarii
by Hajer Aounallah, Melissa Regina Fessel, Mauricio Barbugiani Goldfeder, Eneas Carvalho, Chaima Bensaoud, Ana Marisa Chudzinski-Tavassi, Ali Bouattour, Youmna M’ghirbi and Fernanda Faria
Toxins 2021, 13(12), 913; https://0-doi-org.brum.beds.ac.uk/10.3390/toxins13120913 - 20 Dec 2021
Cited by 6 | Viewed by 3317
Abstract
Hemostatic disorders are caused either by platelet-related dysfunctions, defective blood coagulation, or by a combination of both, leading to an increased susceptibility to cardiovascular diseases (CVD) and other related illnesses. The unique specificity of anticoagulants from hematophagous arthropods, such as ticks, suggests that [...] Read more.
Hemostatic disorders are caused either by platelet-related dysfunctions, defective blood coagulation, or by a combination of both, leading to an increased susceptibility to cardiovascular diseases (CVD) and other related illnesses. The unique specificity of anticoagulants from hematophagous arthropods, such as ticks, suggests that tick saliva holds great promise for discovering new treatments for these life-threatening diseases. In this study, we combined in silico and in vitro analyses to characterize the first recombinant serpin, herein called Dromaserpin, from the sialotranscriptome of the Hyalomma dromedarii tick. Our in silico data described Dromaserpin as a secreted protein of ~43 kDa with high similarities to previously characterized inhibitory serpins. The recombinant protein (rDromaserpin) was obtained as a well-structured monomer, which was tested using global blood coagulation and platelet aggregation assays. With this approach, we confirmed rDromaserpin anticoagulant activity as it significantly delayed plasma clotting in activated partial thromboplastin time and thrombin time assays. The profiling of proteolytic activity shows its capacity to inhibit thrombin in the micromolar range (0.2 to 1 μM) and in the presence of heparin this inhibition was clearly increased. It was also able to inhibit Kallikrein, FXIa and slightly FXIIa, with no significant effect on other factors. In addition, the rDromaserpin inhibited thrombin-induced platelet aggregation. Taken together, our data suggest that rDromaserpin deserves to be further investigated as a potential candidate for developing therapeutic compounds targeting disorders related to blood clotting and/or platelet aggregation. Full article
(This article belongs to the Special Issue Celebrating 120 Years of Butantan Institute Contributions for Toxinology)
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10 pages, 2569 KiB  
Article
PKCζ-Mitogen-Activated Protein Kinase Signaling Mediates Crotalphine-Induced Antinociception
by Bárbara G. de Freitas, Natália G. Hösch, Leandro M. Pereira, Tereza C. Barbosa, Gisele Picolo, Yara Cury and Vanessa O. Zambelli
Toxins 2021, 13(12), 912; https://0-doi-org.brum.beds.ac.uk/10.3390/toxins13120912 - 20 Dec 2021
Cited by 4 | Viewed by 2342
Abstract
Crotalphine (CRP) is a structural analogue to a peptide that was first identified in the crude venom from the South American rattlesnake Crotalus durissus terrificus. This peptide induces a potent and long-lasting antinociceptive effect that is mediated by the activation of peripheral [...] Read more.
Crotalphine (CRP) is a structural analogue to a peptide that was first identified in the crude venom from the South American rattlesnake Crotalus durissus terrificus. This peptide induces a potent and long-lasting antinociceptive effect that is mediated by the activation of peripheral opioid receptors. The opioid receptor activation regulates a variety of intracellular signaling, including the mitogen-activated protein kinase (MAPK) pathway. Using primary cultures of sensory neurons, it was demonstrated that crotalphine increases the level of activated ERK1/2 and JNK-MAPKs and this increase is dependent on the activation of protein kinase Cζ (PKCζ). However, whether PKCζ-MAPK signaling is critical for crotalphine-induced antinociception is unknown. Here, we biochemically demonstrated that the systemic crotalphine activates ERK1/2 and JNK and decreases the phosphorylation of p38 in the lumbar spinal cord. The in vivo pharmacological inhibition of spinal ERK1/2 and JNK, but not of p38, blocks the antinociceptive effect of crotalphine. Of interest, the administration of a PKCζ pseudosubstrate (PKCζ inhibitor) prevents crotalphine-induced ERK activation in the spinal cord, followed by the abolishment of crotalphine-induced analgesia. Together, our results demonstrate that the PKCζ-ERK signaling pathway is involved in crotalphine-induced analgesia. Our study opens a perspective for the PKCζ-MAPK axis as a target for pain control. Full article
(This article belongs to the Special Issue Celebrating 120 Years of Butantan Institute Contributions for Toxinology)
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18 pages, 3089 KiB  
Article
Bitis arietans Snake Venom and Kn-Ba, a Snake Venom Serine Protease, Induce the Production of Inflammatory Mediators in THP-1 Macrophages
by Ângela Alice Amadeu Megale, Fabio Carlos Magnoli, Felipe Raimondi Guidolin, Kemily Stephanie Godoi, Fernanda Calheta Vieira Portaro and Wilmar Dias-da-Silva
Toxins 2021, 13(12), 906; https://0-doi-org.brum.beds.ac.uk/10.3390/toxins13120906 - 16 Dec 2021
Cited by 5 | Viewed by 2438
Abstract
Bitis arietans is a snake of medical importance found throughout sub-Saharan Africa and in savannas and pastures of Morocco and western Arabia. The effects of its venom are characterized by local and systemic alterations, such as inflammation and cardiovascular and hemostatic disturbances, which [...] Read more.
Bitis arietans is a snake of medical importance found throughout sub-Saharan Africa and in savannas and pastures of Morocco and western Arabia. The effects of its venom are characterized by local and systemic alterations, such as inflammation and cardiovascular and hemostatic disturbances, which can lead to victims’ death or permanent disability. To better characterize the inflammatory process induced by this snake’s venom, the participation of eicosanoids and PAF (platelet- activating factor) in this response were demonstrated in a previous study. In addition, edema and early increased vascular permeability followed by an accumulation of polymorphonuclear (PMN) cells in the peritoneal cavity were accompanied by the production of the eicosanoids LTB4, LTC4, TXB2, and PGE2, and local and systemic production of IL-6 and MCP-1. In this context, the present study focused on the identification of inflammatory mediators produced by human macrophages derived from THP-1 cells in response to Bitis arietans venom (BaV), and Kn-Ba, a serine protease purified from this venom. Here, we show that Kn-Ba, and even the less intensive BaV, induced the production of the cytokine TNF and the chemokines RANTES and IL-8. Only Kn-Ba was able to induce the production of IL-6, MCP-1, and IP-10, whereas PGE2 was produced only in response to BaV. Finally, the release of IL-1β in culture supernatants suggests the activation of the inflammasomes by the venom of Bitis arietans and by Kn-Ba, which will be investigated in more detail in future studies. Full article
(This article belongs to the Special Issue Celebrating 120 Years of Butantan Institute Contributions for Toxinology)
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12 pages, 2659 KiB  
Article
Oral Tolerance Induction by Bothrops jararaca Venom in a Murine Model and Cross-Reactivity with Toxins of Other Snake Venoms
by Lilian Rumi Tsuruta, Ana Maria Moro, Denise V. Tambourgi and Osvaldo Augusto Sant’Anna
Toxins 2021, 13(12), 865; https://0-doi-org.brum.beds.ac.uk/10.3390/toxins13120865 - 03 Dec 2021
Cited by 1 | Viewed by 2145
Abstract
Oral tolerance is defined as a specific suppression of cellular and humoral immune responses to a particular antigen through prior oral administration of an antigen. It has unique immunological importance since it is a natural and continuous event driven by external antigens. It [...] Read more.
Oral tolerance is defined as a specific suppression of cellular and humoral immune responses to a particular antigen through prior oral administration of an antigen. It has unique immunological importance since it is a natural and continuous event driven by external antigens. It is characterized by low levels of IgG in the serum of animals after immunization with the antigen. There is no report of induction of oral tolerance to Bothrops jararaca venom. Here, we induced oral tolerance to B. jararaca venom in BALB/c mice and evaluated the specific tolerance and cross-reactivity with the toxins of other Bothrops species after immunization with the snake venoms adsorbed to/encapsulated in nanostructured SBA-15 silica. Animals that received a high dose of B. jararaca venom (1.8 mg) orally responded by showing antibody titers similar to those of immunized animals. On the other hand, mice tolerized orally with three doses of 1 µg of B. jararaca venom showed low antibody titers. In animals that received a low dose of B. jararaca venom and were immunized with B. atrox or B. jararacussu venom, tolerance was null or only partial. Immunoblot analysis against the venom of different Bothrops species provided details about the main tolerogenic epitopes and clearly showed a difference compared to antiserum of immunized animals. Full article
(This article belongs to the Special Issue Celebrating 120 Years of Butantan Institute Contributions for Toxinology)
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20 pages, 4151 KiB  
Article
Recombinant Production and Characterization of a New Toxin from Cryptops iheringi Centipede Venom Revealed by Proteome and Transcriptome Analysis
by Lhiri Hanna De Lucca Caetano, Milton Yutaka Nishiyama-Jr, Bianca de Carvalho Lins Fernandes Távora, Ursula Castro de Oliveira, Inácio de Loiola Meirelles Junqueira-de-Azevedo, Eliana L. Faquim-Mauro and Geraldo Santana Magalhães
Toxins 2021, 13(12), 858; https://0-doi-org.brum.beds.ac.uk/10.3390/toxins13120858 - 02 Dec 2021
Cited by 4 | Viewed by 3024
Abstract
Among the Chilopoda class of centipede, the Cryptops genus is one of the most associated with envenomation in humans in the metropolitan region of the state of São Paulo. To date, there is no study in the literature about the toxins present in [...] Read more.
Among the Chilopoda class of centipede, the Cryptops genus is one of the most associated with envenomation in humans in the metropolitan region of the state of São Paulo. To date, there is no study in the literature about the toxins present in its venom. Thus, in this work, a transcriptomic characterization of the Cryptops iheringi venom gland, as well as a proteomic analysis of its venom, were performed to obtain a toxin profile of this species. These methods indicated that 57.9% of the sequences showed to be putative toxins unknown in public databases; among them, we pointed out a novel putative toxin named Cryptoxin-1. The recombinant form of this new toxin was able to promote edema in mice footpads with massive neutrophils infiltration, linking this toxin to envenomation symptoms observed in accidents with humans. Our findings may elucidate the role of this toxin in the venom, as well as the possibility to explore other proteins found in this work. Full article
(This article belongs to the Special Issue Celebrating 120 Years of Butantan Institute Contributions for Toxinology)
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12 pages, 3223 KiB  
Article
Novel Cysteine Protease Inhibitor Derived from the Haementeria vizottoi Leech: Recombinant Expression, Purification, and Characterization
by Débora do Carmo Linhares, Fernanda Faria, Roberto Tadashi Kodama, Adriane Michele Xavier Prado Amorim, Fernanda Calheta Vieira Portaro, Dilza Trevisan-Silva, Karla Fernanda Ferraz and Ana Marisa Chudzinski-Tavassi
Toxins 2021, 13(12), 857; https://0-doi-org.brum.beds.ac.uk/10.3390/toxins13120857 - 02 Dec 2021
Cited by 2 | Viewed by 2719
Abstract
Cathepsin L (CatL) is a lysosomal cysteine protease primarily involved in the terminal degradation of intracellular and endocytosed proteins. More specifically, in humans, CatL has been implicated in cancer progression and metastasis, as well as coronary artery diseases and others. Given this, the [...] Read more.
Cathepsin L (CatL) is a lysosomal cysteine protease primarily involved in the terminal degradation of intracellular and endocytosed proteins. More specifically, in humans, CatL has been implicated in cancer progression and metastasis, as well as coronary artery diseases and others. Given this, the search for potent CatL inhibitors is of great importance. In the search for new molecules to perform proteolytic activity regulation, salivary secretions from hematophagous animals have been an important source, as they present protease inhibitors that evolved to disable host proteases. Based on the transcriptome of the Haementeria vizzotoi leech, the cDNA of Cystatin-Hv was selected for this study. Cystatin-Hv was expressed in Pichia pastoris and purified by two chromatographic steps. The kinetic results using human CatL indicated that Cystatin-Hv, in its recombinant form, is a potent inhibitor of this protease, with a Ki value of 7.9 nM. Consequently, the present study describes, for the first time, the attainment and the biochemical characterization of a recombinant cystatin from leeches as a potent CatL inhibitor. While searching out for new molecules of therapeutic interest, this leech cystatin opens up possibilities for the future use of this molecule in studies involving cellular and in vivo models. Full article
(This article belongs to the Special Issue Celebrating 120 Years of Butantan Institute Contributions for Toxinology)
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9 pages, 987 KiB  
Article
Scorpion Envenomation of Lactating Rats Decreases the Seizure Threshold in Offspring
by Marina de Oliveira Rodrigues Barbosa, Maria Eliza F. do Val de Paulo and Ana Leonor Abrahão Nencioni
Toxins 2021, 13(12), 853; https://0-doi-org.brum.beds.ac.uk/10.3390/toxins13120853 - 30 Nov 2021
Cited by 1 | Viewed by 1804
Abstract
Few data are available in the literature describing the long-term effects of envenoming in the perinatal period. In this study, the relationship between envenoming of lactating rats and possible behavioral changes in the mother and in her offspring were investigated. Lactating Wistar rats [...] Read more.
Few data are available in the literature describing the long-term effects of envenoming in the perinatal period. In this study, the relationship between envenoming of lactating rats and possible behavioral changes in the mother and in her offspring were investigated. Lactating Wistar rats received a single dose of T. serrulatus crude venom on postnatal days 2 (V2), 10 (V10) or 16 (V16), and had their maternal behavior evaluated. The seizure threshold was evaluated in adulthood offspring. A decrease in maternal care during envenoming was observed in V2 and V10 groups. The retrieval behavior was absent in the V2 group, and a lower seizure threshold in the adult offspring of all groups was observed. During envenoming, mothers stayed away from their offspring for a relatively long time. Maternal deprivation during the early postnatal period is one of the most potent stressors for pups and could be responsible, at least in part, for the decrease in the convulsive threshold of the offspring since stress is pointed to as a risk factor for epileptogenesis. Furthermore, the scorpionic accident generates an intense immune response, and inflammation in neonates increases the susceptibility to seizures in adulthood. Therefore, maternal envenoming during lactation can have adverse effects on offspring in adulthood. Full article
(This article belongs to the Special Issue Celebrating 120 Years of Butantan Institute Contributions for Toxinology)
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13 pages, 1917 KiB  
Article
New Insights into the Hypotensins from Tityus serrulatus Venom: Pro-Inflammatory and Vasopeptidases Modulation Activities
by Bruno Duzzi, Cristiane Castilho Fernandes Silva, Roberto Tadashi Kodama, Daniela Cajado-Carvalho, Carla Cristina Squaiella-Baptistão and Fernanda Calheta Vieira Portaro
Toxins 2021, 13(12), 846; https://0-doi-org.brum.beds.ac.uk/10.3390/toxins13120846 - 26 Nov 2021
Cited by 7 | Viewed by 1813
Abstract
The Tityus serrulatus scorpion is considered the most dangerous of the Brazilian fauna due to the severe clinical manifestations in injured victims. Despite being abundant components of the venom, few linear peptides have been characterized so far, such as hypotensins. In vivo studies [...] Read more.
The Tityus serrulatus scorpion is considered the most dangerous of the Brazilian fauna due to the severe clinical manifestations in injured victims. Despite being abundant components of the venom, few linear peptides have been characterized so far, such as hypotensins. In vivo studies have demonstrated that hypotensin I (TsHpt-I) exerts hypotensive activity, with an angiotensin-converting enzyme (ACE)-independent mechanism of action. Since experiments have not yet been carried out to analyze the direct interaction of hypotensins with ACE, and to deepen the knowledge about these peptides, hypotensins I and II (TsHpt-II) were studied regarding their modulatory action over the activities of ACE and neprilysin (NEP), which are the peptidases involved in blood pressure control. Aiming to search for indications of possible pro-inflammatory action, hypotensins were also analyzed for their role in murine macrophage viability, the release of interleukins and phagocytic activity. TsHpt-I and -II were used in kinetic studies with the metallopeptidases ACE and NEP, and both hypotensins were able to increase the activity of ACE. TsHpt-I presented itself as an inhibitor of NEP, whereas TsHpt-II showed weak inhibition of the enzyme. The mechanism of inhibition of TsHpt-I in relation to NEP was defined as non-competitive, with an inhibition constant (Ki) of 4.35 μM. Concerning the analysis of cell viability and modulation of interleukin levels and phagocytic activity, BALB/c mice’s naïve macrophages were used, and an increase in TNF production in the presence of TsHpt-I and -II was observed, as well as an increase in IL-6 production in the presence of TsHpt-II only. Both hypotensins were able to increase the phagocytic activity of murine macrophages in vitro. The difference between TsHpt-I and -II is the residue at position 15, with a glutamine in TsHpt-I and a glutamic acid in TsHpt-II. Despite this, kinetic analyzes and cell assays indicated different actions of TsHpt-I and -II. Taken together, these results suggest a new mechanism for the hypotensive effects of TsHpt-I and -II. Furthermore, the release of some interleukins also suggests a role for these peptides in the venom inflammatory response. Even though these molecules have been well studied, the present results suggest a new mechanism for the hypotensive effects of TsHpt-I Full article
(This article belongs to the Special Issue Celebrating 120 Years of Butantan Institute Contributions for Toxinology)
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13 pages, 2012 KiB  
Article
Crotoxin Modulates Events Involved in Epithelial–Mesenchymal Transition in 3D Spheroid Model
by Ellen Emi Kato and Sandra Coccuzzo Sampaio
Toxins 2021, 13(11), 830; https://0-doi-org.brum.beds.ac.uk/10.3390/toxins13110830 - 22 Nov 2021
Cited by 5 | Viewed by 3205
Abstract
Epithelial–mesenchymal transition (EMT) occurs in the early stages of embryonic development and plays a significant role in the migration and the differentiation of cells into various types of tissues of an organism. However, tumor cells, with altered form and function, use the EMT [...] Read more.
Epithelial–mesenchymal transition (EMT) occurs in the early stages of embryonic development and plays a significant role in the migration and the differentiation of cells into various types of tissues of an organism. However, tumor cells, with altered form and function, use the EMT process to migrate and invade other tissues in the body. Several experimental (in vivo and in vitro) and clinical trial studies have shown the antitumor activity of crotoxin (CTX), a heterodimeric phospholipase A2 present in the Crotalus durissus terrificus venom. In this study, we show that CTX modulates the microenvironment of tumor cells. We have also evaluated the effect of CTX on the EMT process in the spheroid model. The invasion of type I collagen gels by heterospheroids (mix of MRC-5 and A549 cells constitutively prepared with 12.5 nM CTX), expression of EMT markers, and secretion of MMPs were analyzed. Western blotting analysis shows that CTX inhibits the expression of the mesenchymal markers, N-cadherin, α-SMA, and αv. This study provides evidence of CTX as a key modulator of the EMT process, and its antitumor action can be explored further for novel drug designing against metastatic cancer. Full article
(This article belongs to the Special Issue Celebrating 120 Years of Butantan Institute Contributions for Toxinology)
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19 pages, 4457 KiB  
Article
Crotalphine Attenuates Pain and Neuroinflammation Induced by Experimental Autoimmune Encephalomyelitis in Mice
by Aline C. Giardini, Bianca G. Evangelista, Morena B. Sant’Anna, Barbara B. Martins, Carmen L. P. Lancellotti, Adriano P. Ciena, Marucia Chacur, Rosana L. Pagano, Orlando G. Ribeiro, Vanessa O. Zambelli and Gisele Picolo
Toxins 2021, 13(11), 827; https://0-doi-org.brum.beds.ac.uk/10.3390/toxins13110827 - 22 Nov 2021
Cited by 7 | Viewed by 2581
Abstract
Multiple sclerosis (MS) is a demyelinating disease of inflammatory and autoimmune origin, which induces sensory and progressive motor impairments, including pain. Cells of the immune system actively participate in the pathogenesis and progression of MS by inducing neuroinflammation, tissue damage, and demyelination. Crotalphine [...] Read more.
Multiple sclerosis (MS) is a demyelinating disease of inflammatory and autoimmune origin, which induces sensory and progressive motor impairments, including pain. Cells of the immune system actively participate in the pathogenesis and progression of MS by inducing neuroinflammation, tissue damage, and demyelination. Crotalphine (CRO), a structural analogue to a peptide firstly identified in Crotalus durissus terrificus snake venom, induces analgesia by endogenous opioid release and type 2 cannabinoid receptor (CB2) activation. Since CB2 activation downregulates neuroinflammation and ameliorates symptoms in mice models of MS, it was presently investigated whether CRO has a beneficial effect in the experimental autoimmune encephalomyelitis (EAE). CRO was administered on the 5th day after immunization, in a single dose, or five doses starting at the peak of disease. CRO partially reverted EAE-induced mechanical hyperalgesia and decreased the severity of the clinical signs. In addition, CRO decreases the inflammatory infiltrate and glial cells activation followed by TNF-α and IL-17 downregulation in the spinal cord. Peripherally, CRO recovers the EAE-induced impairment in myelin thickness in the sciatic nerve. Therefore, CRO interferes with central and peripheral neuroinflammation, opening perspectives to MS control. Full article
(This article belongs to the Special Issue Celebrating 120 Years of Butantan Institute Contributions for Toxinology)
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14 pages, 1959 KiB  
Article
The Deleterious Effects of Shiga Toxin Type 2 Are Neutralized In Vitro by FabF8:Stx2 Recombinant Monoclonal Antibody
by Daniela Luz, Fernando D. Gómez, Raíssa L. Ferreira, Bruna S. Melo, Beatriz E. C. Guth, Wagner Quintilio, Ana Maria Moro, Agostina Presta, Flavia Sacerdoti, Cristina Ibarra, Gang Chen, Sachdev S. Sidhu, María Marta Amaral and Roxane M. F. Piazza
Toxins 2021, 13(11), 825; https://0-doi-org.brum.beds.ac.uk/10.3390/toxins13110825 - 22 Nov 2021
Cited by 2 | Viewed by 2066
Abstract
Hemolytic Uremic Syndrome (HUS) associated with Shiga-toxigenic Escherichia coli (STEC) infections is the principal cause of acute renal injury in pediatric age groups. Shiga toxin type 2 (Stx2) has in vitro cytotoxic effects on kidney cells, including human glomerular endothelial (HGEC) and Vero [...] Read more.
Hemolytic Uremic Syndrome (HUS) associated with Shiga-toxigenic Escherichia coli (STEC) infections is the principal cause of acute renal injury in pediatric age groups. Shiga toxin type 2 (Stx2) has in vitro cytotoxic effects on kidney cells, including human glomerular endothelial (HGEC) and Vero cells. Neither a licensed vaccine nor effective therapy for HUS is available for humans. Recombinant antibodies against Stx2, produced in bacteria, appeared as the utmost tool to prevent HUS. Therefore, in this work, a recombinant FabF8:Stx2 was selected from a human Fab antibody library by phage display, characterized, and analyzed for its ability to neutralize the Stx activity from different STEC-Stx2 and Stx1/Stx2 producing strains in a gold standard Vero cell assay, and the Stx2 cytotoxic effects on primary cultures of HGEC. This recombinant Fab showed a dissociation constant of 13.8 nM and a half maximum effective concentration (EC50) of 160 ng/mL to Stx2. Additionally, FabF8:Stx2 neutralized, in different percentages, the cytotoxic effects of Stx2 and Stx1/2 from different STEC strains on Vero cells. Moreover, it significantly prevented the deleterious effects of Stx2 in a dose-dependent manner (up to 83%) in HGEC and protected this cell up to 90% from apoptosis and necrosis. Therefore, this novel and simple anti-Stx2 biomolecule will allow further investigation as a new therapeutic option that could improve STEC and HUS patient outcomes. Full article
(This article belongs to the Special Issue Celebrating 120 Years of Butantan Institute Contributions for Toxinology)
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18 pages, 3928 KiB  
Article
Individual Variability in Bothrops atrox Snakes Collected from Different Habitats in the Brazilian Amazon: New Findings on Venom Composition and Functionality
by Leijane F. Sousa, Matthew L. Holding, Tiago H. M. Del-Rei, Marisa M. T. Rocha, Rosa H. V. Mourão, Hipócrates M. Chalkidis, Benedito Prezoto, H. Lisle Gibbs and Ana M. Moura-da-Silva
Toxins 2021, 13(11), 814; https://0-doi-org.brum.beds.ac.uk/10.3390/toxins13110814 - 18 Nov 2021
Cited by 12 | Viewed by 2356
Abstract
Differences in snake venom composition occur across all taxonomic levels and it has been argued that this variation represents an adaptation that has evolved to facilitate the capture and digestion of prey and evasion of predators. Bothrops atrox is a terrestrial pitviper that [...] Read more.
Differences in snake venom composition occur across all taxonomic levels and it has been argued that this variation represents an adaptation that has evolved to facilitate the capture and digestion of prey and evasion of predators. Bothrops atrox is a terrestrial pitviper that is distributed across the Amazon region, where it occupies different habitats. Using statistical analyses and functional assays that incorporate individual variation, we analyzed the individual venom variability in B. atrox snakes from four different habitats (forest, pasture, degraded area, and floodplain) in and around the Amazon River in Brazil. We observed venom differentiation between spatially distinct B. atrox individuals from the different habitats, with venom variation due to both common (high abundance) and rare (low abundance) proteins. Moreover, differences in the composition of the venoms resulted in individual variability in functionality and heterogeneity in the lethality to mammals and birds, particularly among the floodplain snakes. Taken together, the data obtained from individual venoms of B. atrox snakes, captured in different habitats from the Brazilian Amazon, support the hypothesis that the differential distribution of protein isoforms results in functional distinctiveness and the ability of snakes with different venoms to have variable toxic effects on different prey. Full article
(This article belongs to the Special Issue Celebrating 120 Years of Butantan Institute Contributions for Toxinology)
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14 pages, 2054 KiB  
Article
Modulation of Adhesion Molecules Expression by Different Metalloproteases Isolated from Bothrops Snakes
by Bianca C. Zychar, Patrícia B. Clissa, Eneas Carvalho, Adilson S. Alves, Cristiani Baldo, Eliana L. Faquim-Mauro and Luís Roberto C. Gonçalves
Toxins 2021, 13(11), 803; https://0-doi-org.brum.beds.ac.uk/10.3390/toxins13110803 - 15 Nov 2021
Cited by 7 | Viewed by 2549
Abstract
Snake venom metalloproteinases (SVMP) are involved in local inflammatory reactions observed after snakebites. Based on domain composition, they are classified as PI (pro-domain + proteolytic domain), PII (PI + disintegrin-like domains), or PIII (PII + cysteine-rich domains). Here, we studied the role of [...] Read more.
Snake venom metalloproteinases (SVMP) are involved in local inflammatory reactions observed after snakebites. Based on domain composition, they are classified as PI (pro-domain + proteolytic domain), PII (PI + disintegrin-like domains), or PIII (PII + cysteine-rich domains). Here, we studied the role of different SVMPs domains in inducing the expression of adhesion molecules at the microcirculation of the cremaster muscle of mice. We used Jararhagin (Jar)—a PIII SVMP with intense hemorrhagic activity, and Jar-C—a Jar devoid of the catalytic domain, with no hemorrhagic activity, both isolated from B. jararaca venom and BnP-1—a weakly hemorrhagic P1 SVMP from B. neuwiedi venom. Toxins (0.5 µg) or PBS (100 µL) were injected into the scrotum of mice, and 2, 4, or 24 h later, the protein and gene expression of CD54 and CD31 in the endothelium, and integrins (CD11a and CD11b), expressed in leukocytes were evaluated. Toxins induced significant increases in CD54, CD11a, and CD11b at the initial time and a time-related increase in CD31 expression. In conclusion, our results suggest that, despite differences in hemorrhagic activities and domain composition of the SVMPs used in this study, they behave similarly to the induction of expression of adhesion molecules that promote leukocyte recruitment. Full article
(This article belongs to the Special Issue Celebrating 120 Years of Butantan Institute Contributions for Toxinology)
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13 pages, 726 KiB  
Article
Observation of Bothrops atrox Snake Envenoming Blister Formation from Five Patients: Pathophysiological Insights
by Sarah N. C. Gimenes, Jacqueline A. G. Sachett, Mônica Colombini, Luciana A. Freitas-de-Sousa, Hiochelson N. S. Ibiapina, Allyson G. Costa, Monique F. Santana, Jeong-Jin Park, Nicholas E. Sherman, Luiz C. L. Ferreira, Fan H. Wen, Wuelton M. Monteiro, Ana M. Moura-da-Silva and Jay W. Fox
Toxins 2021, 13(11), 800; https://0-doi-org.brum.beds.ac.uk/10.3390/toxins13110800 - 13 Nov 2021
Cited by 14 | Viewed by 2823
Abstract
In the Brazilian Amazon, Bothrops atrox snakebites are frequent, and patients develop tissue damage with blisters sometimes observed in the proximity of the wound. Antivenoms do not seem to impact blister formation, raising questions regarding the mechanisms underlying blister formation. Here, we launched [...] Read more.
In the Brazilian Amazon, Bothrops atrox snakebites are frequent, and patients develop tissue damage with blisters sometimes observed in the proximity of the wound. Antivenoms do not seem to impact blister formation, raising questions regarding the mechanisms underlying blister formation. Here, we launched a clinical and laboratory-based study including five patients who followed and were treated by the standard clinical protocols. Blister fluids were collected for proteomic analyses and molecular assessment of the presence of venom and antivenom. Although this was a small patient sample, there appeared to be a correlation between the time of blister appearance (shorter) and the amount of venom present in the serum (higher). Of particular interest was the biochemical identification of both venom and antivenom in all blister fluids. From the proteomic analysis of the blister fluids, all were observed to be a rich source of damage-associated molecular patterns (DAMPs), immunomodulators, and matrix metalloproteinase-9 (MMP-9), suggesting that the mechanisms by which blisters are formed includes the toxins very early in envenomation and continue even after antivenom treatment, due to the pro-inflammatory molecules generated by the toxins in the first moments after envenomings, indicating the need for local treatments with anti-inflammatory drugs plus toxin inhibitors to prevent the severity of the wounds. Full article
(This article belongs to the Special Issue Celebrating 120 Years of Butantan Institute Contributions for Toxinology)
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32 pages, 5155 KiB  
Article
Systemic Effects of Hemorrhagic Snake Venom Metalloproteinases: Untargeted Peptidomics to Explore the Pathodegradome of Plasma Proteins
by Luciana Bertholim, Alison F. A. Chaves, Ana K. Oliveira, Milene C. Menezes, Amanda F. Asega, Alexandre K. Tashima, Andre Zelanis and Solange M. T. Serrano
Toxins 2021, 13(11), 764; https://0-doi-org.brum.beds.ac.uk/10.3390/toxins13110764 - 28 Oct 2021
Cited by 4 | Viewed by 2646
Abstract
Hemorrhage induced by snake venom metalloproteinases (SVMPs) is a complex phenomenon that involves capillary disruption and blood extravasation. HF3 (hemorrhagic factor 3) is an extremely hemorrhagic SVMP of Bothrops jararaca venom. Studies using proteomic approaches revealed targets of HF3 among intracellular and extracellular [...] Read more.
Hemorrhage induced by snake venom metalloproteinases (SVMPs) is a complex phenomenon that involves capillary disruption and blood extravasation. HF3 (hemorrhagic factor 3) is an extremely hemorrhagic SVMP of Bothrops jararaca venom. Studies using proteomic approaches revealed targets of HF3 among intracellular and extracellular proteins. However, the role of the cleavage of plasma proteins in the context of the hemorrhage remains not fully understood. The main goal of this study was to analyze the degradome of HF3 in human plasma. For this purpose, approaches for the depletion of the most abundant proteins, and for the enrichment of low abundant proteins of human plasma, were used to minimize the dynamic range of protein concentration, in order to assess the proteolytic activity of HF3 on a wide spectrum of proteins, and to detect the degradation products using mass spectrometry-based untargeted peptidomics. The results revealed the hydrolysis products generated by HF3 and allowed the identification of cleavage sites. A total of 61 plasma proteins were identified as cleaved by HF3. Some of these proteins corroborate previous studies, and others are new HF3 targets, including proteins of the coagulation cascade, of the complement system, proteins acting on the modulation of inflammation, and plasma proteinase inhibitors. Overall, the data indicate that HF3 escapes inhibition and sculpts the plasma proteome by degrading key proteins and generating peptides that may act synergistically in the hemorrhagic process. Full article
(This article belongs to the Special Issue Celebrating 120 Years of Butantan Institute Contributions for Toxinology)
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28 pages, 2637 KiB  
Article
Bothrops Jararaca Snake Venom Modulates Key Cancer-Related Proteins in Breast Tumor Cell Lines
by Carolina Yukiko Kisaki, Stephanie Santos Suehiro Arcos, Fabio Montoni, Wellington da Silva Santos, Hamida Macêdo Calacina, Ismael Feitosa Lima, Daniela Cajado-Carvalho, Emer Suavinho Ferro, Milton Yutaka Nishiyama-Jr and Leo Kei Iwai
Toxins 2021, 13(8), 519; https://0-doi-org.brum.beds.ac.uk/10.3390/toxins13080519 - 25 Jul 2021
Cited by 7 | Viewed by 4763
Abstract
Cancer is characterized by the development of abnormal cells that divide in an uncontrolled way and may spread into other tissues where they may infiltrate and destroy normal body tissue. Several previous reports have described biochemical anti-tumorigenic properties of crude snake venom or [...] Read more.
Cancer is characterized by the development of abnormal cells that divide in an uncontrolled way and may spread into other tissues where they may infiltrate and destroy normal body tissue. Several previous reports have described biochemical anti-tumorigenic properties of crude snake venom or its components, including their capability of inhibiting cell proliferation and promoting cell death. However, to the best of our knowledge, there is no work describing cancer cell proteomic changes following treatment with snake venoms. In this work we describe the quantitative changes in proteomics of MCF7 and MDA-MB-231 breast tumor cell lines following treatment with Bothrops jararaca snake venom, as well as the functional implications of the proteomic changes. Cell lines were treated with sub-toxic doses at either 0.63 μg/mL (low) or 2.5 μg/mL (high) of B. jararaca venom for 24 h, conditions that cause no cell death per se. Proteomics analysis was conducted on a nano-scale liquid chromatography coupled on-line with mass spectrometry (nLC-MS/MS). More than 1000 proteins were identified and evaluated from each cell line treated with either the low or high dose of the snake venom. Protein profiling upon venom treatment showed differential expression of several proteins related to cancer cell metabolism, immune response, and inflammation. Among the identified proteins we highlight histone H3, SNX3, HEL-S-156an, MTCH2, RPS, MCC2, IGF2BP1, and GSTM3. These data suggest that sub-toxic doses of B. jararaca venom have potential to modulate cancer-development related protein targets in cancer cells. This work illustrates a novel biochemical strategy to identify therapeutic targets against cancer cell growth and survival. Full article
(This article belongs to the Special Issue Celebrating 120 Years of Butantan Institute Contributions for Toxinology)
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Review

Jump to: Editorial, Research

20 pages, 7135 KiB  
Review
Fish Cytolysins in All Their Complexity
by Fabiana V. Campos, Helena B. Fiorotti, Juliana B. Coitinho and Suely G. Figueiredo
Toxins 2021, 13(12), 877; https://0-doi-org.brum.beds.ac.uk/10.3390/toxins13120877 - 09 Dec 2021
Cited by 5 | Viewed by 2610
Abstract
The majority of the effects observed upon envenomation by scorpaenoid fish species can be reproduced by the cytolysins present in their venoms. Fish cytolysins are multifunctional proteins that elicit lethal, cytolytic, cardiovascular, inflammatory, nociceptive, and neuromuscular activities, representing a novel class of protein [...] Read more.
The majority of the effects observed upon envenomation by scorpaenoid fish species can be reproduced by the cytolysins present in their venoms. Fish cytolysins are multifunctional proteins that elicit lethal, cytolytic, cardiovascular, inflammatory, nociceptive, and neuromuscular activities, representing a novel class of protein toxins. These large proteins (MW 150–320 kDa) are composed by two different subunits, termed α and β, with about 700 amino acid residues each, being usually active in oligomeric form. There is a high degree of similarity between the primary sequences of cytolysins from different fish species. This suggests these molecules share similar mechanisms of action, which, at least regarding the cytolytic activity, has been proved to involve pore formation. Although the remaining components of fish venoms have interesting biological activities, fish cytolysins stand out because of their multifunctional nature and their ability to reproduce the main events of envenomation on their own. Considerable knowledge about fish cytolysins has been accumulated over the years, although there remains much to be unveiled. In this review, we compiled and compared the current information on the biochemical aspects and pharmacological activities of fish cytolysins, going over their structures, activities, mechanisms of action, and perspectives for the future. Full article
(This article belongs to the Special Issue Celebrating 120 Years of Butantan Institute Contributions for Toxinology)
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28 pages, 2773 KiB  
Review
Inflammatory Effects of Bothrops Phospholipases A2: Mechanisms Involved in Biosynthesis of Lipid Mediators and Lipid Accumulation
by Vanessa Moreira, Elbio Leiguez, Priscila Motta Janovits, Rodrigo Maia-Marques, Cristina Maria Fernandes and Catarina Teixeira
Toxins 2021, 13(12), 868; https://0-doi-org.brum.beds.ac.uk/10.3390/toxins13120868 - 04 Dec 2021
Cited by 12 | Viewed by 3048
Abstract
Phospholipases A2s (PLA2s) constitute one of the major protein groups present in the venoms of viperid and crotalid snakes. Snake venom PLA2s (svPLA2s) exhibit a remarkable functional diversity, as they have been described to induce [...] Read more.
Phospholipases A2s (PLA2s) constitute one of the major protein groups present in the venoms of viperid and crotalid snakes. Snake venom PLA2s (svPLA2s) exhibit a remarkable functional diversity, as they have been described to induce a myriad of toxic effects. Local inflammation is an important characteristic of snakebite envenomation inflicted by viperid and crotalid species and diverse svPLA2s have been studied for their proinflammatory properties. Moreover, based on their molecular, structural, and functional properties, the viperid svPLA2s are classified into the group IIA secreted PLA2s, which encompasses mammalian inflammatory sPLA2s. Thus, research on svPLA2s has attained paramount importance for better understanding the role of this class of enzymes in snake envenomation and the participation of GIIA sPLA2s in pathophysiological conditions and for the development of new therapeutic agents. In this review, we highlight studies that have identified the inflammatory activities of svPLA2s, in particular, those from Bothrops genus snakes, which are major medically important snakes in Latin America, and we describe recent advances in our collective understanding of the mechanisms underlying their inflammatory effects. We also discuss studies that dissect the action of these venom enzymes in inflammatory cells focusing on molecular mechanisms and signaling pathways involved in the biosynthesis of lipid mediators and lipid accumulation in immunocompetent cells. Full article
(This article belongs to the Special Issue Celebrating 120 Years of Butantan Institute Contributions for Toxinology)
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23 pages, 4184 KiB  
Review
Neglected Venomous Animals and Toxins: Underrated Biotechnological Tools in Drug Development
by Guilherme Rabelo Coelho, Daiane Laise da Silva, Emidio Beraldo-Neto, Hugo Vigerelli, Laudiceia Alves de Oliveira, Juliana Mozer Sciani and Daniel Carvalho Pimenta
Toxins 2021, 13(12), 851; https://0-doi-org.brum.beds.ac.uk/10.3390/toxins13120851 - 29 Nov 2021
Cited by 3 | Viewed by 3915
Abstract
Among the vast repertoire of animal toxins and venoms selected by nature and evolution, mankind opted to devote its scientific attention—during the last century—to a restricted group of animals, leaving a myriad of toxic creatures aside. There are several underlying and justifiable reasons [...] Read more.
Among the vast repertoire of animal toxins and venoms selected by nature and evolution, mankind opted to devote its scientific attention—during the last century—to a restricted group of animals, leaving a myriad of toxic creatures aside. There are several underlying and justifiable reasons for this, which include dealing with the public health problems caused by envenoming by such animals. However, these studies became saturated and gave rise to a whole group of animals that become neglected regarding their venoms and secretions. This repertoire of unexplored toxins and venoms bears biotechnological potential, including the development of new technologies, therapeutic agents and diagnostic tools and must, therefore, be assessed. In this review, we will approach such topics through an interconnected historical and scientific perspective that will bring up the major discoveries and innovations in toxinology, achieved by researchers from the Butantan Institute and others, and describe some of the major research outcomes from the study of these neglected animals. Full article
(This article belongs to the Special Issue Celebrating 120 Years of Butantan Institute Contributions for Toxinology)
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18 pages, 1307 KiB  
Review
Lonomia obliqua Envenoming and Innovative Research
by Miryam Paola Alvarez-Flores, Renata Nascimento Gomes, Dilza Trevisan-Silva, Douglas Souza Oliveira, Isabel de Fátima Correia Batista, Marcus Vinicius Buri, Angela Maria Alvarez, Carlos DeOcesano-Pereira, Marcelo Medina de Souza and Ana Marisa Chudzinski-Tavassi
Toxins 2021, 13(12), 832; https://0-doi-org.brum.beds.ac.uk/10.3390/toxins13120832 - 23 Nov 2021
Cited by 8 | Viewed by 6931
Abstract
As a tribute to Butantan Institute in its 120th anniversary, this review describes some of the scientific research efforts carried out in the study of Lonomia envenoming in Brazil, a country where accidents with caterpillars reach over 42,000 individuals per year (especially in [...] Read more.
As a tribute to Butantan Institute in its 120th anniversary, this review describes some of the scientific research efforts carried out in the study of Lonomia envenoming in Brazil, a country where accidents with caterpillars reach over 42,000 individuals per year (especially in South and Southeast Brazil). Thus, the promising data regarding the studies with Lonomia’s toxins contributed to the creation of new research centers specialized in toxinology based at Butantan Institute, as well as to the production of the antilonomic serum (ALS), actions which are in line with the Butantan Institute mission “to research, develop, manufacture, and provide products and services for the health of the population”. In addition, the study of the components of the Lonomia obliqua bristle extract led to the discovery of new molecules with peculiar properties, opening a field of knowledge that could lead to the development and innovation of new drugs aimed at cell regeneration and inflammatory diseases. Full article
(This article belongs to the Special Issue Celebrating 120 Years of Butantan Institute Contributions for Toxinology)
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