Journal of Venomous Animals and Toxins Including Tropical Diseases最新文献

{"title":"Zika virus serological diagnosis: commercial tests and monoclonal antibodies as tools.","authors":"Isaura Beatriz Borges Silva,&nbsp;Aldacilene Souza da Silva,&nbsp;Mariana Sequetin Cunha,&nbsp;Aline Diniz Cabral,&nbsp;Kelly Cristina Alves de Oliveira,&nbsp;Elizabeth De Gaspari,&nbsp;Carlos Roberto Prudencio","doi":"10.1590/1678-9199-JVATITD-2020-0019","DOIUrl":"https://doi.org/10.1590/1678-9199-JVATITD-2020-0019","url":null,"abstract":"<p><p>Zika virus (ZIKV), an emerging arthropod-borne virus (arbovirus) of the <i>Flaviviridae</i> family, is a current issue worldwide, particularly because of the congenital and neurological syndromes associated with infection by this virus. As the initial clinical symptoms of all diseases caused by this group are very similar, clinical diagnosis is difficult. Furthermore, laboratory diagnostic efforts have failed to identify specific and accurate tests for each virus of the <i>Flaviviridae</i> family due to the cross-reactivity of these viruses in serum samples. This situation has resulted in underreporting of the diseases caused by flaviviruses. However, many companies developed commercial diagnostic tests after the recent ZIKV outbreak. Moreover, health regulatory agencies have approved different commercial tests to extend the monitoring of ZIKV infections. Considering that a specific and sensitive diagnostic method for estimating risk and evaluating ZIKV propagation is still needed, this review aims to provide an update of the main commercially approved serological diagnostics test by the US Food and Drug Administration (FDA) and Brazilian National Health Surveillance Agency (ANVISA). Additionally, we present the technologies used for monoclonal antibody production as a tool for the development of diagnostic tests and applications of these antibodies in detecting ZIKV infections worldwide.</p>","PeriodicalId":17565,"journal":{"name":"Journal of Venomous Animals and Toxins Including Tropical Diseases","volume":"26 ","pages":"e20200019"},"PeriodicalIF":2.4,"publicationDate":"2020-11-18","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7685096/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"38679846","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Erratum: Immunohistochemical investigation of neuronal injury in cerebral cortex of cobra-envenomed rats.","authors":"","doi":"10.1590/1678-9199-2004000100005er","DOIUrl":"https://doi.org/10.1590/1678-9199-2004000100005er","url":null,"abstract":"<p><p>[This corrects the article DOI: 10.1590/S1678-91992004000100005.].</p>","PeriodicalId":17565,"journal":{"name":"Journal of Venomous Animals and Toxins Including Tropical Diseases","volume":"26 ","pages":"e5376er"},"PeriodicalIF":2.4,"publicationDate":"2020-11-09","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7653900/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"38633990","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Antifungal activity of liriodenine on agents of systemic mycoses, with emphasis on the genus <i>Paracoccidioides</i>.","authors":"Adriele Dandara Levorato Vinche, Iván de-la-Cruz-Chacón, Alma Rosa González-Esquinca, Julhiany de Fátima da Silva, Gisela Ferreira, Daniela Carvalho Dos Santos, Hans Garcia Garces, Daniela Vanessa Moris de Oliveira, Camila Marçon, Ricardo de Souza Cavalcante, Rinaldo Poncio Mendes","doi":"10.1590/1678-9199-JVATITD-2020-0023","DOIUrl":"10.1590/1678-9199-JVATITD-2020-0023","url":null,"abstract":"<p><strong>Background: </strong>Endemic systemic mycoses remain a health challenge, since these opportunistic diseases are increasingly infecting immunosuppressed patients. The simultaneous use of antifungal compounds and other drugs to treat infectious or non-infectious diseases has led to several interactions and undesirable effects. Thus, new antifungal compounds should be investigated. The present study aimed to evaluate the activity of liriodenine extracted from <i>Annona macroprophyllata</i> on agents of systemic mycoses, with emphasis on the genus <i>Paracoccidioides</i>.</p><p><strong>Methods: </strong>The minimum inhibitory concentration (MIC) and minimum fungicide concentration (MFC) were determined by the microdilution method. The cellular alterations caused by liriodenine on a standard <i>P. brasiliensis</i> (Pb18) strain were evaluated by transmission and scanning electron microscopy.</p><p><strong>Results: </strong>Liriodenine was effective only in 3 of the 8 strains of the genus <i>Paracoccidioides</i> and in the <i>Histoplasma capsulatum</i> strain, in a very low concentration (MIC of 1.95 μg.mL^-1); on yeasts of <i>Candida</i> spp. (MIC of 125 to 250 μg.mL-1), including <i>C. krusei</i> (250 μg.mL^-1), which has intrinsic resistance to fluconazole; and in <i>Cryptococcus neoformans</i> and <i>Cryptococcus gattii</i> (MIC of 62.5 μg.mL^-1). However, liriodenine was not effective against <i>Aspergillus fumigatus</i> at the studied concentrations. Liriodenine exhibited fungicidal activity against all standard strains and clinical isolates that showed to be susceptible by <i>in vitro</i> tests. Electron microscopy revealed cytoplasmic alterations and damage to the cell wall of <i>P. brasiliensis</i> (Pb18).</p><p><strong>Conclusion: </strong>Our results indicate that liriodenine is a promising fungicidal compound that should undergo further investigation with some chemical modifications.</p>","PeriodicalId":17565,"journal":{"name":"Journal of Venomous Animals and Toxins Including Tropical Diseases","volume":"26 ","pages":"e20200023"},"PeriodicalIF":2.4,"publicationDate":"2020-10-28","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7595607/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"38613913","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"In-depth transcriptome reveals the potential biotechnological application of <i>Bothrops jararaca</i> venom gland.","authors":"Leandro de Mattos Pereira,&nbsp;Elisa Alves Messias,&nbsp;Bruna Pereira Sorroche,&nbsp;Angela das Neves Oliveira,&nbsp;Lidia Maria Rebolho Batista Arantes,&nbsp;Ana Carolina de Carvalho,&nbsp;Anita Mitico Tanaka-Azevedo,&nbsp;Kathleen Fernandes Grego,&nbsp;André Lopes Carvalho,&nbsp;Matias Eliseo Melendez","doi":"10.1590/1678-9199-JVATITD-2019-0058","DOIUrl":"https://doi.org/10.1590/1678-9199-JVATITD-2019-0058","url":null,"abstract":"<p><strong>Background: </strong>Lack of complete genomic data of <i>Bothrops jararaca</i> impedes molecular biology research focusing on biotechnological applications of venom gland components. Identification of full-length coding regions of genes is crucial for the correct molecular cloning design.</p><p><strong>Methods: </strong>RNA was extracted from the venom gland of one adult female specimen of <i>Bothrops jararaca</i>. Deep sequencing of the mRNA library was performed using Illumina NextSeq 500 platform. <i>De novo</i> assembly of <i>B. jararaca</i> transcriptome was done using Trinity. Annotation was performed using Blast2GO. All predicted proteins after clustering step were blasted against non-redundant protein database of NCBI using BLASTP. Metabolic pathways present in the transcriptome were annotated using the KAAS-KEGG Automatic Annotation Server. Toxins were identified in the <i>B. jararaca</i> predicted proteome using BLASTP against all protein sequences obtained from Animal Toxin Annotation Project from Uniprot KB/Swiss-Pro database. Figures and data visualization were performed using ggplot2 package in R language environment.</p><p><strong>Results: </strong>We described the in-depth transcriptome analysis of <i>B. jararaca</i> venom gland, in which 76,765 <i>de novo</i> assembled isoforms, 96,044 transcribed genes and 41,196 unique proteins were identified. The most abundant transcript was the zinc metalloproteinase-disintegrin-like jararhagin. Moreover, we identified 78 distinct functional classes of proteins, including toxins, inhibitors and tumor suppressors. Other venom proteins identified were the hemolytic lethal factors stonustoxin and verrucotoxin.</p><p><strong>Conclusion: </strong>It is believed that the application of deep sequencing to the analysis of snake venom transcriptomes may represent invaluable insight on their biotechnological potential focusing on candidate molecules.</p>","PeriodicalId":17565,"journal":{"name":"Journal of Venomous Animals and Toxins Including Tropical Diseases","volume":"26 ","pages":"e20190058"},"PeriodicalIF":2.4,"publicationDate":"2020-10-21","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7579844/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"38569369","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Oxidative stress and antioxidant defense in detoxification systems of snake venom-induced toxicity.","authors":"Degang Dong,&nbsp;Zhongping Deng,&nbsp;Zhangren Yan,&nbsp;Wenli Mao,&nbsp;Jun Yi,&nbsp;Mei Song,&nbsp;Qiang Li,&nbsp;Jun Chen,&nbsp;Qi Chen,&nbsp;Liang Liu,&nbsp;Xi Wang,&nbsp;Xiuqin Huang,&nbsp;Wanchun Wang","doi":"10.1590/1678-9199-JVATITD-2020-0053","DOIUrl":"https://doi.org/10.1590/1678-9199-JVATITD-2020-0053","url":null,"abstract":"<p><strong>Background: </strong>Snakebites remain a major life-threatening event worldwide. It is still difficult to make a positive identification of snake species by clinicians in both Western medicine and Chinese medicine. The main reason for this is a shortage of diagnostic biomarkers and lack of knowledge about pathways of venom-induced toxicity. In traditional Chinese medicine, snakebites are considered to be treated with wind, fire, and wind-fire toxin, but additional studies are required.</p><p><strong>Methods: </strong>Cases of snakebite seen at the Affiliated Hospital of Jiangxi University of Traditional Chinese Medicine were grouped as follows: fire toxin - including four cases of bites by <i>Agkistrodon acutus</i> and three bites by <i>Trimeresurus stejnegeri</i> - and wind-fire toxin - four cases of bites by vipers and three bites by cobras. Serum protein quantification was performed using LC-MS/MS. Differential abundance proteins (DAPs) were identified from comparison of snakebites of each snake species and healthy controls. The protein interaction network was constructed using STITCH database.</p><p><strong>Results: </strong>Principal component analysis and hierarchical clustering of 474 unique proteins exhibited protein expression profiles of wind-fire toxins that are distinct from that of fire toxins. Ninety-three DAPs were identified in each snakebite subgroup as compared with healthy control, of which 38 proteins were found to have significantly different expression levels and 55 proteins displayed no expression in one subgroup, by subgroup comparison. GO analysis revealed that the DAPs participated in bicarbonate/oxygen transport and hydrogen peroxide catabolic process, and affected carbon-oxygen lyase activity and heme binding. Thirty DAPs directly or indirectly acted on hydrogen peroxide in the interaction network of proteins and drug compounds. The network was clustered into four groups: lipid metabolism and transport; IGF-mediated growth; oxygen transport; and innate immunity.</p><p><strong>Conclusions: </strong>Our results show that the pathways of snake venom-induced toxicity may form a protein network of antioxidant defense by regulating oxidative stress through interaction with hydrogen peroxide.</p>","PeriodicalId":17565,"journal":{"name":"Journal of Venomous Animals and Toxins Including Tropical Diseases","volume":"26 ","pages":"e20200053"},"PeriodicalIF":2.4,"publicationDate":"2020-10-19","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7574533/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"38539617","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Venom complexity of <i>Bothrops atrox</i> (common lancehead) siblings.","authors":"Daniela Miki Hatakeyama, Lídia Jorge Tasima, Cesar Adolfo Bravo-Tobar, Caroline Serino-Silva, Alexandre Keiji Tashima, Caroline Fabri Bittencourt Rodrigues, Weslei da Silva Aguiar, Nathália da Costa Galizio, Eduardo Oliveira Venancio de Lima, Victor Koiti Kavazoi, Juan David Gutierrez-Marín, Iasmim Baptista de Farias, Sávio Stefanini Sant'Anna, Kathleen Fernandes Grego, Karen de Morais-Zani, Anita Mitico Tanaka-Azevedo","doi":"10.1590/1678-9199-JVATITD-2020-0018","DOIUrl":"10.1590/1678-9199-JVATITD-2020-0018","url":null,"abstract":"<p><strong>Background: </strong>Variability in snake venoms is a well-studied phenomenon. However, sex-based variation of <i>Bothrops atrox</i> snake venom using siblings is poorly investigated. <i>Bothrops atrox</i> is responsible for the majority of snakebite accidents in the Brazilian Amazon region. Differences in the venom composition of <i>Bothrops</i> genus have been linked to several factors such as ontogeny, geographical distribution, prey preferences and sex. Thus, in the current study, venom samples of <i>Bothrops atrox</i> male and female siblings were analyzed in order to compare their biochemical and biological characteristics.</p><p><strong>Methods: </strong>Venoms were collected from five females and four males born from a snake captured from the wild in São Bento (Maranhão, Brazil), and kept in the Laboratory of Herpetology of Butantan Intitute. The venoms were analyzed individually and as a pool of each gender. The assays consisted in protein quantification, 1-DE, mass spectrometry, proteolytic, phospholipase A₂, L-amino acid oxidase activities, minimum coagulant dose upon plasma, minimum hemorrhagic dose and lethal dose 50%.</p><p><strong>Results: </strong>Electrophoretic profiles of male's and female's venom pools were quite similar, with minor sex-based variation. Male venom showed higher LAAO, PLA₂ and hemorrhagic activities, while female venom showed higher coagulant activity. On the other hand, the proteolytic activities did not show statistical differences between pools, although some individual variations were observed. Meanwhile, proteomic profile revealed 112 different protein compounds; of which 105 were common proteins of female's and male's venom pools and seven were unique to females. Despite individual variations, lethality of both pools showed similar values.</p><p><strong>Conclusion: </strong>Although differences between female and male venoms were observed, our results show that individual variations are significant even between siblings, highlighting that biological activities of venoms and its composition are influenced by other factors beyond gender.</p>","PeriodicalId":17565,"journal":{"name":"Journal of Venomous Animals and Toxins Including Tropical Diseases","volume":"26 ","pages":"e20200018"},"PeriodicalIF":1.8,"publicationDate":"2020-10-12","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7553035/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"38622700","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"The coevolution between telson morphology and venom glands in scorpions (Arachnida).","authors":"Wilson R Lourenço","doi":"10.1590/1678-9199-JVATITD-2020-0128","DOIUrl":"https://doi.org/10.1590/1678-9199-JVATITD-2020-0128","url":null,"abstract":"<p><p>As in previous contributions to the <i>JVATiTD</i>, the aim of this note is to bring some general information on a particular aspect of the scorpion biology. An attempt is made to explain the possible coevolution of telson morphology and venom glands, which took place during several hundred million years and in particular since scorpions migrated from aquatic to terrestrial environments. Three components can be directly associated with predation and defensive behaviours: (1) morphology of the chelae and structure of the chelae fingers granulations; (2) morphology of the metasoma and in particular of the telson; (3) evolution of tegumentary glands in the telson toward different types of venom glands. Since a number of recent contributions already treated some of these aspects, I will limit my comments to the possible evolution of the telson in relation to the evolution of venom glands. As in previous contributions, the content of this article is basically addressed to non-specialists on scorpions whose research embraces scorpions in several fields such as venom toxins and public health.</p>","PeriodicalId":17565,"journal":{"name":"Journal of Venomous Animals and Toxins Including Tropical Diseases","volume":"26 ","pages":"e20200128"},"PeriodicalIF":2.4,"publicationDate":"2020-10-09","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7546543/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"38516665","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Erratum: Streamlined downstream process for efficient and sustainable F(ab')₂ antivenom preparation.","authors":"","doi":"10.1590/1678-9199-JVATITD-2020-0025er","DOIUrl":"https://doi.org/10.1590/1678-9199-JVATITD-2020-0025er","url":null,"abstract":"<p><p>[This corrects the article DOI: 10.1590/1678-9199-jvatitd-2020-0025.].</p>","PeriodicalId":17565,"journal":{"name":"Journal of Venomous Animals and Toxins Including Tropical Diseases","volume":"26 ","pages":"e2020025er"},"PeriodicalIF":2.4,"publicationDate":"2020-10-09","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7546365/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"38516666","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"A Kunitz-type peptide from <i>Dendroaspis polylepis</i> venom as a simultaneous inhibitor of serine and cysteine proteases.","authors":"Roberto Tadashi Kodama,&nbsp;Alexandre Kazuo Kuniyoshi,&nbsp;Cristiane Castilho Fernandes da Silva,&nbsp;Daniela Cajado-Carvalho,&nbsp;Bruno Duzzi,&nbsp;Douglas Ceolin Mariano,&nbsp;Daniel C Pimenta,&nbsp;Rafael Borges,&nbsp;Wilmar Dias da Silva,&nbsp;Fernanda Calheta Vieira Portaro","doi":"10.1590/1678-9199-JVATITD-2020-0037","DOIUrl":"https://doi.org/10.1590/1678-9199-JVATITD-2020-0037","url":null,"abstract":"<p><strong>Background: </strong>Proteases play an important role for the proper physiological functions of the most diverse organisms. When unregulated, they are associated with several pathologies. Therefore, proteases have become potential therapeutic targets regarding the search for inhibitors. Snake venoms are complex mixtures of molecules that can feature a variety of functions, including peptidase inhibition. Considering this, the present study reports the purification and characterization of a Kunitz-type peptide present in the <i>Dendroaspis polylepis</i> venom as a simultaneous inhibitor of elastase-1 and cathepsin L.</p><p><strong>Methods: </strong>The low molecular weight pool from <i>D. polylepis</i> venom was fractionated in reverse phase HPLC and all peaks were tested in fluorimetric assays. The selected fraction that presented inhibitory activity over both proteases was submitted to mass spectrometry analysis, and the obtained sequence was determined as a Kunitz-type serine protease inhibitor homolog dendrotoxin I. The molecular docking of the Kunitz peptide on the elastase was carried out in the program Z-DOCK, and the program RosettaDock was used to add hydrogens to the models, which were re-ranked using ZRANK program.</p><p><strong>Results: </strong>The fraction containing the Kunitz molecule presented similar inhibition of both elastase-1 and cathepsin L. This Kunitz-type peptide was characterized as an uncompetitive inhibitor for elastase-1, presenting an inhibition constant (K_i) of 8 μM. The docking analysis led us to synthesize two peptides: PEP1, which was substrate for both elastase-1 and cathepsin L, and PEP2, a 30-mer cyclic peptide, which showed to be a cathepsin L competitive inhibitor, with a K_i of 1.96 µM, and an elastase-1 substrate.</p><p><strong>Conclusion: </strong>This work describes a Kunitz-type peptide toxin presenting inhibitory potential over serine and cysteine proteases, and this could contribute to further understand the envenomation process by <i>D. polylepis</i>. In addition, the PEP2 inhibits the cathepsin L activity with a low inhibition constant.</p>","PeriodicalId":17565,"journal":{"name":"Journal of Venomous Animals and Toxins Including Tropical Diseases","volume":"26 ","pages":"e20200037"},"PeriodicalIF":2.4,"publicationDate":"2020-10-07","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7546081/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"38516662","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Comparative gender peptidomics of <i>Bothrops atrox</i> venoms: are there differences between them?","authors":"Adriana Simizo, Eduardo S Kitano, Sávio S Sant'Anna, Kathleen Fernandes Grego, Anita Mitico Tanaka-Azevedo, Alexandre K Tashima","doi":"10.1590/1678-9199-JVATITD-2020-0055","DOIUrl":"10.1590/1678-9199-JVATITD-2020-0055","url":null,"abstract":"<p><strong>Background: </strong><i>Bothrops atrox</i> is known to be the pit viper responsible for most snakebites and human fatalities in the Amazon region. It can be found in a wide geographical area including northern South America, the east of Andes and the Amazon basin. Possibly, due to its wide distribution and generalist feeding, intraspecific venom variation was reported by previous proteomics studies. Sex-based and ontogenetic variations on venom compositions of <i>Bothrops</i> snakes were also subject of proteomic and peptidomic analysis. However, the venom peptidome of <i>B. atrox</i> remains unknown.</p><p><strong>Methods: </strong>We conducted a mass spectrometry-based analysis of the venom peptides of individual male and female specimens combining bottom-up and top-down approaches.</p><p><strong>Results: </strong>We identified in <i>B. atrox</i> a total of 105 native peptides in the mass range of 0.4 to 13.9 kDa. Quantitative analysis showed that phospholipase A₂ and bradykinin potentiating peptides were the most abundant peptide families in both genders, whereas disintegrin levels were significantly increased in the venoms of females. Known peptides processed at non-canonical sites and new peptides as the Ba1a, which contains the SVMP BATXSVMPII1 catalytic site, were also revealed in this work.</p><p><strong>Conclusion: </strong>The venom peptidomes of male and female specimens of <i>B. atrox</i> were analyzed by mass spectrometry-based approaches in this work. The study points to differences in disintegrin levels in the venoms of females that may result in distinct pathophysiology of envenomation. Further research is required to explore the potential biological implications of this finding.</p>","PeriodicalId":17565,"journal":{"name":"Journal of Venomous Animals and Toxins Including Tropical Diseases","volume":"26 ","pages":"e20200055"},"PeriodicalIF":2.4,"publicationDate":"2020-10-07","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7546584/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"38516664","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}