Bothrops insularis venomics: A proteomic analysis supported by transcriptomic-generated sequence data

Valente, Richard H.; Guimarães, Patricia Ramos; Junqueira, Magno; Neves-Ferreira, Ana Gisele C.; Soares, Márcia Regina; Chapeaurouge, Alex; Trugilho, Monique Ramos de Oliveira; León, Ileana R.; Rocha, Surza Lucia Gonçalves da; Oliveira-Carvalho, Ana Lúcia; Wermelinger, Luciana S.; Dutra, Denis L. S.; Leão, Luciana I.; Junqueira-de-Azevedo, Inácio L.M.; Ho, Paulo Lee; Zingali, Russolina B.; Perales, Jonás; Domont, Gilberto B.

doi:10.1016/j.jprot.2009.01.001

Cited by 96 publications

(87 citation statements)

References 71 publications

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“…It is not common to obtain high quality MS/MS spectra by CID fragmentation from highly charged peptides (Ͼ ϩ3) (55, 56), however, for this 39-residue peptide with charge ϩ5 the complete y-series and part of the b-series were obtained, allowing its complete sequencing. Moreover, other LAAO fragments have been found in the venoms of BC, BF and BJ (Table I), similarly as previously described in the venoms of B. moojeni (31,57) and B. insularis (58). All other peptides found by de novo sequencing were homologous or identical to sequences present in the BPP-CNP precursor which is composed of seven BPP molecules aligned in tandem after a hydrophobic signal peptide sequence, followed by a putative intervening sequence and a C-type natriuretic peptide at the C terminus (59).…”

Section: De Novo Sequencing Of Peptides Present In the Venomssupporting

confidence: 79%

Peptidomics of Three Bothrops Snake Venoms: Insights Into the Molecular Diversification of Proteomes and Peptidomes

Tashima

Zelanis

Kitano

et al. 2012

Molecular & Cellular Proteomics

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Snake venom proteomes/peptidomes are highly complex and maintenance of their integrity within the gland lumen is crucial for the expression of toxin activities. There has been considerable progress in the field of venom proteomics, however, peptidomics does not progress as fast, because of the lack of comprehensive venom sequence databases for analysis of MS data. Therefore, in many cases venom peptides have to be sequenced manually by MS/MS analysis or Edman degradation. This is critical for rare snake species, as is the case of Bothrops cotiara (BC) and B. fonsecai (BF), which are regarded as near threatened with extinction. In this study we conducted a comprehensive analysis of the venom peptidomes of BC, BF, and B. jararaca (BJ) using a combination of solid-phase extraction and reversed-phase HPLC to fractionate the peptides, followed by nano-liquid chromatography-tandem MS (LC-MS/MS) or direct infusion electrospray ionization-(ESI)-MS/MS or MALDI-MS/MS analyses. We detected marked differences in the venom peptidomes and identified peptides ranging from 7 to 39 residues in length by de novo sequencing. Forty-four unique sequences were manually identified, out of which 30 are new peptides, including 17 bradykinin-potentiating peptides, three poly-histidine-poly-glycine peptides and interestingly, 10 L-amino acid oxidase fragments. Some of the new bradykinin-potentiating peptides display significant bradykinin potentiating activity. Automated database search revealed fragments from several toxins in the peptidomes, mainly from L-amino acid oxidase, and allowed the determination of the peptide bond specificity of proteinases and amino acid occurrences for the P4-P4 sites. We also demonstrate that the venom lyophilization/resolubilization process greatly increases the complexity of the peptidome because of the imbalance caused to the venom proteome and the consequent activity of proteinases on venom components. The use of proteinase inhibitors clearly showed different outcomes in the peptidome characterization and suggested that degradomic-peptidomic analysis of snake venoms is highly sensitive to the conditions of sampling procedures. Molecular & Cellular Proteomics 11: 10.1074/mcp.M112.019331, 1245-1262, 2012.Snake venoms are the products of specialized secretory glands located above the upper jawbone in venomous snakes. Like most secretory proteins, venom toxins are synthesized in the cytoplasm of secretory cells in the gland and transferred to the rough endoplasmic reticulum, then to the Golgi apparatus, and finally transported via secretory granules to the lumen of the venom gland (1). The snake venomous secretion is an aqueous solution containing a high amount of proteins and peptides, however the mechanisms for controlling protein secretion into the gland lumen and for regulating its protein/peptide concentration, ionic strength, and pH are unknown. As in all eukaryotic cells the proteomes of the venom gland tissue are highly complex, comprising a much great number and diversity of multidomain proteins (2...

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Section: De Novo Sequencing Of Peptides Present In the Venomssupporting

confidence: 79%

Peptidomics of Three Bothrops Snake Venoms: Insights Into the Molecular Diversification of Proteomes and Peptidomes

Tashima

Zelanis

Kitano

et al. 2012

Molecular & Cellular Proteomics

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“…Bothrops jararaca (B. jararaca) é uma espécie predominantemente noturna e terrestre (Sazima, 1988) e encontra-se em diversos ambientes: florestas tropicais, semitropicais, campos abertos e cerrados (SAZIMA, 1992 SANO-MARTINS et al, 1997;SANTORO;SANO-MARTINS, 2004;VARANDA;GIANNINI, 1999).…”

Section: Bothrops Jararacaunclassified

“…Além dessas moléculas, existe ainda uma variedade de enzimas e peptídeos encontrados nos venenos das serpentes do gênero Bothrops, como apresentados no quadro 1 (Junqueira-de-Azevedo;Ho, 2002;Kashima et al, 2004;Cidade et al, 2006, Valente et al, 2009Cardoso et al, 2010;Rodrigues et al, 2012;Zelanis et al, 2012).…”

Section: Moléculas Do Veneno De Serpentesunclassified

“…Essas proteínas são amplamente distribuídas no veneno de lagartos e de serpentes, inclusive do gênero Bothrops (CARDOSO et al, 2010;CIDADE et al, 2006;JUNQUEIRA-DE-AZEVEDO & HO, 2002;VALENTE et al, 2009 AZEVEDO et al, 2001;SUTO et al, 2005;TOKUNAGA;MORITA, 2005;TRUMMAL et al, 2011;ZELANIS et al, 2012).…”

Section: Proteínas Secretórias Ricas Em Cisteína (Crisps)unclassified

“…P (pré-domínio); Pro (pró-domínio); Proteinase (domínio metaloproteases); S (domínio espaçador); Dis (domínio desintegrina); Dis-like (domínio semelhante à desintegrina); Cys-rich (domínio rico em cisteína); Lec (domínio semelhante à lectina); SVMPs P-III do veneno da C. atrox (VAP); Ativador do fator X da víbora Lebetina (VLFXA). Fonte: Modificado de Fox e As SVMPs correspondem a cerca de 30% da composição do veneno das Viperidae (CIDADE et al, 2006;JUNQUEIRA-DE-AZEVEDO;HO, 2002;TERRA et al, 2009;VALENTE et al, 2009), sugerindo um papel importante no processo de envenenamento. Essas enzimas estão relacionadas à toxicidade do veneno com funções na formação de edema, na inflamação, no sangramento, na coagulação intravascular e na necrose (BJARNASON;FOX, 1994;SERRANO, 2009;TAKEDA;IWANAGA, 2012).…”

Section: Metaloproteasesunclassified

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Análise do transcriptoma do fígado da serpente Bothrops jararaca utilizando expressed sequences tags (ESTs).

Gomes¹

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amo, meu porto seguro. Aos meus pais Antônia Maria da Silva Gomes e José Geraldo Gomes, que sempre acreditaram em mim, e sempre fizeram o melhor pela minha educação.Às minhas irmãs Cristiane Maria Gomes e Thais Maria Gomes, minhas companheiras de sempre.Sem vocês nada disso seria possível. E claro ao meu cachorro Theo por sua alegria toda vez que chego em casa." "In memoriam de Faustemira das GraçasCruz Alves Pereira que rezou por mim e me deu força para continuar em meu caminho." AGRADECIMENTOSGostaria de agradecer a todos que direta ou indiretamente tenham contribuído para o término do mestrado e especialmente para a conclusão deste trabalho, que é apenas o início de um longo caminho a ser percorrido, a começar pela minha orientadora Dra. Anita Mitico Tanaka-Azevedo pelos seus ensinamentos, por ter confiado a mim este trabalho e por ter me aceito no seu grupo de trabalho com quem tive a oportunidade de aprender muito, e foi muito importante para o meu crescimento profissional.À Professora Dra. Aparecida Sadae Tanaka, minha co-orientadora, que me acompanhou durante toda a realização deste trabalho, por seu exemplo de profissionalismo, seriedade à pesquisa, e por sempre me fazer enxergar mais longe.Ao amigo Dr. Diego de Souza Buarque que me acompanhou durante todas as fases deste trabalho, obrigada por sua ajuda e companhia em todos os momentos, "inclusive quando escapamos do raio". Obrigada pela paciência.Aos amigos Tatiane Sanches Soares e Felipe Araújo de Oliveira, meus parceiros de todos os momentos, "meu triângulo", obrigada por poder sempre contar com vocês e por vocês sempre me aguentarem durante meus momentos, sou privilegiada por poder contar com vocês! A todos os companheiros do laboratório do Infar e do Instituto Butantan que me ajudaram de diferentes maneiras durante a realização deste trabalho, Gabriela Catalano, Lucyla Tiemi "que sempre tem uma bala para mim", Patrícia Andrade, Thyago Cardoso "por me fazer sempre rir", Stephen Lu, Karla Oliveira, Ricardo Torquato e Karen de Morais Zani. À Dra Kathleen Fernandes Grego do Laboratório de Herpetologia do InstitutoButantan, pela ajuda na coleta do fígado das serpentes B. jararaca. À Professora Glória por sua colaboração e orientação na parte de bioinformática.Aos funcionários do Infar, em especial à técnica Jucilene Barbosa da Silva, pelo sequenciamento e por sua amizade.Às minhas amigas, Andréa Carvalho e Fernanda Soma por sempre me entenderem e me apoiarem durante todas as fases deste trabalho, que sempre estiveram presentes, mesmo à distância quando eu precisava, e sempre me fizeram companhia, à nossas tardes na Starbucks, aos filmes e, claro, aos shows que sempre fizeram parte dessas nossas histórias. Valeu meninas! À minha eterna amiga Tais Costa de Oliveira, que mesmo eu estando longe, e não muito presente, ainda é minha amiga, que mesmo me achando "louca" ainda assim consegue me entender. Porque amizade é assim! Aos meus amigos do Laboratório de Genética do Instituto Butantan, Dra. Sueli "Sesso", Fernando e Prof. Dr. Carlos Marandová, que não est...

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Photobiomodulation Therapy to Treat Snakebites Caused by Bothrops atrox

Carvalho,

Souza,

Melo

et al. 2024

JAMA Intern Med

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ImportanceBothrops venom acts almost immediately at the bite site and causes tissue damage.ObjectiveTo investigate the feasibility and explore the safety and efficacy of low-level laser therapy (LLLT) in reducing the local manifestations of B atrox envenomations.Design, Setting, and ParticipantsThis was a double-blind randomized clinical trial conducted at Fundação de Medicina Tropical Doutor Heitor Vieira Dourado, in Manaus, Brazil. A total of 60 adult participants were included from November 2020 to March 2022, with 30 in each group. Baseline characteristics on admission were similarly distributed between groups. Data analysis was performed from August to December 2022.InterventionThe intervention group received LLLT combined with regular antivenom treatment. The laser used was a gallium arsenide laser with 4 infrared laser emitters and 4 red laser emitters, 4 J/cm2 for 40 seconds at each application point.Main Outcomes and MeasuresFeasibility was assessed by eligibility, recruitment, and retention rates; protocol fidelity; and patients’ acceptability. The primary efficacy outcome of this study was myolysis estimated by the value of creatine kinase (U/L) on the third day of follow-up. Secondary efficacy outcomes were (1) pain intensity, (2) circumference measurement ratio, (3) extent of edema, (4) difference between the bite site temperature and that of the contralateral limb, (5) need for the use of analgesics, (6) frequency of secondary infections, and (7) necrosis. These outcomes were measured 48 hours after admission. Disability assessment was carried out from 4 to 6 months after patients’ discharge. P values for outcomes were adjusted with Bonferroni correction.ResultsA total of 60 patients (mean [SD] age, 43.2 [15.3] years; 8 female individuals [13%] and 52 male individuals [87%]) were included. The study was feasible, and patient retention and acceptability were high. Creatine kinase was significantly lower in the LLLT group (mean [SD], 163.7 [160.0] U/L) 48 hours after admission in relation to the comparator (412.4 [441.3] U/L) (P = .03). Mean (SD) pain intensity (2.9 [2.7] vs 5.0 [2.4]; P = .004), circumference measurement ratio (6.6% [6.6%] vs 17.1% [11.6%]; P &lt; .001), and edema extent (25.8 [15.0] vs 40.1 [22.7] cm; P = .002) were significantly lower in the LLLT group in relation to the comparator. No difference was observed between the groups regarding the mean difference between the bite site temperature and the contralateral limb. Secondary infections, necrosis, disability outcomes, and the frequency of need for analgesics were similar in both groups. No adverse event was observed.Conclusions and RelevanceThe data from this randomized clinical trial suggest that the use of LLLT was feasible and safe in a hospital setting and effective in reducing muscle damage and the local inflammatory process caused by B atrox envenomations.Trial RegistrationBrazilian Registry of Clinical Trials Identifier: RBR-4qw4vf

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Bothrops insularis venomics: A proteomic analysis supported by transcriptomic-generated sequence data

Cited by 96 publications

References 71 publications

Peptidomics of Three Bothrops Snake Venoms: Insights Into the Molecular Diversification of Proteomes and Peptidomes

Peptidomics of Three Bothrops Snake Venoms: Insights Into the Molecular Diversification of Proteomes and Peptidomes

Análise do transcriptoma do fígado da serpente Bothrops jararaca utilizando expressed sequences tags (ESTs).

Photobiomodulation Therapy to Treat Snakebites Caused by Bothrops atrox

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