Prospection, structural analysis and phylogenetic relationships of endogenous γ-phospholipase A2 inhibitors in Brazilian Bothrops snakes (Viperidae, Crotalinae)

Estevão-Costa, Maria Inácia; Rocha, Bruno Coelho; Mudado, Mauricio de Alvarenga; Redondo, Rodrigo A. F.; Franco, Glória Regina; Fortes-Dias, Consuelo Latorre

doi:10.1016/j.toxicon.2008.04.167

Cited by 28 publications

(41 citation statements)

References 28 publications

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“…)[61] Bothrops jararacussu Jararacussu (Port. )[22], [61] Bothrops neuwiedi Jararaca pintada (Port. )[61] Cerrophidion godmani Honduras montane pit viper[21] Crotalus durissus collilineatus Brazilian rattlesnake[71] Crotalus durissus terrificus South American rattlesnake, tropical rattlesnake[51–53] Lachesis muta South American bushmaster[72] Gloydius brevicaudus Short-tailed mamushi, Japanese mamushi or Chinese mamushi[73] Protobothrops flavoviridis Habu[25] Protobothrops elegans Sakishima habu[41]

a Recombinant homolog

…”

Section: Gamma Class Of Sbplis (Sbγplis)mentioning

confidence: 99%

Endogenous phospholipase A2 inhibitors in snakes: a brief overview

Campos-Júnior

Melo

Dias

et al. 2016

J Venom Anim Toxins Incl Trop Dis

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The blood plasma of numerous snake species naturally comprises endogenous phospholipase A2 inhibitors, which primarily neutralize toxic phospholipases A2 that may eventually reach their circulation. This inhibitor type is generally known as snake blood phospholipase A2 inhibitors (sbPLIs). Most, if not all sbPLIs are oligomeric glycosylated proteins, although the carbohydrate moiety may not be essential for PLA2 inhibition in every case. The presently known sbPLIs belong to one of three structural classes – namely sbαPLI, sbβPLI or sbγPLI – depending on the presence of characteristic C-type lectin-like domains, leucine-rich repeats or three-finger motifs, respectively. Currently, the most numerous inhibitors described in the literature are sbαPLIs and sbγPLIs, whereas sbβPLIs are rare. When the target PLA2 is a Lys49 homolog or an Asp49 myotoxin, the sbPLI is denominated a myotoxin inhibitor protein (MIP). In this brief overview, the most relevant data on sbPLIs will be presented. Representative examples of sbαPLIs and sbγPLIs from two Old World – Gloydius brevicaudus and Malayopython reticulatus – and two New World – Bothrops alternatus and Crotalus durissus terrificus – snake species will be emphasized.

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a Recombinant homolog

…”

Section: Gamma Class Of Sbplis (Sbγplis)mentioning

confidence: 99%

Endogenous phospholipase A2 inhibitors in snakes: a brief overview

Campos-Júnior

Melo

Dias

et al. 2016

J Venom Anim Toxins Incl Trop Dis

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“…Estevão-Costa et al (36) studied phospholipase A 2 inhibitors (PLIs) present in snake serum. Three different structural classes of PLIs (α, β, and γ) were noted from the study.…”

Section: Overview On Bothrops Erythromelas Venommentioning

confidence: 99%

An overview of Bothrops erythromelas venom

Néry

Luna

Fernandes

et al. 2016

Rev. Soc. Bras. Med. Trop.

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This review discusses studies on the venom of Bothrops erythromelas published over the past 36 years. During this period, many contributions have been made to understand the venomous snake, its venom, and its experimental and clinical effects better. The following chronological overview is based on 29 articles that were published between 1979 and 2015, with emphasis on diverse areas. The complexity of this task demands an integration of multidisciplinary research tools to study toxinology. This science is in need of renewed conceptual and experimental platforms aimed at obtaining a profound understanding of the highly complex pathophysiology of snakebite envenoming and toxins isolated from snakes.

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“…The B. jararaca scenario has allowed us to explore uncharted territory, as this organism has an incomplete sequence database and we were therefore required to rely on those of orthologous organisms. In particular, B. jararaca plasma was chosen because it is a main research model studied at the Laboratory of Toxinology (FIOCRUZ, Brazil), and several natural inhibitors of snake toxins have already been identified/characterized from this biological matrix (35)(36)(37). (38), and 40 g were processed to complete dryness via lyophilization.…”

mentioning

confidence: 99%

PepExplorer: A Similarity-driven Tool for Analyzing de Novo Sequencing Results

Leprevost

Valente

Lima

et al. 2014

Molecular & Cellular Proteomics

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Peptide spectrum matching is the current gold standard for protein identification via mass-spectrometry-based proteomics. Peptide spectrum matching compares experimental mass spectra against theoretical spectra generated from a protein sequence database to perform identification, but protein sequences not present in a database cannot be identified unless their sequences are in part conserved. The alternative approach, de novo sequencing, can make it possible to infer a peptide sequence directly from a mass spectrum, but interpreting long lists of peptide sequences resulting from large-scale experiments is not trivial. With this as motivation, PepExplorer was developed to use rigorous pattern recognition to assemble a list of homologue proteins using de novo sequencing data coupled to sequence alignment to allow biological interpretation of the data. PepExplorer can read the output of various widely adopted de novo sequencing tools and converge to a list of proteins with a global false-discovery rate. To this end, it employs a radial basis function neural network that considers precursor charge states, de novo sequencing scores, peptide lengths, and alignment scores to select similar protein candidates, from a target-decoy database, usually obtained from phylogenetically related species. Alignments are performed using a modified Smith-Waterman algorithm tailored for the task at hand. We verified the effectiveness of our approach using a reference set of identifications generated by ProLuCID when searching for Pyrococcus furiosus mass spectra on the corresponding NCBI RefSeq database. We then modified the sequence database by swapping amino acids until ProLuCID was no longer capable of identifying any proteins. By searching the mass spectra using PepExplorer on the modified database, we were able to recover most of the identifications at a 1% false-discovery rate. Finally, we employed PepExplorer to disclose a comprehensive proteomic assessment of the Bothrops jararaca plasma, a known biological source of natural inhibitors of snake toxins. PepExplorer is integrated into the PatternLab for Proteomics environment, which makes available various tools for downstream data analysis, including resources for quantitative and differential proteomics. Molecular & Cellular

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Prospection, structural analysis and phylogenetic relationships of endogenous γ-phospholipase A2 inhibitors in Brazilian Bothrops snakes (Viperidae, Crotalinae)

Cited by 28 publications

References 28 publications

Endogenous phospholipase A2 inhibitors in snakes: a brief overview

Endogenous phospholipase A2 inhibitors in snakes: a brief overview

An overview of Bothrops erythromelas venom

PepExplorer: A Similarity-driven Tool for Analyzing de Novo Sequencing Results

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