Proteolytic action of Bothrops jararaca venom upon its own constituents

Sousa, Juliana do Nascimento; Monteiro, Robson Q.; Castro, Helena C.; Zingali, Russolina B.

doi:10.1016/s0041-0101(00)00208-7

Cited by 29 publications

(14 citation statements)

References 23 publications

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“…Non-labeled peaks in panels D and E are autodegradation products from the SE venom. The autoproteolytic action of B. jararaca venom from the SE population upon incubation for 48 h at acidic (pH 5.0) or alkaline (8.5) pH has been previously reported by Sousa and co-workers [112]. …”

supporting

confidence: 58%

Combined venomics, venom gland transcriptomics, bioactivities, and antivenomics of two Bothrops jararaca populations from geographic isolated regions within the Brazilian Atlantic rainforest

Machado

Plá

Sanz

et al. 2016

Journal of Proteomics

119

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supporting

confidence: 58%

Combined venomics, venom gland transcriptomics, bioactivities, and antivenomics of two Bothrops jararaca populations from geographic isolated regions within the Brazilian Atlantic rainforest

Machado

Plá

Sanz

et al. 2016

Journal of Proteomics

119

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“…Firstly, lyophilisation and preservation of venom may initially prevent degradation of venom components, although mRNAs found specifically in venom could have unique properties leading to an unusual long-term stability. Physiochemical properties of venom, including the presence of high concentrations of citrate [30]–[32] and a weakly acidic pH [33]–[34] [5], may provide universal stability to many venom components. Finally, there is evidence for toxin-specific inhibitors in venom such as the QKW tri-peptide inhibitors of SVMPs [15], and such specific or non-specific inhibitors may play a role in stabilising other components of venom, including mRNAs.…”

Section: Discussionmentioning

confidence: 99%

Unusual Stability of Messenger RNA in Snake Venom Reveals Gene Expression Dynamics of Venom Replenishment

et al. 2012

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Venom is a critical evolutionary innovation enabling venomous snakes to become successful limbless predators; it is therefore vital that venomous snakes possess a highly efficient venom production and delivery system to maintain their predatory arsenal. Here, we exploit the unusual stability of messenger RNA in venom to conduct, for the first time, quantitative PCR to characterise the dynamics of gene expression of newly synthesised venom proteins following venom depletion. Quantitative PCR directly from venom enables real-time dynamic studies of gene expression in the same animals because it circumvents the conventional requirement to sacrifice snakes to extract mRNA from dissected venom glands. Using qPCR and proteomic analysis, we show that gene expression and protein re-synthesis triggered by venom expulsion peaks between days 3–7 of the cycle of venom replenishment, with different protein families expressed in parallel. We demonstrate that venom re-synthesis occurs very rapidly following depletion of venom stores, presumably to ensure venomous snakes retain their ability to efficiently predate and remain defended from predators. The stability of mRNA in venom is biologically fascinating, and could significantly empower venom research by expanding opportunities to produce transcriptomes from historical venom stocks and rare or endangered venomous species, for new therapeutic, diagnostic and evolutionary studies.

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“…Protein Identifications in the Venoms Fractionated in the Presence of Proteinase Inhibitors-Viperid snake venoms possess high amounts of proteolytic enzymes (SVMPs and SVSPs), however there are protection mechanisms in the venom solution to avoid self-proteolysis (3,88,89). The proteolytic enzymes have optimal activity at alkaline pH (8 -9), whereas the pH of the venom solution is slightly acidic.…”

Section: De Novo Sequencing Of Peptides Present In the Venomsmentioning

confidence: 99%

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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Proteolytic action of Bothrops jararaca venom upon its own constituents

Cited by 29 publications

References 23 publications

Combined venomics, venom gland transcriptomics, bioactivities, and antivenomics of two Bothrops jararaca populations from geographic isolated regions within the Brazilian Atlantic rainforest

Combined venomics, venom gland transcriptomics, bioactivities, and antivenomics of two Bothrops jararaca populations from geographic isolated regions within the Brazilian Atlantic rainforest

Unusual Stability of Messenger RNA in Snake Venom Reveals Gene Expression Dynamics of Venom Replenishment

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

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