Intra-specific variation in venom of the African Puff Adder (Bitis arietans): Differential expression and activity of snake venom metalloproteinases (SVMPs)

Currier, Rachel B.; Harrison, Robert A.; Rowley, Paul D.; Laing, G.D.; Wagstaff, Simon C.

doi:10.1016/j.toxicon.2009.12.009

Cited by 72 publications

(72 citation statements)

References 21 publications

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“…Geographical variation of venom composition occurs in some snakes and is suggested to evolve in response to changes in diets [11,[15][16][17]. Cone snails (of the family Conidae) are predatory gastropods that use a venom primarily to capture prey.…”

Section: Introductionmentioning

confidence: 99%

Effects of geographical heterogeneity in species interactions on the evolution of venom genes

2015

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Geographical heterogeneity in the composition of biotic interactions can create a mosaic of selection regimes that may drive the differentiation of phenotypes that operate at the interface of these interactions. Nonetheless, little is known about effects of these geographical mosaics on the evolution of genes encoding traits associated with species interactions. Predatory marine snails of the family Conidae use venom, a cocktail of conotoxins, to capture prey. We characterized patterns of geographical variation at five conotoxin genes of a vermivorous species, Conus ebraeus, at Hawaii, Guam and American Samoa, and evaluated how these patterns of variation are associated with geographical heterogeneity in prey utilization. All populations show distinct patterns of prey utilization. Three 'highly polymorphic' conotoxin genes showed significant geographical differences in allelic frequency, and appear to be affected by different modes of selection among populations. Two genes exhibited low levels of diversity and a general lack of differentiation among populations. Levels of diversity of 'highly polymorphic' genes exhibit a positive relationship with dietary breadth. The different patterns of evolution exhibited by conotoxin genes suggest that these genes play different roles in prey capture, and that some genes are more greatly affected by differences in predator-prey interactions than others. Moreover, differences in dietary breadth appear to have a greater influence on the differentiation of venoms than differences in the species of prey.

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Section: Introductionmentioning

confidence: 99%

Effects of geographical heterogeneity in species interactions on the evolution of venom genes

2015

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“…In most instances, proteomic/peptidomic analyses of snake venoms are conducted using pooled samples from many specimens to overcome the well documented individual variability that occurs both at the protein and peptide levels (38,42,43). Moreover, fresh venom samples are usually lyophilized to preserve the structural integrity of proteins.…”

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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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“…The physiopathological effects of venom results from synergic action of the composite mixture (Currier et al, 2010). The amount of snake venom component depends on the snake species, diet, season and geographical regions (Rodrgues et al, 1998;Currier et al, 2010).…”

Section: Introductionmentioning

confidence: 99%

Spectrophotometric study of the anti-caseinolytic activity of root extracts of Teclea nobilis and Vepris zambesiaca on Bitis arietans venom

Chayamiti¹

2013

Afr. J. Pharm. Pharmacol.

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Intra-specific variation in venom of the African Puff Adder (Bitis arietans): Differential expression and activity of snake venom metalloproteinases (SVMPs)

Cited by 72 publications

References 21 publications

Effects of geographical heterogeneity in species interactions on the evolution of venom genes

Effects of geographical heterogeneity in species interactions on the evolution of venom genes

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

Spectrophotometric study of the anti-caseinolytic activity of root extracts of Teclea nobilis and Vepris zambesiaca on Bitis arietans venom

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