Systemic alterations induced by a Bothrops alternatus hemorrhagic metalloproteinase (baltergin) in mice

Maruñak, Silvana; Teibler, Pamela; Ruíz, Raquel; Pérez, O.C. Acosta de; Leiva, Laura

doi:10.1016/j.toxicon.2008.10.010

Cited by 34 publications

(22 citation statements)

References 20 publications

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“…Nevertheless, in the present study, the activity levels differed between those two species, a fact that might be attributable to the use of crude venom rather than purified enzymes. Despite the relatively low overall enzymatic activity observed in our study, B. alternatus bites have often been reported to cause local tissue damage, hemorrhage, coagulation disorders, respiratory failure, renal failure, and shock (Gay et al, 2009). …”

Section: Discussioncontrasting

confidence: 59%

In vitro comparison of enzymatic effects among Brazilian Bothrops spp. venoms

Campos

Pucca

Roncolato

et al. 2013

Toxicon

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In various types of snake venom, the major toxic components are proteinases and members of the phospholipase A2 family, although other enzymes also contribute to the toxicity. In this study, we evaluated the proteolytic, phospholipase, and L-Amino acid oxidase activities in the venom of five Bothrops species-Bothrops jararaca, Bothrops jararacussu, Bothrops moojeni, Bothrops neuwiedi, and Bothrops alternatus-all of which are used in the production of commercial antivenom, prepared in horses. The enzymatic activities of each species' venom were classified as high, moderate, or low. B. moojeni venom demonstrated the highest enzymatic activity profile, followed by the venom of B. neuwiedi, B. jararacussu, B. jararaca, and B. alternatus. To our knowledge, this is the first study to compare all of these enzymes from multiple species, which is significant in view of the activity of L-amino acid oxidase across Bothrops species.

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Section: Discussioncontrasting

confidence: 59%

In vitro comparison of enzymatic effects among Brazilian Bothrops spp. venoms

Campos

Pucca

Roncolato

et al. 2013

Toxicon

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“…Alternagin inhibits the binding of K562 cells to collagen by selectively blocking α 2 β 1 integrin, in a manner similar to jararhagin from B. jararaca venom; this inhibitory action is apparently mediated by alternagin-C. Subsequently, Gay et al [44,45] also isolated alternagin (which they termed balteragin) from Argentine B. alternatus . This protein causes edema, hemorrhage and necrosis when administered intramuscularly in mice, and systemic hemorrhage, primarily in the lungs, kidneys and liver, when administered intravenously.…”

Section: Resultsmentioning

confidence: 99%

A transcriptomic analysis of gene expression in the venom gland of the snake Bothrops alternatus (urutu)

et al. 2010

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BackgroundThe genus Bothrops is widespread throughout Central and South America and is the principal cause of snakebite in these regions. Transcriptomic and proteomic studies have examined the venom composition of several species in this genus, but many others remain to be studied. In this work, we used a transcriptomic approach to examine the venom gland genes of Bothrops alternatus, a clinically important species found in southeastern and southern Brazil, Uruguay, northern Argentina and eastern Paraguay.ResultsA cDNA library of 5,350 expressed sequence tags (ESTs) was produced and assembled into 838 contigs and 4512 singletons. BLAST searches of relevant databases showed 30% hits and 70% no-hits, with toxin-related transcripts accounting for 23% and 78% of the total transcripts and hits, respectively. Gene ontology analysis identified non-toxin genes related to general metabolism, transcription and translation, processing and sorting, (polypeptide) degradation, structural functions and cell regulation. The major groups of toxin transcripts identified were metalloproteinases (81%), bradykinin-potentiating peptides/C-type natriuretic peptides (8.8%), phospholipases A2 (5.6%), serine proteinases (1.9%) and C-type lectins (1.5%). Metalloproteinases were almost exclusively type PIII proteins, with few type PII and no type PI proteins. Phospholipases A2 were essentially acidic; no basic PLA2 were detected. Minor toxin transcripts were related to L-amino acid oxidase, cysteine-rich secretory proteins, dipeptidylpeptidase IV, hyaluronidase, three-finger toxins and ohanin. Two non-toxic proteins, thioredoxin and double-specificity phosphatase Dusp6, showed high sequence identity to similar proteins from other snakes. In addition to the above features, single-nucleotide polymorphisms, microsatellites, transposable elements and inverted repeats that could contribute to toxin diversity were observed.ConclusionsBothrops alternatus venom gland contains the major toxin classes described for other Bothrops venoms based on trancriptomic and proteomic studies. The predominance of type PIII metalloproteinases agrees with the well-known hemorrhagic activity of this venom, whereas the lower content of serine proteases and C-type lectins could contribute to less marked coagulopathy following envenoming by this species. The lack of basic PLA2 agrees with the lower myotoxicity of this venom compared to other Bothrops species with these toxins. Together, these results contribute to our understanding of the physiopathology of envenoming by this species.

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“…However, the systemic injection of baltergin, a purified metalloproteinase from B. alternatus venom, only mildly affected the kidney structure. At high doses, baltergin causes congestion, subcapsular hemorrhage and inflammatory infiltrate (Gay et al, 2009). There was no detection of tubular necrosis indicating that different toxins act synergistically to produce the AKI observed in animals treated with whole venom.…”

Section: Bothrops Venommentioning

confidence: 99%