Bothrops jararaca venom gland transcriptome: Analysis of the gene expression pattern

Cidade, Daniela A.P.; Simão, Tatiana de Almeida; Dávila, Alberto M. R.; Wagner, Glauber; Junqueira-de-Azevedo, Inácio L.M.; Ho, Paulo Lee; Bon, Cassian; Zingali, Russolina B.; Albano, Rodolpho Mattos

doi:10.1016/j.toxicon.2006.07.008

Cited by 124 publications

(122 citation statements)

References 75 publications

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“…72 All phylogenies indicate an early cladogenetic event splitting New Word pitvipers into temperate (Agkistrodon, Crotalus, and Sistrurus) and Neotropical (bothropoid genera and Lachesis) groups. 13 The lack of evidence for the occurrence of Kazal-type proteins (or messengers) in the venom proteomes and transcriptomes of species of genera Agkistrodon, 34,35 Sistrurus, 22,24 Bothrops, 26,[31][32][33] and Lachesis, 37 would support the hypothesis B. schlegelii(B).…”

Section: )Ecesgdccdqcrmentioning

confidence: 99%

Snake Venomics and Antivenomics of the Arboreal Neotropical Pitvipers Bothriechis lateralis and Bothriechis schlegelii

et al. 2008

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We report the comparative proteomic characterization of the venoms of two related neotropical arboreal pitvipers from Costa Rica of the genus Bothriechis, B. lateralis (side-striped palm pit viper) and B. schlegelii (eyelash pit viper). The crude venoms were fractionated by reverse-phase HPLC, followed by analysis of each chromatographic fraction by SDS-PAGE, N-terminal sequencing, MALDI-TOF mass fingerprinting, and collision-induced dissociation tandem mass spectrometry of tryptic peptides. The venom proteomes of B. lateralis and B. schlegelii comprise similar number of distinct proteins belonging, respectively, to 8 and 7 protein families. The two Bothriechis venoms contain bradykinin-potentiating peptides (BPPs), and proteins from the phospholipase A 2 (PLA 2 ), serine proteinase, L-amino acid oxidase (LAO), cysteine-rich secretory protein (CRISP), and Zn 2+ -dependent metalloproteinase (SVMP) families, albeit each species exhibit different relative abundances. Each venom also contains unique components, for example, snake venom vascular endothelial growth factor (svVEGF) and C-type lectin-like molecules in B. lateralis, and Kazal-type serine proteinase inhibitor-like proteins in B. schlegelii. Using a similarity coefficient, we estimate that the similarity of the venom proteins between the two Bothriechis taxa may be <10%, indicating a high divergence in their venom compositions, in spite of the fact that both species have evolved to adapt to arboreal habits. The major toxin families of B. lateralis and B. schlegelii are SVMP (55% of the total venom proteins) and PLA 2 (44%), respectively. Their different venom toxin compositions provide clues for rationalizing the distinct signs of envenomation caused by B. schlegelii and B. lateralis. An antivenomic study of the immunoreactivity of the Instituto Clodomiro Picado (ICP) polyvalent antivenom toward Bothriechis venoms revealed that L-amino acid oxidase and SVMPs represent the major antigenic protein species in both venoms. Our results provide a ground for rationalizing the reported protection of the ICP polyvalent antivenom against the hemorrhagic, coagulant, defibrinating, caseinolytic and fibrin(ogen)olytic activities of Bothriechis (schlegelii, lateralis) venoms. However, these analyses also evidenced the limited recognition capability of the polyvalent antivenom toward a number of Bothriechis venom components, predominantly BPPs, svVEGF, Kazal-type inhibitors, some PLA 2 proteins, some serine proteinases, and CRISP molecules.

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Section: )Ecesgdccdqcrmentioning

confidence: 99%

Snake Venomics and Antivenomics of the Arboreal Neotropical Pitvipers Bothriechis lateralis and Bothriechis schlegelii

et al. 2008

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“…less than 50 ng in 100 μg of venom proteins) to known protein families (Tables 1 and 2). Supporting the view that venom proteomes are mainly composed of toxins belonging to a few protein families [4,[9][10][11][12][13][14][16][17][18][19][20][21][22][23][24], the proteins found in the venoms of L. muta and L. stenophrys cluster, respectively, in 8 and 7 different families (bradykinin-potentiating peptides, NGF, PLA 2 , serine proteinase, cysteine-rich secretory proteins (CRISP; only found in L. muta), C-type lectins, L-amino acid oxidase (LAO), and Zn 2+ -dependent metalloproteinases) (Fig. 6), whose relative abundances are listed in Table 3.…”

Section: Characterization Of Bushmaster Venom Proteomesmentioning

confidence: 99%

“…Within-and between-species heterogeneity of venoms may also account for differences in the clinical symptoms observed in accidental envenomations. In order to explore the putative venom components, several laboratories have carried out transcriptomic analyses of the venom glands of viperid (Bitis gabonica [16], Bothrops insularis [17], Bothrops jararacussu [18], Bothrops jararaca [19], Agkistrodon acutus [20,21], Echis ocellatus [22], and Lachesis muta [23]), elapid (Oxyuramus scutellatus [24]), and colubrid (Philodryas olfersii [25]) snake species. Transcriptomic investigations provide catalogues of partial and full-length transcripts that are synthesized by the venom gland.…”

Section: Introductionmentioning

confidence: 99%

Snake venomics of the South and Central American Bushmasters. Comparison of the toxin composition of Lachesis muta gathered from proteomic versus transcriptomic analysis

Sanz

Escolano

Ferretti

et al. 2008

Journal of Proteomics

121

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This article appeared in a journal published by Elsevier. The attached copy is furnished to the author for internal non-commercial research and education use, including for instruction at the authors institution and sharing with colleagues.Other uses, including reproduction and distribution, or selling or licensing copies, or posting to personal, institutional or third party websites are prohibited. were identified in L. muta and L. stenophrys venoms. In addition, both venoms contained a large number of bradykinin-potentiating peptides (BPP) and a C-type natriuretic peptide (C-NP). BPPs and C-NP comprised around 15% of the total venom proteins. In both species, the most abundant proteins were Zn 2+ -metalloproteinases (32-38%) and serine proteinases (25-31%), followed by PLA 2 s (9-12%), galactose-specific C-type lectin (4-8%), L-amino acid oxidase (LAO, 3-5%), CRISP (1.8%; found in L. muta but not in L. stenophrys), and NGF (0.6%).On the other hand, only six L. muta venom-secreted proteins matched any of the previously reported 11 partial or full-length venom gland transcripts, and venom proteome and transcriptome depart in their relative abundances of different toxin families. As expected from their close phylogenetic relationship, the venoms of L. muta and L. stenophrys share (or contain highly similar) proteins, in particular BPPs, serine proteinases, a galactose-specific C-type lectin, and LAO. However, they dramatically depart in their respective PLA 2 complement. Intraspecific quantitative and qualitative differences in the expression of PLA 2 molecules were found when the venoms of five L. muta specimens (3 from Bolivia and 2 from Peru) and the venom of the same species purchased from Sigma were compared.These observations indicate that these class of toxins represents a rapidly-evolving Author's personal copy gene family, and suggests that functional differences due to structural changes in PLA 2 s molecules among these snakes may have been a hallmark during speciation and adaptation of diverging snake populations to new ecological niches, or competition for resources in existing ones. Our data may contribute to a deeper understanding of the biology and ecology of these snakes, and may also serve as a starting point for studying structure-function correlations of individual toxins.

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“…Snake venom metalloproteinases (SVMPs), phospholipases A 2 , , serine proteinases, esterases, Lamino acid oxidases, hyaluronidases, C-type lectins-like and bradykinin-potentiating peptides (BPPs) are the main venom components that acts inducing cellular injury or releasing inflammatory and vasoactive mediators (Warrell, 2010). Transcriptomic and proteomic studies have showed that SVMPs and serine proteinases are the major toxins in the venom, which explained the high local damage and hemorrhage seen in envenomed patients (Table 2) (Cidade et al, 2006;Zelanis et al, 2010). Bothrops toxins are also known for their multiple effects on hemostasis.…”

Section: Bothrops Venommentioning

confidence: 99%

Acute Kidney Injury Induced by Snake and Arthropod Venoms

Berger¹,

Vieira²,

Guimarães³

2012

Renal Failure - The Facts

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Bothrops jararaca venom gland transcriptome: Analysis of the gene expression pattern

Cited by 124 publications

References 75 publications

Snake Venomics and Antivenomics of the Arboreal Neotropical Pitvipers Bothriechis lateralis and Bothriechis schlegelii

Snake Venomics and Antivenomics of the Arboreal Neotropical Pitvipers Bothriechis lateralis and Bothriechis schlegelii

Snake venomics of the South and Central American Bushmasters. Comparison of the toxin composition of Lachesis muta gathered from proteomic versus transcriptomic analysis

Acute Kidney Injury Induced by Snake and Arthropod Venoms

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