Testing the Toxicofera: Comparative transcriptomics casts doubt on the single, early evolution of the reptile venom system

Hargreaves, Adam D; Swain, Martin; Logan, Darren W.; Mulley, John F.

doi:10.1016/j.toxicon.2014.10.004

Cited by 71 publications

(90 citation statements)

References 111 publications

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“…Although it is known some characteristics of these enzymes, few studies have reported the identification of phospholipases B in the venom of Sistrurus catenatus edwardsii (Chapeaurouge et al, 2015), and in the venom-gland transcriptome of Crotalus adamanteus (Rokyta et al, 2011), Drysdalia coronoides (Chatrath et al, 2011), Ophiophagus hannah (Vonk et al, 2013), Micrurus fulvius (Margres et al, 2013) and Echis coloratus (Hargreaves et al, 2014). Moreover, these enzymes were identified in the venom of the elapid snakes Austrelaps superbus and P. colletti by isoelectric focusing followed by haemolytic activity assays (Bernheimer, Weinstein and Linder, 1986).…”

Section: Discussionmentioning

confidence: 99%

Identification of hyaluronidase and phospholipase B in Lachesis muta rhombeata venom

Wiezel

Santos

Cordeiro

et al. 2015

Toxicon

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Hyaluronidases contribute to local and systemic damages after envenoming, since they act as spreading factors cleaving the hyaluronan presents in the connective tissues of the victim, facilitating the diffusion of venom components. Although hyaluronidases are ubiquitous in snake venoms, they still have not been detected in transcriptomic analysis of the Lachesis venom gland and neither in the proteome of its venom performed previously. This work purified a hyaluronidase from Lachesis muta rhombeata venom whose molecular mass was estimated by SDS-PAGE to be 60 kDa. The hyaluronidase was more active at pH 6 and 37 °C when salt concentration was kept constant and more active in the presence of 0.15 M monovalent ions when the pH was kept at 6. Venom was fractionated by reversed-phase liquid chromatography (RPLC). Edman sequencing after RPLC failed to detect hyaluronidase, but identified a new serine proteinase isoform. The hyaluronidase was identified by mass spectrometry analysis of the protein bands in SDS-PAGE. Additionally, phospholipase B was identified for the first time in Lachesis genus venom. The discovery of new bioactive molecules might contribute to the design of novel drugs and biotechnology products as well as to development of more effective treatments against the envenoming.

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Section: Discussionmentioning

confidence: 99%

Identification of hyaluronidase and phospholipase B in Lachesis muta rhombeata venom

Wiezel

Santos

Cordeiro

et al. 2015

Toxicon

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“…[12], as well as Erythrolamprus miliaris , Oxyrhopus guibei and Xenodon merremi described here. For Colubrinae, transcriptomes of oral glands from Pantherophis guttatus, Opheodrys aestivus [9] and Boiga irregularis (Duvernoy’s venom gland); [12] were generated, although only the last one was complemented by venom proteomic analysis. Nevertheless, many toxins from the other subfamilies have been investigated by more focused approaches, such as protein purification from the venom (e.g., Borikenophis portoricensis [47]) or specific cDNA cloning, including some genera with particularly toxic venom, such as the natricine Rhabdophis [66].…”

Section: Resultsmentioning

confidence: 99%

“…Whether or not these type IIE PLA 2 s represent truly new toxins or accessory proteins of the venom glands remains to be clarified, but Hargreaves et al [9] found them to be exclusively expressed at low levels in the venom glands of the species tested. …”

Section: Resultsmentioning

confidence: 99%

“…Very low levels of LAAO activity were detected in Brown Treesnake ( B. irregularis ) venom [72]; however, assays of venom from 13 different species of colubrine, dipsadine and natricine rear-fanged snakes detected no LAAO activity [73]. In a comparative transcriptomic analysis of tissues from Pantherophis guttatus , an LAAO was shown to be expressed in the scent gland but not in the salivary glands of this species [9], suggesting it is not a venom component. Recently, however, an LAAO was found moderately expressed in the venom glands of the colubrid Phalotris mertensi , and the MS/MS spectrometric analysis clearly showed its presence in the venom of this species [57].…”

Section: Resultsmentioning

confidence: 99%

“…[1,2,3]), have further accelerated the pace of sequence acquisition and compositional analysis and constituted the basis of large-scale biotechnological explorative initiatives (e.g., [4]). These studies collectively created very complete inventories of the toxin families and superfamilies present in species representing significant risk to human health, further refined by a growing knowledge of the relative abundances, post-translational modifications and also structural conservation of proteins across numerous genera [5,6,7,8,9,10,11,12,13,14,15,16,17,18]. As a side product of the accumulation of this knowledge, the observed differences in venom composition among related taxa are becoming appreciated as a productive model for making evolutionary inferences about diversifying selection.…”

Section: Introductionmentioning

confidence: 99%

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Colubrid Venom Composition: An -Omics Perspective

Junqueira-de-Azevedo

Campos

Ching

et al. 2016

Toxins

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Snake venoms have been subjected to increasingly sensitive analyses for well over 100 years, but most research has been restricted to front-fanged snakes, which actually represent a relatively small proportion of extant species of advanced snakes. Because rear-fanged snakes are a diverse and distinct radiation of the advanced snakes, understanding venom composition among “colubrids” is critical to understanding the evolution of venom among snakes. Here we review the state of knowledge concerning rear-fanged snake venom composition, emphasizing those toxins for which protein or transcript sequences are available. We have also added new transcriptome-based data on venoms of three species of rear-fanged snakes. Based on this compilation, it is apparent that several components, including cysteine-rich secretory proteins (CRiSPs), C-type lectins (CTLs), CTLs-like proteins and snake venom metalloproteinases (SVMPs), are broadly distributed among “colubrid” venoms, while others, notably three-finger toxins (3FTxs), appear nearly restricted to the Colubridae (sensu stricto). Some putative new toxins, such as snake venom matrix metalloproteinases, are in fact present in several colubrid venoms, while others are only transcribed, at lower levels. This work provides insights into the evolution of these toxin classes, but because only a small number of species have been explored, generalizations are still rather limited. It is likely that new venom protein families await discovery, particularly among those species with highly specialized diets.

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