High molecular weight components of the injected venom of fish-hunting cone snails target the vascular system

Safavi-­Hemami, Helena; Möller, Carolina; Marí, Frank; Purcell, Anthony W.

doi:10.1016/j.jprot.2013.07.007

Cited by 16 publications

(14 citation statements)

References 38 publications

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“…ACE also inactivates bradykinin, a vasodilator peptide, and thus contributes to blood pressure increase in mammals. In invertebrates, ACE-related genes have been cloned in a few insects [ 66 - 68 ], in the duck leech Theromyzon tessulatus [ 69 ], and recently ACE-encoding transcript was reported in the venom duct transcriptome of Conus victoriae [ 70 ], while the peptide was found in the proteomes of C. purpuranscens and C. ermineus [ 71 ]. For the cone snails it was suggested that the vasoconstrictory activity of ACE enzymes might play a role in envenomation, perhaps increasing the local concentration and effectiveness of the venom, or, more generally, interfering with cardiovascular homeostatic mechanisms as seen in other venomous animals.…”

Section: Resultsmentioning

confidence: 99%

The venomous cocktail of the vampire snail Colubraria reticulata (Mollusca, Gastropoda)

Modica

Lombardo²,

Franchini

et al. 2015

BMC Genomics

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BackgroundHematophagy arose independently multiple times during metazoan evolution, with several lineages of vampire animals particularly diversified in invertebrates. However, the biochemistry of hematophagy has been studied in a few species of direct medical interest and is still underdeveloped in most invertebrates, as in general is the study of venom toxins. In cone snails, leeches, arthropods and snakes, the strong target specificity of venom toxins uniquely aligns them to industrial and academic pursuits (pharmacological applications, pest control etc.) and provides a biochemical tool for studying biological activities including cell signalling and immunological response. Neogastropod snails (cones, oyster drills etc.) are carnivorous and include active predators, scavengers, grazers on sessile invertebrates and hematophagous parasites; most of them use venoms to efficiently feed. It has been hypothesized that trophic innovations were the main drivers of rapid radiation of Neogastropoda in the late Cretaceous.We present here the first molecular characterization of the alimentary secretion of a non-conoidean neogastropod, Colubraria reticulata. Colubrariids successfully feed on the blood of fishes, throughout the secretion into the host of a complex mixture of anaesthetics and anticoagulants. We used a NGS RNA-Seq approach, integrated with differential expression analyses and custom searches for putative secreted feeding-related proteins, to describe in detail the salivary and mid-oesophageal transcriptomes of this Mediterranean vampire snail, with functional and evolutionary insights on major families of bioactive molecules.ResultsA remarkably low level of overlap was observed between the gene expression in the two target tissues, which also contained a high percentage of putatively secreted proteins when compared to the whole body. At least 12 families of feeding-related proteins were identified, including: 1) anaesthetics, such as ShK Toxin-containing proteins and turripeptides (ion-channel blockers), Cysteine-rich secretory proteins (CRISPs), Adenosine Deaminase (ADA); 2) inhibitors of primary haemostasis, such as novel vWFA domain-containing proteins, the Ectonucleotide pyrophosphatase/phosphodiesterase family member 5 (ENPP5) and the wasp Antigen-5; 3) anticoagulants, such as TFPI-like multiple Kunitz-type protease inhibitors, Peptidases S1 (PS1), CAP/ShKT domain-containing proteins, Astacin metalloproteases and Astacin/ShKT domain-containing proteins; 4) additional proteins, such the Angiotensin-Converting Enzyme (ACE: vasopressive) and the cytolytic Porins.ConclusionsColubraria feeding physiology seems to involve inhibitors of both primary and secondary haemostasis, anaesthetics, a vasoconstrictive enzyme to reduce feeding time and tissue-degrading proteins such as Porins and Astacins. The complexity of Colubraria venomous cocktail and the divergence from the arsenal of the few neogastropods studied to date (mostly conoideans) suggest that biochemical diversification of neogastropods might be largely...

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Section: Resultsmentioning

confidence: 99%

The venomous cocktail of the vampire snail Colubraria reticulata (Mollusca, Gastropoda)

Modica

Lombardo²,

Franchini

et al. 2015

BMC Genomics

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“…The presence of angiotensin-converting enzyme-1 (ACE-1) and endothelin converting enzyme-1 (ECE-1) metalloproteases that activate vasoconstrictive peptides was recently demonstrated in the injected venoms of the piscivorous C. purpurascens and Conus ermineus [ 176 ]. ACE was also found to be highly expressed in the venom gland of the molluscivorous C. victoriae [ 27 ].…”

Section: Conoproteinsmentioning

confidence: 99%

Conotoxin Gene Superfamilies

2014

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Conotoxins are the peptidic components of the venoms of marine cone snails (genus Conus). They are remarkably diverse in terms of structure and function. Unique potency and selectivity profiles for a range of neuronal targets have made several conotoxins valuable as research tools, drug leads and even therapeutics, and has resulted in a concerted and increasing drive to identify and characterise new conotoxins. Conotoxins are translated from mRNA as peptide precursors, and cDNA sequencing is now the primary method for identification of new conotoxin sequences. As a result, gene superfamily, a classification based on precursor signal peptide identity, has become the most convenient method of conotoxin classification. Here we review each of the described conotoxin gene superfamilies, with a focus on the structural and functional diversity present in each. This review is intended to serve as a practical guide to conotoxin superfamilies and to facilitate interpretation of the increasing number of conotoxin precursor sequences being identified by targeted-cDNA sequencing and more recently high-throughput transcriptome sequencing.

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“…According to Safavi-Hemami and collaborators (2013), who described an angiotensin I-converting enzyme in the venom of cone snails, this enzyme may promote vasoconstriction of blood vessels at the sting site by angiotensin II, along with catecholamine [13]. In fact, animals and patients envenomed by scorpions from the Buthidae family present elevation of plasma renin–angiotensin activity and, consequently, an increase of angiotensin II [43,44].…”

Section: Discussionmentioning

confidence: 99%

“…For instance, in snake venoms, serine peptidases can affect the coagulation cascade and kallikrein–kinin system, while metallopeptidases target components of blood coagulation and platelet aggregation, both resulting in an imbalance of the hemostatic system [10,11]. Although snake venom peptidases are the most studied, due to their abundance, proteolytic activity has recently been described in jellyfish [12], cone snail [13], wasp [14], spider [15], and scorpion [16] venoms.…”

Section: Introductionmentioning

confidence: 99%

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Insights into the Hypertensive Effects of Tityus serrulatus Scorpion Venom: Purification of an Angiotensin-Converting Enzyme-Like Peptidase

Cajado-Carvalho

Kuniyoshi

Duzzi

et al. 2016

Toxins

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The number of cases of envenomation by scorpions has grown significantly in Brazil since 2007, with the most severe cases being caused by the Tityus serrulatus scorpion. Although envenomed patients mostly suffer neurotoxic manifestations, other symptoms, such as hypertension, cannot be exclusively attributed to neurotoxins. Omics analyses have detected plentiful amounts of metalloproteases in T. serrulatus venom. However, the roles played by these enzymes in envenomation are still unclear. Endeavoring to investigate the functions of scorpion venom proteases, we describe here for the first time an Angiotensin I-Converting Enzyme-like peptidase (ACE-like) purified from T. serrulatus venom. The crude venom cleaved natural and fluorescent substrates and these activities were inhibited by captopril. Regarding the serum neutralization, the scorpion antivenom was more effective at blocking the ACE-like activity than arachnid antivenom, although neither completely inhibited the venom cleavage action, even at higher doses. ACE-like was purified from the venom after three chromatographic steps and its identity was confirmed by mass spectrometric and transcriptomic analyses. Bioinformatics analysis showed homology between the ACE-like transcript sequences from Tityus spp. and human testis ACE. These findings advance our understanding of T. serrulatus venom components and may improve treatment of envenomation victims, as ACE-like may contribute to envenomation symptoms, especially the resulting hypertension.

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High molecular weight components of the injected venom of fish-hunting cone snails target the vascular system

Cited by 16 publications

References 38 publications

The venomous cocktail of the vampire snail Colubraria reticulata (Mollusca, Gastropoda)

The venomous cocktail of the vampire snail Colubraria reticulata (Mollusca, Gastropoda)

Conotoxin Gene Superfamilies

Insights into the Hypertensive Effects of Tityus serrulatus Scorpion Venom: Purification of an Angiotensin-Converting Enzyme-Like Peptidase

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