Isolation and characterization of renin-like aspartic-proteases from Echis ocellatus venom

Wilkinson, Mark C.; Nightingale, Djh; Harrison, Robert A.; Wagstaff, Simon C.

doi:10.1016/j.toxicon.2017.07.008

Cited by 1 publication

(2 citation statements)

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“…72 The latter protease was recently purified from the venom, and its renin-like activity was confirmed. 73 Renin is a mammalian aspartic protease catalyzing the first step of the renin–angiotensin pathway in which angiotensinogen is processed to angiotensin I. This is then cleaved by angiotensin-converting enzyme to angiotensin II, a vasoconstrictor.…”

Section: Resultsmentioning

confidence: 99%

“…Thus far, such a protease has been identified as a minor venom component of various Russian vipers , and the Indian saw-scaled viper, Echis c. carinatus . The latter protease was recently purified from the venom, and its renin-like activity was confirmed . Renin is a mammalian aspartic protease catalyzing the first step of the renin–angiotensin pathway in which angiotensinogen is processed to angiotensin I.…”

Section: Resultsmentioning

confidence: 99%

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Comprehensive Study of the Proteome and Transcriptome of the Venom of the Most Venomous European Viper: Discovery of a New Subclass of Ancestral Snake Venom Metalloproteinase Precursor-Derived Proteins

et al. 2019

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The nose-horned viper, its nominotypical subspecies Vipera ammodytes ammodytes ( Vaa ), in particular, is, medically, one of the most relevant snakes in Europe. The local and systemic clinical manifestations of poisoning by the venom of this snake are the result of the pathophysiological effects inflicted by enzymatic and nonenzymatic venom components acting, most prominently, on the blood, cardiovascular, and nerve systems. This venom is a very complex mixture of pharmacologically active proteins and peptides. To help improve the current antivenom therapy toward higher specificity and efficiency and to assist drug discovery, we have constructed, by combining transcriptomic and proteomic analyses, the most comprehensive library yet of the Vaa venom proteins and peptides. Sequence analysis of the venom gland cDNA library has revealed the presence of messages encoding 12 types of polypeptide precursors. The most abundant are those for metalloproteinase inhibitors (MPis), bradykinin-potentiating peptides (BPPs), and natriuretic peptides (NPs) (all three on a single precursor), snake C-type lectin-like proteins (snaclecs), serine proteases (SVSPs), P-II and P-III metalloproteinases (SVMPs), secreted phospholipases A 2 (sPLA 2 s), and disintegrins (Dis). These constitute >88% of the venom transcriptome. At the protein level, 57 venom proteins belonging to 16 different protein families have been identified and, with SVSPs, sPLA 2 s, snaclecs, and SVMPs, comprise ∼80% of all venom proteins. Peptides detected in the venom include NPs, BPPs, and inhibitors of SVSPs and SVMPs. Of particular interest, a transcript coding for a protein similar to P-III SVMPs but lacking the MP domain was also found at the protein level in the venom. The existence of such proteins, also supported by finding similar venom gland transcripts in related snake species, has been demonstrated for the first time, justifying the proposal of a new P-IIIe subclass of ancestral SVMP precursor-derived proteins.

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Section: Resultsmentioning

confidence: 99%