Tags

Type your tag names separated by a space and hit enter

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.
J Proteome Res. 2019 05 03; 18(5):2287-2309.JP

Abstract

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 A2 (sPLA2s), 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, sPLA2s, 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.

Authors+Show Affiliations

Department of Molecular and Biomedical Sciences , Jožef Stefan Institute , Jamova cesta 39 , SI-1000 Ljubljana , Slovenia.Department of Molecular and Biomedical Sciences , Jožef Stefan Institute , Jamova cesta 39 , SI-1000 Ljubljana , Slovenia.Department of Molecular and Biomedical Sciences , Jožef Stefan Institute , Jamova cesta 39 , SI-1000 Ljubljana , Slovenia.Department of Molecular and Biomedical Sciences , Jožef Stefan Institute , Jamova cesta 39 , SI-1000 Ljubljana , Slovenia.

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

31017792

Citation

Leonardi, Adrijana, et al. "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." Journal of Proteome Research, vol. 18, no. 5, 2019, pp. 2287-2309.
Leonardi A, Sajevic T, Pungerčar J, et al. 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. J Proteome Res. 2019;18(5):2287-2309.
Leonardi, A., Sajevic, T., Pungerčar, J., & Križaj, I. (2019). 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. Journal of Proteome Research, 18(5), 2287-2309. https://doi.org/10.1021/acs.jproteome.9b00120
Leonardi A, et al. 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. J Proteome Res. 2019 05 3;18(5):2287-2309. PubMed PMID: 31017792.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - 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. AU - Leonardi,Adrijana, AU - Sajevic,Tamara, AU - Pungerčar,Jože, AU - Križaj,Igor, Y1 - 2019/04/24/ PY - 2019/4/25/pubmed PY - 2020/6/2/medline PY - 2019/4/25/entrez KW - Vipera ammodytes ammodytes KW - Viperidae KW - metalloproteinase KW - new subclass KW - proteomics KW - snake KW - transcriptomics KW - venom composition SP - 2287 EP - 2309 JF - Journal of proteome research JO - J Proteome Res VL - 18 IS - 5 N2 - 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 A2 (sPLA2s), 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, sPLA2s, 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. SN - 1535-3907 UR - https://www.unboundmedicine.com/medline/citation/31017792/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_ L2 - https://doi.org/10.1021/acs.jproteome.9b00120 DB - PRIME DP - Unbound Medicine ER -