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Biochemistry and toxicology of proteins and peptides purified from the venom of Vipera berus berus

The isolation and characterization of individual snake venom components is important for a deeper understanding of the pathophysiology of envenomation and for improving the therapeutic procedures of patients. It also opens possibilities for the discovery of novel toxins that might be useful as tools...

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Autores principales: Siigur, Jüri, Siigur, Ene
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Elsevier 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9234072/
https://www.ncbi.nlm.nih.gov/pubmed/35769869
http://dx.doi.org/10.1016/j.toxcx.2022.100131
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author Siigur, Jüri
Siigur, Ene
author_facet Siigur, Jüri
Siigur, Ene
author_sort Siigur, Jüri
collection PubMed
description The isolation and characterization of individual snake venom components is important for a deeper understanding of the pathophysiology of envenomation and for improving the therapeutic procedures of patients. It also opens possibilities for the discovery of novel toxins that might be useful as tools for understanding cellular and molecular processes. The variable venom composition, toxicological and immunological properties of the common vipers (Vipera berus berus) have been reviewed. The combination of venom gland transcriptomics, bottom-up and top-down proteomics enabled comparison of common viper venom proteomes from multiple individuals. V. b. berus venom contains proteins and peptides belonging to 10–15 toxin families: snake venom metalloproteinase, phospholipases A(2) (PLA(2)), snake venom serine proteinase, aspartic protease, L-amino acid oxidase (LAAO), hyaluronidase, 5′-nucleotidase, glutaminyl-peptide cyclotransferase, disintegrin, C-type lectin (snaclec), nerve growth factor, Kunitz type serine protease inhibitor, snake venom vascular endothelial growth factor, cysteine-rich secretory protein, bradykinin potentiating peptide, natriuretic peptides. PLA(2) and LAAO from V. b. berus venom produce more pronounced cytotoxic effects in cancer cells than normal cells, via induction of apoptosis, cell cycle arrest and suppression of proliferation. Proteomic data of V. b. berus venoms from different parts of Russia and Slovakian Republic have been compared with analogous data for Vipera nikolskii venom. Proteomic studies demonstrated quantitative differences in the composition of V. b. berus venom from different geographical regions. Differences in the venom composition of V. berus were mainly driven by the age, sex, habitat and diet of the snakes. The venom variability of V. berus results in a loss of antivenom efficacy against snakebites. The effectiveness of antibodies is discussed. This review presents an overview with a special focus on different toxins that have been isolated and characterized from the venoms of V. b. berus. Their main biochemical properties and toxic actions are described.
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spelling pubmed-92340722022-06-28 Biochemistry and toxicology of proteins and peptides purified from the venom of Vipera berus berus Siigur, Jüri Siigur, Ene Toxicon X Review The isolation and characterization of individual snake venom components is important for a deeper understanding of the pathophysiology of envenomation and for improving the therapeutic procedures of patients. It also opens possibilities for the discovery of novel toxins that might be useful as tools for understanding cellular and molecular processes. The variable venom composition, toxicological and immunological properties of the common vipers (Vipera berus berus) have been reviewed. The combination of venom gland transcriptomics, bottom-up and top-down proteomics enabled comparison of common viper venom proteomes from multiple individuals. V. b. berus venom contains proteins and peptides belonging to 10–15 toxin families: snake venom metalloproteinase, phospholipases A(2) (PLA(2)), snake venom serine proteinase, aspartic protease, L-amino acid oxidase (LAAO), hyaluronidase, 5′-nucleotidase, glutaminyl-peptide cyclotransferase, disintegrin, C-type lectin (snaclec), nerve growth factor, Kunitz type serine protease inhibitor, snake venom vascular endothelial growth factor, cysteine-rich secretory protein, bradykinin potentiating peptide, natriuretic peptides. PLA(2) and LAAO from V. b. berus venom produce more pronounced cytotoxic effects in cancer cells than normal cells, via induction of apoptosis, cell cycle arrest and suppression of proliferation. Proteomic data of V. b. berus venoms from different parts of Russia and Slovakian Republic have been compared with analogous data for Vipera nikolskii venom. Proteomic studies demonstrated quantitative differences in the composition of V. b. berus venom from different geographical regions. Differences in the venom composition of V. berus were mainly driven by the age, sex, habitat and diet of the snakes. The venom variability of V. berus results in a loss of antivenom efficacy against snakebites. The effectiveness of antibodies is discussed. This review presents an overview with a special focus on different toxins that have been isolated and characterized from the venoms of V. b. berus. Their main biochemical properties and toxic actions are described. Elsevier 2022-06-12 /pmc/articles/PMC9234072/ /pubmed/35769869 http://dx.doi.org/10.1016/j.toxcx.2022.100131 Text en © 2022 The Authors https://creativecommons.org/licenses/by/4.0/This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Review
Siigur, Jüri
Siigur, Ene
Biochemistry and toxicology of proteins and peptides purified from the venom of Vipera berus berus
title Biochemistry and toxicology of proteins and peptides purified from the venom of Vipera berus berus
title_full Biochemistry and toxicology of proteins and peptides purified from the venom of Vipera berus berus
title_fullStr Biochemistry and toxicology of proteins and peptides purified from the venom of Vipera berus berus
title_full_unstemmed Biochemistry and toxicology of proteins and peptides purified from the venom of Vipera berus berus
title_short Biochemistry and toxicology of proteins and peptides purified from the venom of Vipera berus berus
title_sort biochemistry and toxicology of proteins and peptides purified from the venom of vipera berus berus
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9234072/
https://www.ncbi.nlm.nih.gov/pubmed/35769869
http://dx.doi.org/10.1016/j.toxcx.2022.100131
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