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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...
Autores principales: | , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Elsevier
2022
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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. |
format | Online Article Text |
id | pubmed-9234072 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | Elsevier |
record_format | MEDLINE/PubMed |
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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