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A novel bioactive peptide from wasp venom
Wasp venoms contain a number of pharmacologically active biomolecules, undertaking a wide range of functions necessary for the wasp's survival. We purified and characterized a novel bioactive peptide (vespin) from the venoms of Vespa magnifica (Smith) wasps with unique primary structure. Its am...
Autores principales: | , , , |
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Formato: | Texto |
Lenguaje: | English |
Publicado: |
Library Publishing Media
2010
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3086190/ https://www.ncbi.nlm.nih.gov/pubmed/21544181 |
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author | Chen, Lingling Chen, Wenlin Yang, Hailong Lai, Ren |
author_facet | Chen, Lingling Chen, Wenlin Yang, Hailong Lai, Ren |
author_sort | Chen, Lingling |
collection | PubMed |
description | Wasp venoms contain a number of pharmacologically active biomolecules, undertaking a wide range of functions necessary for the wasp's survival. We purified and characterized a novel bioactive peptide (vespin) from the venoms of Vespa magnifica (Smith) wasps with unique primary structure. Its amino acid sequence was determined to be CYQRRVAITAGGLKHRLMSSLIIIIIIRINYLRDNSVIILESSY. It has 44 residues including 15 leucines or isoleucines (32%) in the sequence. Vespin showed contractile activity on isolated ileum smooth muscle. The cDNA encoding vespin precursor was cloned from the cDNA library of the venomous glands. The precursor consists of 67 amino acid residues including the predicted signal peptide and mature vespin. A di-basic enzymatic processing site (-KR-) is located between the signal peptide and the mature peptide. Vespin did not show similarity with any known proteins or peptides by BLAST search, suggesting it is a novel bioactive peptide from wasp venoms. |
format | Text |
id | pubmed-3086190 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2010 |
publisher | Library Publishing Media |
record_format | MEDLINE/PubMed |
spelling | pubmed-30861902011-05-04 A novel bioactive peptide from wasp venom Chen, Lingling Chen, Wenlin Yang, Hailong Lai, Ren J Venom Res Research Report Wasp venoms contain a number of pharmacologically active biomolecules, undertaking a wide range of functions necessary for the wasp's survival. We purified and characterized a novel bioactive peptide (vespin) from the venoms of Vespa magnifica (Smith) wasps with unique primary structure. Its amino acid sequence was determined to be CYQRRVAITAGGLKHRLMSSLIIIIIIRINYLRDNSVIILESSY. It has 44 residues including 15 leucines or isoleucines (32%) in the sequence. Vespin showed contractile activity on isolated ileum smooth muscle. The cDNA encoding vespin precursor was cloned from the cDNA library of the venomous glands. The precursor consists of 67 amino acid residues including the predicted signal peptide and mature vespin. A di-basic enzymatic processing site (-KR-) is located between the signal peptide and the mature peptide. Vespin did not show similarity with any known proteins or peptides by BLAST search, suggesting it is a novel bioactive peptide from wasp venoms. Library Publishing Media 2010-09-30 /pmc/articles/PMC3086190/ /pubmed/21544181 Text en ©The Authors http://creativecommons.org/licenses/by-nc/2.0/uk/ This is an open access article, published under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/). This license permits non-commercial use, distribution and reproduction of the article, provided the original work is appropriately acknowledged with correct citation details. |
spellingShingle | Research Report Chen, Lingling Chen, Wenlin Yang, Hailong Lai, Ren A novel bioactive peptide from wasp venom |
title | A novel bioactive peptide from wasp venom |
title_full | A novel bioactive peptide from wasp venom |
title_fullStr | A novel bioactive peptide from wasp venom |
title_full_unstemmed | A novel bioactive peptide from wasp venom |
title_short | A novel bioactive peptide from wasp venom |
title_sort | novel bioactive peptide from wasp venom |
topic | Research Report |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3086190/ https://www.ncbi.nlm.nih.gov/pubmed/21544181 |
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