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Characterization of the Molecular Diversity and Degranulation Activity of Mastoparan Family Peptides from Wasp Venoms

Wasp stings have become an increasingly serious public health problem because of their high incidence and mortality rates in various countries and regions. Mastoparan family peptides are the most abundant natural peptides in hornet venoms and solitary wasp venom. However, there is a lack of systemat...

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Autores principales: Ye, Xiangdong, Liu, Xin, Luo, Xudong, Sun, Fang, Qin, Chenhu, Ding, Li, Zhu, Wen, Zhang, Huajun, Zhou, Haimei, Chen, Zongyun
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2023
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10222454/
https://www.ncbi.nlm.nih.gov/pubmed/37235365
http://dx.doi.org/10.3390/toxins15050331
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author Ye, Xiangdong
Liu, Xin
Luo, Xudong
Sun, Fang
Qin, Chenhu
Ding, Li
Zhu, Wen
Zhang, Huajun
Zhou, Haimei
Chen, Zongyun
author_facet Ye, Xiangdong
Liu, Xin
Luo, Xudong
Sun, Fang
Qin, Chenhu
Ding, Li
Zhu, Wen
Zhang, Huajun
Zhou, Haimei
Chen, Zongyun
author_sort Ye, Xiangdong
collection PubMed
description Wasp stings have become an increasingly serious public health problem because of their high incidence and mortality rates in various countries and regions. Mastoparan family peptides are the most abundant natural peptides in hornet venoms and solitary wasp venom. However, there is a lack of systematic and comprehensive studies on mastoparan family peptides from wasp venoms. In our study, for the first time, we evaluated the molecular diversity of 55 wasp mastoparan family peptides from wasp venoms and divided them into four major subfamilies. Then, we established a wasp peptide library containing all 55 known mastoparan family peptides by chemical synthesis and C-terminal amidation modification, and we systematically evaluated their degranulation activities in two mast cell lines, namely the RBL-2H3 and P815 cell lines. The results showed that among the 55 mastoparans, 35 mastoparans could significantly induce mast cell degranulation, 7 mastoparans had modest mast cell degranulation activity, and 13 mastoparans had little mast cell degranulation activity, suggesting functional variation in mastoparan family peptides from wasp venoms. Structure–function relationship studies found that the composition of amino acids in the hydrophobic face and amidation in the C-terminal region are critical for the degranulation activity of mastoparan family peptides from wasp venoms. Our research will lay a theoretical foundation for studying the mechanism underlying the degranulation activity of wasp mastoparans and provide new evidence to support the molecular design and molecular optimization of natural mastoparan peptides from wasp venoms in the future.
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spelling pubmed-102224542023-05-28 Characterization of the Molecular Diversity and Degranulation Activity of Mastoparan Family Peptides from Wasp Venoms Ye, Xiangdong Liu, Xin Luo, Xudong Sun, Fang Qin, Chenhu Ding, Li Zhu, Wen Zhang, Huajun Zhou, Haimei Chen, Zongyun Toxins (Basel) Article Wasp stings have become an increasingly serious public health problem because of their high incidence and mortality rates in various countries and regions. Mastoparan family peptides are the most abundant natural peptides in hornet venoms and solitary wasp venom. However, there is a lack of systematic and comprehensive studies on mastoparan family peptides from wasp venoms. In our study, for the first time, we evaluated the molecular diversity of 55 wasp mastoparan family peptides from wasp venoms and divided them into four major subfamilies. Then, we established a wasp peptide library containing all 55 known mastoparan family peptides by chemical synthesis and C-terminal amidation modification, and we systematically evaluated their degranulation activities in two mast cell lines, namely the RBL-2H3 and P815 cell lines. The results showed that among the 55 mastoparans, 35 mastoparans could significantly induce mast cell degranulation, 7 mastoparans had modest mast cell degranulation activity, and 13 mastoparans had little mast cell degranulation activity, suggesting functional variation in mastoparan family peptides from wasp venoms. Structure–function relationship studies found that the composition of amino acids in the hydrophobic face and amidation in the C-terminal region are critical for the degranulation activity of mastoparan family peptides from wasp venoms. Our research will lay a theoretical foundation for studying the mechanism underlying the degranulation activity of wasp mastoparans and provide new evidence to support the molecular design and molecular optimization of natural mastoparan peptides from wasp venoms in the future. MDPI 2023-05-12 /pmc/articles/PMC10222454/ /pubmed/37235365 http://dx.doi.org/10.3390/toxins15050331 Text en © 2023 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/).
spellingShingle Article
Ye, Xiangdong
Liu, Xin
Luo, Xudong
Sun, Fang
Qin, Chenhu
Ding, Li
Zhu, Wen
Zhang, Huajun
Zhou, Haimei
Chen, Zongyun
Characterization of the Molecular Diversity and Degranulation Activity of Mastoparan Family Peptides from Wasp Venoms
title Characterization of the Molecular Diversity and Degranulation Activity of Mastoparan Family Peptides from Wasp Venoms
title_full Characterization of the Molecular Diversity and Degranulation Activity of Mastoparan Family Peptides from Wasp Venoms
title_fullStr Characterization of the Molecular Diversity and Degranulation Activity of Mastoparan Family Peptides from Wasp Venoms
title_full_unstemmed Characterization of the Molecular Diversity and Degranulation Activity of Mastoparan Family Peptides from Wasp Venoms
title_short Characterization of the Molecular Diversity and Degranulation Activity of Mastoparan Family Peptides from Wasp Venoms
title_sort characterization of the molecular diversity and degranulation activity of mastoparan family peptides from wasp venoms
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10222454/
https://www.ncbi.nlm.nih.gov/pubmed/37235365
http://dx.doi.org/10.3390/toxins15050331
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