Profiling hymenopteran venom toxins: Protein families, structural landscape, biological activities, and pharmacological benefits

IF 3.6 Q2 TOXICOLOGY Toxicon: X Pub Date : 2022-06-01 DOI:10.1016/j.toxcx.2022.100119
Juan Carlos Guido-Patiño , Fabien Plisson
{"title":"Profiling hymenopteran venom toxins: Protein families, structural landscape, biological activities, and pharmacological benefits","authors":"Juan Carlos Guido-Patiño ,&nbsp;Fabien Plisson","doi":"10.1016/j.toxcx.2022.100119","DOIUrl":null,"url":null,"abstract":"<div><p>Hymenopterans are an untapped source of venom secretions. Their recent proteo-transcriptomic studies have revealed an extraordinary pool of toxins that participate in various biological processes, including pain, paralysis, allergic reactions, and antimicrobial activities. Comprehensive and clade-specific campaigns to collect hymenopteran venoms are therefore needed. We consider that data-driven bioprospecting may help prioritise sampling and alleviate associated costs. This work established the current protein landscape from hymenopteran venoms to evaluate possible sample bias by studying their origins, sequence diversity, known structures, and biological functions. We collected all 282 reported hymenopteran toxins (peptides and proteins) from the UniProt database that we clustered into 21 protein families from the three studied clades - wasps, bees, and ants. We identified 119 biological targets of hymenopteran toxins ranging from pathogen membranes to eukaryotic proteases, ion channels and protein receptors. Our systematic study further extended to hymenopteran toxins' therapeutic and biotechnological values, where we revealed promising applications in crop pests, human infections, autoimmune diseases, and neurodegenerative disorders.</p></div>","PeriodicalId":37124,"journal":{"name":"Toxicon: X","volume":"14 ","pages":"Article 100119"},"PeriodicalIF":3.6000,"publicationDate":"2022-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.sciencedirect.com/science/article/pii/S2590171022000297/pdfft?md5=02a7ddd19385c79beb148abded09d3a6&pid=1-s2.0-S2590171022000297-main.pdf","citationCount":"8","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Toxicon: X","FirstCategoryId":"1085","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/S2590171022000297","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q2","JCRName":"TOXICOLOGY","Score":null,"Total":0}
引用次数: 8

Abstract

Hymenopterans are an untapped source of venom secretions. Their recent proteo-transcriptomic studies have revealed an extraordinary pool of toxins that participate in various biological processes, including pain, paralysis, allergic reactions, and antimicrobial activities. Comprehensive and clade-specific campaigns to collect hymenopteran venoms are therefore needed. We consider that data-driven bioprospecting may help prioritise sampling and alleviate associated costs. This work established the current protein landscape from hymenopteran venoms to evaluate possible sample bias by studying their origins, sequence diversity, known structures, and biological functions. We collected all 282 reported hymenopteran toxins (peptides and proteins) from the UniProt database that we clustered into 21 protein families from the three studied clades - wasps, bees, and ants. We identified 119 biological targets of hymenopteran toxins ranging from pathogen membranes to eukaryotic proteases, ion channels and protein receptors. Our systematic study further extended to hymenopteran toxins' therapeutic and biotechnological values, where we revealed promising applications in crop pests, human infections, autoimmune diseases, and neurodegenerative disorders.

Abstract Image

查看原文
分享 分享
微信好友 朋友圈 QQ好友 复制链接
本刊更多论文
处女膜毒液毒素简介:蛋白质家族、结构景观、生物活性和药理学益处
膜翅目昆虫是一个未开发的毒液分泌物来源。他们最近的蛋白质转录组学研究揭示了一个特殊的毒素库,参与各种生物过程,包括疼痛、麻痹、过敏反应和抗菌活性。因此,需要开展针对膜翅目昆虫的全面和具体运动,收集膜翅目昆虫的毒液。我们认为数据驱动的生物勘探可能有助于优先采样和降低相关成本。本研究通过研究膜翅目昆虫毒液的起源、序列多样性、已知结构和生物学功能,建立了目前膜翅目昆虫毒液的蛋白质图谱,以评估可能的样本偏差。我们从UniProt数据库中收集了所有282个已报道的膜翅目毒素(多肽和蛋白质),我们将它们归类为来自三个研究分支——黄蜂、蜜蜂和蚂蚁的21个蛋白质家族。我们确定了119个膜翅目毒素的生物靶点,从病原体膜到真核蛋白酶、离子通道和蛋白质受体。我们的系统研究进一步扩展到膜翅目昆虫毒素的治疗和生物技术价值,在那里我们发现了在作物害虫、人类感染、自身免疫性疾病和神经退行性疾病方面有前景的应用。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
求助全文
约1分钟内获得全文 去求助
来源期刊
Toxicon: X
Toxicon: X Pharmacology, Toxicology and Pharmaceutics-Toxicology
CiteScore
6.50
自引率
0.00%
发文量
33
审稿时长
14 weeks
期刊最新文献
A polygeneric immunogen composed of 22 venoms from sub-Saharan African snakes to expand the neutralization scope of the EchiTAb-plus-ICP antivenom Stress levels, hematological condition, and productivity of plasma-producing horses used for snake antivenom manufacture: A comparison of two industrial bleeding methods Diagnosis of human envenoming by terrestrial venomous animals: Routine, advances, and perspectives Supplementation of polyclonal antibodies, developed against epitope-string toxin-specific peptide immunogens, to commercial polyvalent antivenom, shows improved neutralization of Indian Big Four and Naja kaouthia snake venoms Bioprospection of rattlesnake venom peptide fractions with anti-adipose and anti-insulin resistance activity in vitro
×
引用
GB/T 7714-2015
复制
MLA
复制
APA
复制
导出至
BibTeX EndNote RefMan NoteFirst NoteExpress
×
×
提示
您的信息不完整,为了账户安全,请先补充。
现在去补充
×
提示
您因"违规操作"
具体请查看互助需知
我知道了
×
提示
现在去查看 取消
×
提示
确定
0
微信
客服QQ
Book学术公众号 扫码关注我们
反馈
×
意见反馈
请填写您的意见或建议
请填写您的手机或邮箱
已复制链接
已复制链接
快去分享给好友吧!
我知道了
×
扫码分享
扫码分享
Book学术官方微信
Book学术文献互助
Book学术文献互助群
群 号:481959085
Book学术
文献互助 智能选刊 最新文献 互助须知 联系我们:info@booksci.cn
Book学术提供免费学术资源搜索服务,方便国内外学者检索中英文文献。致力于提供最便捷和优质的服务体验。
Copyright © 2023 Book学术 All rights reserved.
ghs 京公网安备 11010802042870号 京ICP备2023020795号-1