单系寄生虫病毒横纹肌的预测分泌组:宿主-寄生虫相互作用的假设分子机制

M. Mirabent-Casals, V. Caña-Bozada, F. N. Morales-Serna, A. García‐Gasca
{"title":"单系寄生虫病毒横纹肌的预测分泌组:宿主-寄生虫相互作用的假设分子机制","authors":"M. Mirabent-Casals, V. Caña-Bozada, F. N. Morales-Serna, A. García‐Gasca","doi":"10.3390/parasitologia3010004","DOIUrl":null,"url":null,"abstract":"Helminth parasites secrete several types of biomolecules to ensure their entry into and survival in their hosts. The proteins secreted to the extracellular environment participate in the pathogenesis and anthelmintic immune responses. The aim of this work was to identify and functionally annotate the excretory/secretory (ES) proteins of the monogenean ectoparasite Rhabdosynochus viridisi through bioinformatic approaches. A total of 1655 putative ES proteins were identified, 513 (31%) were annotated in the UniProtKB/Swiss-Prot database, and 269 (16%) were mapped to 212 known protein domains and 710 GO terms. We identified six putative multifunctional proteins. A total of 556 ES proteins were mapped to 179 KEGG pathways and 136 KO. ECPred predicted 223 enzymes (13.5%) and 1315 non-enzyme proteins (79.5%) from the secretome of R. viridisi. A total of 1045 (63%) proteins were predicted as antigen with a threshold 0.5. We also identified six venom allergen-like proteins. Our results suggest that ES proteins from R. viridisi are involved in immune evasion strategies and some may contribute to immunogenicity.","PeriodicalId":74398,"journal":{"name":"Parasitologia (Basel, Switzerland)","volume":" ","pages":""},"PeriodicalIF":0.0000,"publicationDate":"2023-01-10","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"1","resultStr":"{\"title\":\"Predicted Secretome of the Monogenean Parasite Rhabdosynochus viridisi: Hypothetical Molecular Mechanisms for Host-Parasite Interactions\",\"authors\":\"M. Mirabent-Casals, V. Caña-Bozada, F. N. Morales-Serna, A. García‐Gasca\",\"doi\":\"10.3390/parasitologia3010004\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"Helminth parasites secrete several types of biomolecules to ensure their entry into and survival in their hosts. The proteins secreted to the extracellular environment participate in the pathogenesis and anthelmintic immune responses. The aim of this work was to identify and functionally annotate the excretory/secretory (ES) proteins of the monogenean ectoparasite Rhabdosynochus viridisi through bioinformatic approaches. A total of 1655 putative ES proteins were identified, 513 (31%) were annotated in the UniProtKB/Swiss-Prot database, and 269 (16%) were mapped to 212 known protein domains and 710 GO terms. We identified six putative multifunctional proteins. A total of 556 ES proteins were mapped to 179 KEGG pathways and 136 KO. ECPred predicted 223 enzymes (13.5%) and 1315 non-enzyme proteins (79.5%) from the secretome of R. viridisi. A total of 1045 (63%) proteins were predicted as antigen with a threshold 0.5. We also identified six venom allergen-like proteins. Our results suggest that ES proteins from R. viridisi are involved in immune evasion strategies and some may contribute to immunogenicity.\",\"PeriodicalId\":74398,\"journal\":{\"name\":\"Parasitologia (Basel, Switzerland)\",\"volume\":\" \",\"pages\":\"\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"2023-01-10\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"1\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Parasitologia (Basel, Switzerland)\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://doi.org/10.3390/parasitologia3010004\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Parasitologia (Basel, Switzerland)","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.3390/parasitologia3010004","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 1

摘要

寄生虫分泌几种类型的生物分子以确保它们进入宿主并在宿主体内存活。分泌到细胞外环境的蛋白质参与了虫虫的发病机制和免疫反应。本研究的目的是通过生物信息学方法对单系外寄生虫病毒横纹肌(Rhabdosynochus virus)的排泄/分泌(ES)蛋白进行鉴定和功能注释。总共鉴定了1655个推定的ES蛋白,其中513个(31%)被UniProtKB/Swiss-Prot数据库注释,269个(16%)被映射到212个已知蛋白结构域和710个GO项。我们鉴定了六种假定的多功能蛋白。556个ES蛋白被定位到179个KEGG通路和136个KO通路。ECPred预测出223种酶(13.5%)和1315种非酶蛋白(79.5%)。共有1045个(63%)蛋白被预测为抗原,阈值为0.5。我们还发现了六种毒液过敏原样蛋白。我们的研究结果表明,来自病毒弧菌的ES蛋白参与了免疫逃避策略,其中一些可能有助于免疫原性。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
Predicted Secretome of the Monogenean Parasite Rhabdosynochus viridisi: Hypothetical Molecular Mechanisms for Host-Parasite Interactions
Helminth parasites secrete several types of biomolecules to ensure their entry into and survival in their hosts. The proteins secreted to the extracellular environment participate in the pathogenesis and anthelmintic immune responses. The aim of this work was to identify and functionally annotate the excretory/secretory (ES) proteins of the monogenean ectoparasite Rhabdosynochus viridisi through bioinformatic approaches. A total of 1655 putative ES proteins were identified, 513 (31%) were annotated in the UniProtKB/Swiss-Prot database, and 269 (16%) were mapped to 212 known protein domains and 710 GO terms. We identified six putative multifunctional proteins. A total of 556 ES proteins were mapped to 179 KEGG pathways and 136 KO. ECPred predicted 223 enzymes (13.5%) and 1315 non-enzyme proteins (79.5%) from the secretome of R. viridisi. A total of 1045 (63%) proteins were predicted as antigen with a threshold 0.5. We also identified six venom allergen-like proteins. Our results suggest that ES proteins from R. viridisi are involved in immune evasion strategies and some may contribute to immunogenicity.
求助全文
通过发布文献求助,成功后即可免费获取论文全文。 去求助
来源期刊
CiteScore
1.70
自引率
0.00%
发文量
0
×
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
确定
请完成安全验证×
copy
已复制链接
快去分享给好友吧!
我知道了
右上角分享
点击右上角分享
0
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 布克学术 All rights reserved.
京ICP备2023020795号-1
ghs 京公网安备 11010802042870号
Book学术文献互助
Book学术文献互助群
群 号:481959085
Book学术官方微信