小孢子虫极管功能和入侵机制的新发现

IF 2.1 4区 生物学 Q3 MICROBIOLOGY Journal of Eukaryotic Microbiology Pub Date : 2024-07-07 DOI:10.1111/jeu.13043
Maurine Fayet, Mengxian Long, Bing Han, Abdel Belkorchia, Frédéric Delbac, Valerie Polonais
{"title":"小孢子虫极管功能和入侵机制的新发现","authors":"Maurine Fayet,&nbsp;Mengxian Long,&nbsp;Bing Han,&nbsp;Abdel Belkorchia,&nbsp;Frédéric Delbac,&nbsp;Valerie Polonais","doi":"10.1111/jeu.13043","DOIUrl":null,"url":null,"abstract":"<p>Microsporidia comprise a large phylum of single-cell and obligate intracellular parasites that can infect a wide range of invertebrate and vertebrate hosts including humans. These fungal-related parasites are characterized by a highly reduced genome, a strong energy dependence on their host, but also by their unique invasion organelle known as the polar tube which is coiled within the resistant spore. Upon appropriate environmental stimulation, the long hollow polar tube (ranging from 50 to 500 μm in length) is extruded at ultra-fast speeds (300 μm/s) from the spore acting as a harpoon-like organelle to transport and deliver the infectious material or sporoplasm into the host cell. To date, seven polar tube proteins (PTPs) with distinct localizations along the extruded polar tube have been described. For example, the specific location of PTP4 and PTP7 at the tip of the polar tube supports their role in interacting with cellular receptor(s). This chapter provides a brief overview on the current understanding of polar tube structure and dynamics of extrusion, primarily through recent advancements in cryo-tomography and 3D reconstruction. It also explores the various mechanisms used for host cell invasion. Finally, recent studies on the structure and maturation of sporoplasm and its moving through the tube are discussed.</p>","PeriodicalId":15672,"journal":{"name":"Journal of Eukaryotic Microbiology","volume":"71 5","pages":""},"PeriodicalIF":2.1000,"publicationDate":"2024-07-07","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"New insights into Microsporidia polar tube function and invasion mechanism\",\"authors\":\"Maurine Fayet,&nbsp;Mengxian Long,&nbsp;Bing Han,&nbsp;Abdel Belkorchia,&nbsp;Frédéric Delbac,&nbsp;Valerie Polonais\",\"doi\":\"10.1111/jeu.13043\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p>Microsporidia comprise a large phylum of single-cell and obligate intracellular parasites that can infect a wide range of invertebrate and vertebrate hosts including humans. These fungal-related parasites are characterized by a highly reduced genome, a strong energy dependence on their host, but also by their unique invasion organelle known as the polar tube which is coiled within the resistant spore. Upon appropriate environmental stimulation, the long hollow polar tube (ranging from 50 to 500 μm in length) is extruded at ultra-fast speeds (300 μm/s) from the spore acting as a harpoon-like organelle to transport and deliver the infectious material or sporoplasm into the host cell. To date, seven polar tube proteins (PTPs) with distinct localizations along the extruded polar tube have been described. For example, the specific location of PTP4 and PTP7 at the tip of the polar tube supports their role in interacting with cellular receptor(s). This chapter provides a brief overview on the current understanding of polar tube structure and dynamics of extrusion, primarily through recent advancements in cryo-tomography and 3D reconstruction. It also explores the various mechanisms used for host cell invasion. Finally, recent studies on the structure and maturation of sporoplasm and its moving through the tube are discussed.</p>\",\"PeriodicalId\":15672,\"journal\":{\"name\":\"Journal of Eukaryotic Microbiology\",\"volume\":\"71 5\",\"pages\":\"\"},\"PeriodicalIF\":2.1000,\"publicationDate\":\"2024-07-07\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Journal of Eukaryotic Microbiology\",\"FirstCategoryId\":\"99\",\"ListUrlMain\":\"https://onlinelibrary.wiley.com/doi/10.1111/jeu.13043\",\"RegionNum\":4,\"RegionCategory\":\"生物学\",\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q3\",\"JCRName\":\"MICROBIOLOGY\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Journal of Eukaryotic Microbiology","FirstCategoryId":"99","ListUrlMain":"https://onlinelibrary.wiley.com/doi/10.1111/jeu.13043","RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q3","JCRName":"MICROBIOLOGY","Score":null,"Total":0}
引用次数: 0

摘要

小孢子虫是一大门单细胞强制性胞内寄生虫,可感染包括人类在内的多种无脊椎动物和脊椎动物宿主。这些与真菌有关的寄生虫的特点是基因组高度减小,对宿主的能量依赖性很强,而且具有独特的入侵细胞器,即盘绕在抗性孢子内的极管。在适当的环境刺激下,长长的空心极管(长度从 50 微米到 500 微米不等)以超高速(300 微米/秒)从孢子中挤出,像鱼叉一样将感染性物质或孢子体运送到宿主细胞中。迄今为止,已经描述了七种极管蛋白(PTPs),它们沿着挤出的极管具有不同的定位。例如,PTP4 和 PTP7 在极管顶端的特定位置支持了它们与细胞受体相互作用的作用。本章主要通过低温层析成像和三维重建的最新进展,简要概述了目前对极性管结构和挤压动态的理解。本章还探讨了宿主细胞入侵的各种机制。最后,还讨论了孢子质的结构和成熟及其在极管中移动的最新研究。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
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
New insights into Microsporidia polar tube function and invasion mechanism

Microsporidia comprise a large phylum of single-cell and obligate intracellular parasites that can infect a wide range of invertebrate and vertebrate hosts including humans. These fungal-related parasites are characterized by a highly reduced genome, a strong energy dependence on their host, but also by their unique invasion organelle known as the polar tube which is coiled within the resistant spore. Upon appropriate environmental stimulation, the long hollow polar tube (ranging from 50 to 500 μm in length) is extruded at ultra-fast speeds (300 μm/s) from the spore acting as a harpoon-like organelle to transport and deliver the infectious material or sporoplasm into the host cell. To date, seven polar tube proteins (PTPs) with distinct localizations along the extruded polar tube have been described. For example, the specific location of PTP4 and PTP7 at the tip of the polar tube supports their role in interacting with cellular receptor(s). This chapter provides a brief overview on the current understanding of polar tube structure and dynamics of extrusion, primarily through recent advancements in cryo-tomography and 3D reconstruction. It also explores the various mechanisms used for host cell invasion. Finally, recent studies on the structure and maturation of sporoplasm and its moving through the tube are discussed.

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
4.30
自引率
4.50%
发文量
85
审稿时长
6-12 weeks
期刊介绍: The Journal of Eukaryotic Microbiology publishes original research on protists, including lower algae and fungi. Articles are published covering all aspects of these organisms, including their behavior, biochemistry, cell biology, chemotherapy, development, ecology, evolution, genetics, molecular biology, morphogenetics, parasitology, systematics, and ultrastructure.
期刊最新文献
Retention of blue-green cryptophyte organelles by Mesodinium rubrum and their effects on photophysiology and growth. Effect of protease inhibitors on the intraerythrocytic development of Babesia microti and Babesia duncani, the causative agents of human babesiosis. Fine structural features of the free-living stages of Amyloodinium ocellatum (Dinoflagellata, Thoracosphaeraceae): A marine fish ectoparasite. Broad-range necrophytophagy in the flagellate Orciraptor agilis (Viridiraptoridae, Cercozoa) and the underappreciated role of scavenging among protists. Functional stress responses in Glaucophyta: Evidence of ethylene and abscisic acid functions in Cyanophora paradoxa.
×
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