NcSWP8, a New Spore Wall Protein, Interacts with Polar Tube Proteins in the Parasitic Microsporidia Vairimorpha (Nosema) ceranae.

IF 4.2 2区 生物学 Q2 MICROBIOLOGY Microorganisms Pub Date : 2025-01-12 DOI:10.3390/microorganisms13010142
Pengfei Wang, Dufu Li, Qianmin Hai, Siming Liu, Yueyue Zhang, Jun Zhang, Jinshan Xu, Zhengang Ma, Zeyang Zhou
{"title":"NcSWP8, a New Spore Wall Protein, Interacts with Polar Tube Proteins in the Parasitic Microsporidia <i>Vairimorpha (Nosema) ceranae</i>.","authors":"Pengfei Wang, Dufu Li, Qianmin Hai, Siming Liu, Yueyue Zhang, Jun Zhang, Jinshan Xu, Zhengang Ma, Zeyang Zhou","doi":"10.3390/microorganisms13010142","DOIUrl":null,"url":null,"abstract":"<p><p><i>Vairimorpha (Nosema) ceranae</i> is a pathogen that affects <i>Apis mellifera</i> and <i>Apis ceranae</i> Fabricius, capable of spreading within and between honeybee colonies. The spore wall of microsporidia is the initial structure to contact the host cell directly, which may play a crucial role in the infection process. Currently, several spore wall proteins have been identified in microsporidia, but only two spore wall proteins from <i>V. ceranae</i> have been characterized. Here, we report the expression and identification of a novel spore wall protein, NcSWP8, with a molecular mass of 21.37 kDa in <i>V. ceranae</i>. Subcellular localization analysis revealed that NcSWP8 was localized on the spore wall of <i>V. ceranae</i>. Co-immunoprecipitation and Far-Western blotting experiments demonstrated that NcSWP8 could stably interact with polar tube proteins, NcPTP2 and NcPTP3. The antibody blocking assay significantly decreased their infection rate, indicating that NcSWP8 played a significant role in the process of <i>V. ceranae</i> infection. These results together suggested that NcSWP8 was a new spore wall protein localized to the spore wall and interacted with the polar tube proteins, playing a crucial role in supporting the formation of the spore wall and potentially affecting the process of infection of <i>V. ceranae</i>.</p>","PeriodicalId":18667,"journal":{"name":"Microorganisms","volume":"13 1","pages":""},"PeriodicalIF":4.2000,"publicationDate":"2025-01-12","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11767685/pdf/","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Microorganisms","FirstCategoryId":"99","ListUrlMain":"https://doi.org/10.3390/microorganisms13010142","RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q2","JCRName":"MICROBIOLOGY","Score":null,"Total":0}
引用次数: 0

Abstract

Vairimorpha (Nosema) ceranae is a pathogen that affects Apis mellifera and Apis ceranae Fabricius, capable of spreading within and between honeybee colonies. The spore wall of microsporidia is the initial structure to contact the host cell directly, which may play a crucial role in the infection process. Currently, several spore wall proteins have been identified in microsporidia, but only two spore wall proteins from V. ceranae have been characterized. Here, we report the expression and identification of a novel spore wall protein, NcSWP8, with a molecular mass of 21.37 kDa in V. ceranae. Subcellular localization analysis revealed that NcSWP8 was localized on the spore wall of V. ceranae. Co-immunoprecipitation and Far-Western blotting experiments demonstrated that NcSWP8 could stably interact with polar tube proteins, NcPTP2 and NcPTP3. The antibody blocking assay significantly decreased their infection rate, indicating that NcSWP8 played a significant role in the process of V. ceranae infection. These results together suggested that NcSWP8 was a new spore wall protein localized to the spore wall and interacted with the polar tube proteins, playing a crucial role in supporting the formation of the spore wall and potentially affecting the process of infection of V. ceranae.

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
一种新的孢子壁蛋白NcSWP8与微孢子虫的极性管蛋白相互作用。
蜜蜂微孢子虫是一种影响蜜蜂和蜜蜂的病原体,能够在蜜蜂群体内和群体间传播。微孢子虫的孢子壁是与宿主细胞直接接触的初始结构,在感染过程中可能起着至关重要的作用。目前,在微孢子虫中已经鉴定出了几种孢子壁蛋白,但仅鉴定了两种来自ceranae的孢子壁蛋白。在此,我们报道了一种新的孢子壁蛋白NcSWP8的表达和鉴定,其分子质量为21.37 kDa。亚细胞定位分析表明NcSWP8定位于ceranae的孢子壁上。共免疫沉淀和Far-Western blotting实验表明,NcSWP8能稳定地与极管蛋白NcPTP2和NcPTP3相互作用。抗体阻断实验显著降低了它们的感染率,表明NcSWP8在V. ceranae感染过程中发挥了重要作用。这些结果表明NcSWP8是一种定位于孢子壁并与极管蛋白相互作用的新孢子壁蛋白,在支持孢子壁的形成中起着至关重要的作用,并可能影响ceranae的感染过程。
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
Microorganisms
Microorganisms Medicine-Microbiology (medical)
CiteScore
7.40
自引率
6.70%
发文量
2168
审稿时长
20.03 days
期刊介绍: Microorganisms (ISSN 2076-2607) is an international, peer-reviewed open access journal which provides an advanced forum for studies related to prokaryotic and eukaryotic microorganisms, viruses and prions. It publishes reviews, research papers and communications. Our aim is to encourage scientists to publish their experimental and theoretical results in as much detail as possible. There is no restriction on the length of the papers. The full experimental details must be provided so that the results can be reproduced. Electronic files and software regarding the full details of the calculation or experimental procedure, if unable to be published in a normal way, can be deposited as supplementary electronic material.
期刊最新文献
Strain Diversity in the Human Microbiome: Personal Variation, Pathobionts, Therapeutics, and Methodological Challenges. Editorial for "Gut Microbiota, Diet, and Gastrointestinal Cancer". Effects of Microbial Inoculants from Three Nutrient-Poor Environments on Soil Improvement and Plant Growth Promotion in Sandy Soil. Editorial for Special Issue "Animal Viral Infectious Diseases". Association of TLR4 Polymorphisms with Increased Susceptibility to Recurrent Vulvovaginal Candidiasis in Greek Women.
×
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:604180095
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