A single-pass type I membrane protein, mannose-specific L-type lectin, potentially involved in the adhesion and invasion of Cryptosporidium parvum.

IF 2.3 2区 医学 Q2 PARASITOLOGY
Parasite Pub Date : 2024-01-01 Epub Date: 2024-08-29 DOI:10.1051/parasite/2024051
Xiaotian Zhang, Songying Sun, Wenchao Zhao, Luyang Wang, Guanda Liang, Yuexin Wang, Baiyi Cai, Longxian Zhang, Xiaoying Li, Sumei Zhang
{"title":"A single-pass type I membrane protein, mannose-specific L-type lectin, potentially involved in the adhesion and invasion of Cryptosporidium parvum.","authors":"Xiaotian Zhang, Songying Sun, Wenchao Zhao, Luyang Wang, Guanda Liang, Yuexin Wang, Baiyi Cai, Longxian Zhang, Xiaoying Li, Sumei Zhang","doi":"10.1051/parasite/2024051","DOIUrl":null,"url":null,"abstract":"<p><p>Cryptosporidium is a globally distributed zoonotic protozoan parasite that can cause severe diarrhea in humans and animals. L-type lectins are carbohydrate-binding proteins involved in multiple pathways in animals and plants, including protein transportation, secretion, innate immunity, and the unfolded protein response signaling pathway. However, the biological function of the L-type lectins remains unknown in Cryptosporidium parvum. Here, we preliminarily characterized an L-type lectin in C. parvum (CpLTL) that contains a lectin-leg-like domain. Immunofluorescence assay confirmed that CpLTL is located on the wall of oocysts, the surface of the mid-anterior region of the sporozoite and the cytoplasm of merozoites. The involvement of CpLTL in parasite invasion is partly supported by experiments showing that an anti-CpLTL antibody could partially block the invasion of C. parvum sporozoites into host cells. Moreover, the recombinant CpLTL showed binding ability with mannose and the surface of host cells, and competitively inhibited the invasion of C. parvum. Two host cell proteins were identified by proteomics which should be prioritized for future validation of CpLTL-binding. Our data indicated that CpLTL is potentially involved in the adhesion and invasion of C. parvum.</p>","PeriodicalId":19796,"journal":{"name":"Parasite","volume":null,"pages":null},"PeriodicalIF":2.3000,"publicationDate":"2024-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11363900/pdf/","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Parasite","FirstCategoryId":"3","ListUrlMain":"https://doi.org/10.1051/parasite/2024051","RegionNum":2,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"2024/8/29 0:00:00","PubModel":"Epub","JCR":"Q2","JCRName":"PARASITOLOGY","Score":null,"Total":0}
引用次数: 0

Abstract

Cryptosporidium is a globally distributed zoonotic protozoan parasite that can cause severe diarrhea in humans and animals. L-type lectins are carbohydrate-binding proteins involved in multiple pathways in animals and plants, including protein transportation, secretion, innate immunity, and the unfolded protein response signaling pathway. However, the biological function of the L-type lectins remains unknown in Cryptosporidium parvum. Here, we preliminarily characterized an L-type lectin in C. parvum (CpLTL) that contains a lectin-leg-like domain. Immunofluorescence assay confirmed that CpLTL is located on the wall of oocysts, the surface of the mid-anterior region of the sporozoite and the cytoplasm of merozoites. The involvement of CpLTL in parasite invasion is partly supported by experiments showing that an anti-CpLTL antibody could partially block the invasion of C. parvum sporozoites into host cells. Moreover, the recombinant CpLTL showed binding ability with mannose and the surface of host cells, and competitively inhibited the invasion of C. parvum. Two host cell proteins were identified by proteomics which should be prioritized for future validation of CpLTL-binding. Our data indicated that CpLTL is potentially involved in the adhesion and invasion of C. parvum.

一种单通道 I 型膜蛋白,即甘露糖特异性 L 型凝集素,可能参与了副猪隐孢子虫的粘附和入侵。
隐孢子虫是一种分布于全球的人畜共患原生动物寄生虫,可导致人类和动物严重腹泻。L 型凝集素是一种碳水化合物结合蛋白,参与动物和植物的多种途径,包括蛋白质运输、分泌、先天免疫和未折叠蛋白反应信号途径。然而,L 型凝集素在副隐孢子虫中的生物功能仍然未知。在这里,我们初步鉴定了一种含有类凝集素结构域的副隐孢子虫 L 型凝集素(CpLTL)。免疫荧光检测证实,CpLTL 位于卵囊壁、孢子虫中前部表面和子囊虫细胞质中。实验表明,抗 CpLTL 抗体可部分阻断寄生虫孢子虫对宿主细胞的侵袭,这在一定程度上支持了 CpLTL 参与寄生虫侵袭的观点。此外,重组 CpLTL 显示出与甘露糖和宿主细胞表面的结合能力,并竞争性地抑制了 C. parvum 的入侵。蛋白质组学发现了两种宿主细胞蛋白,这两种蛋白应优先用于未来验证CpLTL的结合能力。我们的数据表明,CpLTL可能参与了伞菌的粘附和入侵。
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 求助全文
来源期刊
Parasite
Parasite 医学-寄生虫学
CiteScore
5.50
自引率
6.90%
发文量
49
审稿时长
3 months
期刊介绍: Parasite is an international open-access, peer-reviewed, online journal publishing high quality papers on all aspects of human and animal parasitology. Reviews, articles and short notes may be submitted. Fields include, but are not limited to: general, medical and veterinary parasitology; morphology, including ultrastructure; parasite systematics, including entomology, acarology, helminthology and protistology, and molecular analyses; molecular biology and biochemistry; immunology of parasitic diseases; host-parasite relationships; ecology and life history of parasites; epidemiology; therapeutics; new diagnostic tools. All papers in Parasite are published in English. Manuscripts should have a broad interest and must not have been published or submitted elsewhere. No limit is imposed on the length of manuscripts, but they should be concisely written. Papers of limited interest such as case reports, epidemiological studies in punctual areas, isolated new geographical records, and systematic descriptions of single species will generally not be accepted, but might be considered if the authors succeed in demonstrating their interest.
×
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