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大规模间日疟原虫-玻利维亚松鼠猴滋养体-裂殖体转化蛋白质组

A large scale Plasmodium vivax- Saimiri boliviensis trophozoite-schizont transition proteome.

作者信息

Anderson D C, Lapp Stacey A, Barnwell John W, Galinski Mary R

机构信息

Bioscience Division, SRI International, Harrisonburg, VA, United States of America.

Emory Vaccine Center, Yerkes National Primate Research Center, Emory University, Atlanta, GA, United States of America.

出版信息

PLoS One. 2017 Aug 22;12(8):e0182561. doi: 10.1371/journal.pone.0182561. eCollection 2017.

Abstract

Plasmodium vivax is a complex protozoan parasite with over 6,500 genes and stage-specific differential expression. Much of the unique biology of this pathogen remains unknown, including how it modifies and restructures the host reticulocyte. Using a recently published P. vivax reference genome, we report the proteome from two biological replicates of infected Saimiri boliviensis host reticulocytes undergoing transition from the late trophozoite to early schizont stages. Using five database search engines, we identified a total of 2000 P. vivax and 3487 S. boliviensis proteins, making this the most comprehensive P. vivax proteome to date. PlasmoDB GO-term enrichment analysis of proteins identified at least twice by a search engine highlighted core metabolic processes and molecular functions such as glycolysis, translation and protein folding, cell components such as ribosomes, proteasomes and the Golgi apparatus, and a number of vesicle and trafficking related clusters. Database for Annotation, Visualization and Integrated Discovery (DAVID) v6.8 enriched functional annotation clusters of S. boliviensis proteins highlighted vesicle and trafficking-related clusters, elements of the cytoskeleton, oxidative processes and response to oxidative stress, macromolecular complexes such as the proteasome and ribosome, metabolism, translation, and cell death. Host and parasite proteins potentially involved in cell adhesion were also identified. Over 25% of the P. vivax proteins have no functional annotation; this group includes 45 VIR members of the large PIR family. A number of host and pathogen proteins contained highly oxidized or nitrated residues, extending prior trophozoite-enriched stage observations from S. boliviensis infections, and supporting the possibility of oxidative stress in relation to the disease. This proteome significantly expands the size and complexity of the known P. vivax and Saimiri host iRBC proteomes, and provides in-depth data that will be valuable for ongoing research on this parasite's biology and pathogenesis.

摘要

间日疟原虫是一种复杂的原生动物寄生虫,拥有超过6500个基因和阶段特异性差异表达。这种病原体的许多独特生物学特性仍然未知,包括它如何修饰和重组宿主网织红细胞。利用最近发表的间日疟原虫参考基因组,我们报告了来自感染玻利维亚松鼠猴宿主网织红细胞的两个生物学重复样本的蛋白质组,这些网织红细胞正经历从晚期滋养体到早期裂殖体阶段的转变。使用五个数据库搜索引擎,我们总共鉴定出2000种间日疟原虫蛋白和3487种玻利维亚松鼠猴蛋白,这使得该蛋白质组成为迄今为止最全面的间日疟原虫蛋白质组。通过搜索引擎至少鉴定两次的蛋白质的PlasmoDB基因本体论术语富集分析突出了核心代谢过程和分子功能,如糖酵解、翻译和蛋白质折叠,细胞成分如核糖体、蛋白酶体和高尔基体,以及一些与囊泡和运输相关的簇。注释、可视化和综合发现数据库(DAVID)v6.8对玻利维亚松鼠猴蛋白的富集功能注释簇突出了与囊泡和运输相关的簇、细胞骨架成分、氧化过程和对氧化应激的反应、大分子复合物如蛋白酶体和核糖体、代谢、翻译和细胞死亡。还鉴定了可能参与细胞粘附的宿主和寄生虫蛋白。超过25%的间日疟原虫蛋白没有功能注释;这一组包括大型PIR家族的45个VIR成员。许多宿主和病原体蛋白含有高度氧化或硝化的残基,扩展了先前对玻利维亚松鼠猴感染滋养体富集阶段的观察结果,并支持了与疾病相关的氧化应激的可能性。这个蛋白质组显著扩大了已知的间日疟原虫和松鼠猴宿主感染红细胞蛋白质组的规模和复杂性,并提供了深入的数据,这对于正在进行的关于这种寄生虫生物学和发病机制的研究将是有价值的。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/9df2/5567661/6c1888be3f37/pone.0182561.g001.jpg

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