State Key Laboratory of Silkworm Genome Biology, Southwest University, Chongqing 400715, China; Chongqing Key Laboratory of Microsporidia Infection and Control, Southwest University, Chongqing 400715, China.
State Key Laboratory of Silkworm Genome Biology, Southwest University, Chongqing 400715, China; Chongqing Key Laboratory of Microsporidia Infection and Control, Southwest University, Chongqing 400715, China.
J Proteomics. 2022 Jul 15;263:104617. doi: 10.1016/j.jprot.2022.104617. Epub 2022 May 18.
Microsporidium is a kind of intracellular fungal pathogen that greatly threatens the human health, breeding industry, and food security. All members of microsporidia possess a unique, highly specialized invasion organelle, described as the polar filament. Like "reversing a finger of gloves", the polar filament discharges out of mature spores to transform as the polar tube, and pathogenic sporoplasm is transported to host cell through polar tube to complete infection. During the invasion process, the structure of polar filament and polar tube has changed, so does the protein composition on them? In this study, we firstly proposed a purification method for polar filament and polar tube from microsporidium Nosema bombycis which was infected silkworm Bombyx mori, and it was also found that the structure of polar filament and polar tube was obviously different. Therefore, the proteome of these two structures was comparatively analyzed. A total of 881 and 1216 proteins were respectively identified from the polar filament and polar tube. Ten potential novel polar tube proteins (PTPs) were screened, providing a reference for the novel PTPs identification. Compared with the polar filament, there were 35 upregulated and 41 downregulated proteins on the polar tube. GO and KEGG pathway analysis of all proteins from the polar filament and polar tube provided us with a profound understanding for the microsporidian germination process, which was of great significance for clarifying the infection mechanism of microsporidia. SIGNIFICANCE: Microsporidia are obligate intracellular parasites that infect a wide variety of hosts, including humans. The polar filament is a unique invasion organelle for microsporidia, and it is also one of the important indexes of microsporidian taxonomy. The polar tube is deformed from the primitive polar filament in mature spores. During the germination, the polar filament turns into a polar tube, like "reversing a finger of gloves", through which pathogenic sporoplasm is transported to host cells to complete infection. Since the structure of the polar filament and polar tube has changed, what about their protein composition? In this study, it was the first time to purify the polar filament and the polar tube from microsporidium Nosema bombycis that was infected silkworm Bombyx mori, which provided new insights for studying the invasion organelle of microsporidia. Comparing the fine structure of polar filament and polar tube, we found that their structure was obviously different. Therefore, the protein composition of these two structures is supposed to be varied. In this case, the proteome of these two structures was comparatively analyzed. A total of 881 and 1216 proteins were respectively identified from the polar filament and polar tube. Ten potential novel polar tube proteins (PTPs) were screened, providing a reference for the novel PTPs identification. Compared with the polar filament, there were 35 upregulated and 41 downregulated proteins on the polar tube. GO and KEGG pathway analysis of all proteins from the polar filament and polar tube provided us with a profound understanding for the microsporidian germination process, which was of great significance for clarifying the infection mechanism of microsporidia.
微孢子虫是一种严重威胁人类健康、养殖业和食品安全的细胞内真菌病原体。所有微孢子虫都具有独特的、高度专业化的入侵细胞器，称为极丝。极丝像“翻手套的手指”一样，从成熟孢子中排出，转化为极管，致病孢子质通过极管输送到宿主细胞完成感染。在入侵过程中，极丝和极管的结构发生了变化，它们上面的蛋白质组成是否也发生了变化？在这项研究中，我们首次提出了一种从感染家蚕的微孢子虫Nosema bombycis 中纯化极丝和极管的方法，同时还发现极丝和极管的结构明显不同。因此，我们对这两种结构的蛋白质组进行了比较分析。分别从极丝和极管中鉴定到 881 种和 1216 种蛋白质。筛选出 10 种潜在的新型极管蛋白（PTPs），为新型 PTPs 的鉴定提供了参考。与极丝相比，极管上有 35 个上调和 41 个下调的蛋白质。对极丝和极管中所有蛋白质的 GO 和 KEGG 通路分析为我们深入了解微孢子虫的发芽过程提供了帮助，这对阐明微孢子虫的感染机制具有重要意义。
微孢子虫是一种专性细胞内寄生虫，可感染多种宿主，包括人类。极丝是微孢子虫特有的入侵细胞器，也是微孢子虫分类学的重要指标之一。极管是成熟孢子中原极丝的变形。在发芽过程中，极丝通过极管“翻手套的手指”样的转化，将致病孢子质输送到宿主细胞中完成感染。由于极丝和极管的结构发生了变化，它们的蛋白质组成是否也发生了变化？在这项研究中，首次从感染家蚕的微孢子虫 Nosema bombycis 中纯化了极丝和极管，为研究微孢子虫的入侵细胞器提供了新的视角。比较极丝和极管的精细结构，发现它们的结构明显不同。因此，这两种结构的蛋白质组成应该是不同的。在这种情况下，我们对这两种结构的蛋白质组进行了比较分析。分别从极丝和极管中鉴定到 881 种和 1216 种蛋白质。筛选出 10 种潜在的新型极管蛋白（PTPs），为新型 PTPs 的鉴定提供了参考。与极丝相比，极管上有 35 个上调和 41 个下调的蛋白质。对极丝和极管中所有蛋白质的 GO 和 KEGG 通路分析为我们深入了解微孢子虫的发芽过程提供了帮助，这对阐明微孢子虫的感染机制具有重要意义。
