The enormous complexity of the eukaryotic ribosome has been a real challenge in unlocking the mechanistic aspects of its amazing molecular function during mRNA translation and many non-canonical activities of ribosomal proteins in eukaryotic cells. While exploring the uncanny nature of ribosomal P proteins in malaria parasites Plasmodium falciparum, the 60S stalk ribosomal P2 protein has been shown to get exported to the infected erythrocyte (IE) surface as an SDS-resistant oligomer during the early to the mid-trophozoite stage. Inhibiting IE surface P2 either by monoclonal antibody or through genetic knockdown resulted in nuclear division arrest of the parasite. This strange and serendipitous finding has led us to explore more about un-canonical cell biology and the structural involvement of P2 protein in Plasmodium in the search for a novel biochemical role during parasite propagation in the human host.

中文翻译：

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来自恶性疟原虫感染红细胞中核糖体 P2 蛋白的非核糖体见解

真核生物核糖体的巨大复杂性对于在真核细胞中 mRNA 翻译和核糖体蛋白的许多非规范活动中解开其惊人分子功能的机制方面一直是一个真正的挑战。在探索疟疾寄生虫恶性疟原虫中核糖体 P 蛋白的不可思议的性质时，60S 茎核糖体 P2 蛋白已被证明在早期到中期滋养体阶段作为 SDS 抗性寡聚体输出到受感染的红细胞 (IE) 表面. 通过单克隆抗体或通过基因敲低抑制 IE 表面 P2 导致寄生虫的核分裂停滞。这一奇怪而偶然的发现促使我们更多地探索非典型细胞生物学和 P2 蛋白在疟原虫在寄生虫在人类宿主中繁殖过程中寻找新的生化作用。