Asymmetric Cell Division Laboratory, Division of Infectious Disease and Immunology, CSIR-Indian Institute of Chemical Biology, Kolkata, India.
Microbiologyopen. 2021 Aug;10(4):e1188. doi: 10.1002/mbo3.1188.
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.
真核核糖体的巨大复杂性一直是在揭示其在 mRNA 翻译过程中惊人的分子功能以及真核细胞中核糖体蛋白的许多非典型活性的机制方面的一个真正挑战。在探索疟原虫恶性疟原虫中核糖体 P 蛋白的不可思议性质时，已经表明 60S 柄核糖体 P2 蛋白在早期到中滋养体阶段会作为一种抗 SDS 的寡聚体被输出到感染的红细胞 (IE) 表面。通过单克隆抗体或通过基因敲低抑制 IE 表面 P2 会导致寄生虫的核分裂停止。这一奇怪而偶然的发现促使我们更深入地探索非典型细胞生物学和 P2 蛋白在恶性疟原虫中的结构参与，以寻找寄生虫在人类宿主中繁殖过程中的新的生化作用。
