Non‐ribosomal insights into ribosomal P2 protein in Plasmodium falciparum‐infected erythrocytes

Abstract 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 ribo...

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Main Authors: Sudipta Das, Bhaskar Roy, Saswata Chakrabarty
Format: Article
Language:English
Published: Wiley 2021-08-01
Series:MicrobiologyOpen
Subjects:
Online Access:https://doi.org/10.1002/mbo3.1188
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spelling doaj-e5be0fa550ba46349b03a30ec0fec5ae2021-08-30T09:04:32ZengWileyMicrobiologyOpen2045-88272021-08-01104n/an/a10.1002/mbo3.1188Non‐ribosomal insights into ribosomal P2 protein in Plasmodium falciparum‐infected erythrocytesSudipta Das0Bhaskar Roy1Saswata Chakrabarty2Asymmetric Cell Division Laboratory Division of Infectious Disease and Immunology CSIR‐Indian Institute of Chemical Biology Kolkata IndiaAsymmetric Cell Division Laboratory Division of Infectious Disease and Immunology CSIR‐Indian Institute of Chemical Biology Kolkata IndiaAsymmetric Cell Division Laboratory Division of Infectious Disease and Immunology CSIR‐Indian Institute of Chemical Biology Kolkata IndiaAbstract 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.https://doi.org/10.1002/mbo3.1188cell divisionchannel protein complexmalarianuclear divisionPlasmodium falciparumprotein oligomerization
collection DOAJ
language English
format Article
sources DOAJ
author Sudipta Das
Bhaskar Roy
Saswata Chakrabarty
spellingShingle Sudipta Das
Bhaskar Roy
Saswata Chakrabarty
Non‐ribosomal insights into ribosomal P2 protein in Plasmodium falciparum‐infected erythrocytes
MicrobiologyOpen
cell division
channel protein complex
malaria
nuclear division
Plasmodium falciparum
protein oligomerization
author_facet Sudipta Das
Bhaskar Roy
Saswata Chakrabarty
author_sort Sudipta Das
title Non‐ribosomal insights into ribosomal P2 protein in Plasmodium falciparum‐infected erythrocytes
title_short Non‐ribosomal insights into ribosomal P2 protein in Plasmodium falciparum‐infected erythrocytes
title_full Non‐ribosomal insights into ribosomal P2 protein in Plasmodium falciparum‐infected erythrocytes
title_fullStr Non‐ribosomal insights into ribosomal P2 protein in Plasmodium falciparum‐infected erythrocytes
title_full_unstemmed Non‐ribosomal insights into ribosomal P2 protein in Plasmodium falciparum‐infected erythrocytes
title_sort non‐ribosomal insights into ribosomal p2 protein in plasmodium falciparum‐infected erythrocytes
publisher Wiley
series MicrobiologyOpen
issn 2045-8827
publishDate 2021-08-01
description Abstract 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.
topic cell division
channel protein complex
malaria
nuclear division
Plasmodium falciparum
protein oligomerization
url https://doi.org/10.1002/mbo3.1188
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