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...
Main Authors: | , , |
---|---|
Format: | Article |
Language: | English |
Published: |
Wiley
2021-08-01
|
Series: | MicrobiologyOpen |
Subjects: | |
Online Access: | https://doi.org/10.1002/mbo3.1188 |
id |
doaj-e5be0fa550ba46349b03a30ec0fec5ae |
---|---|
record_format |
Article |
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 |
work_keys_str_mv |
AT sudiptadas nonribosomalinsightsintoribosomalp2proteininplasmodiumfalciparuminfectederythrocytes AT bhaskarroy nonribosomalinsightsintoribosomalp2proteininplasmodiumfalciparuminfectederythrocytes AT saswatachakrabarty nonribosomalinsightsintoribosomalp2proteininplasmodiumfalciparuminfectederythrocytes |
_version_ |
1721185559327539200 |