Molecular study of binding of Plasmodium ribosomal protein P2 to erythrocytes

Mishra, Pushpa; Dmello, Crismita; Sengupta, Disha; Singh, Suraj; Kirkise, Nikita; Hosur, Ramakrishna V.; Sharma, Shobhona

doi:10.1016/j.biochi.2020.07.007

Cited by 4 publications

(3 citation statements)

References 58 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“… 10 , 11 At this stage, denaturation resistant PfP2 tetramer was found to be present on the IE surface, hinting at its possible role at the onset of parasite schizogony. In previous reports, 26 , 27 , 28 , 61 , 62 , 63 , 64 , 65 using FM4-64 and NMR, a possibility of PfP2 tetramer being involved in lipid interaction on the IE surface was indicated. It was not known about the specific class of lipid which was the bona fide ligand to the PfP2 tetramer on the IE surface.…”

Section: Discussionmentioning

confidence: 92%

M-O-M mediated denaturation resistant P2 tetramer on the infected erythrocyte surface of malaria parasite imports serum fatty acids

Das,

Manna,

Majumdar

et al. 2024

iScience

View full text Add to dashboard Cite

Section: Discussionmentioning

confidence: 92%

M-O-M mediated denaturation resistant P2 tetramer on the infected erythrocyte surface of malaria parasite imports serum fatty acids

Das,

Manna,

Majumdar

et al. 2024

iScience

View full text Add to dashboard Cite

“…falciparum P2 forms a molten globule tetramer indicating some functional implications of tetrameric P2 on the surface of iRBCs at the late trophozoite stage. In a recent discovery, it has been demonstrated that P2 tetramers stabilize themselves on the iRBC surface by interacting with RBC Band3 protein where N terminal 70 amino acids of P2 interact to form the oligomers and associate with Band 3 protein (Mishra et al, 2020 ).…”

Section: In Solution P2 Forms a Stable Tetramer Which Is A Molten Globule In Nature Having Hydrophobic Pockets On The Surfacementioning

confidence: 99%

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

Roy

Chakrabarty

2021

MicrobiologyOpen

View full text Add to dashboard Cite

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.

show abstract

“…PfPP2 tetramer could provide sites for intermolecular association in an aqueous environment and may have the possibility to bind non-polar/hydrophobic molecules as a bonafide ligand(s) on iRBC surface. In a recent discovery, it has been demonstrated that rec.PfP2 tetramers stabilise themselves on the iRBC surface by interacting with Band 3 protein where N terminal 70 amino acids of PfP2 interact to form the oligomers and associate with Band 3 protein (35). Between the P. falciparum P2 and the human P2, there is 69% amino acid sequence homology but they differ in their oligomerization pattern and behaviour as the human P2 at physiological pH forms a stable dimer (36) but under same condition, P. falciparum P2 forms a molten globule tetramer indicating critical functional implications of tetrameric P2 on the iRBCs surface during mid-late trophozoite stage.…”

Section: Introductionmentioning

confidence: 99%

Denaturation resistant P2 tetramer is required to import fatty acids into intraerythrocytic Plasmodium falciparum

Majumder

Bhattacharjya

et al. 2022

Preprint

View full text Add to dashboard Cite

The initiation of asymmetric karyokinesis of intraerythrocytic Plasmodium falciparum (Pf) begins with- out dismantling the nuclear envelope showing the hallmark feature of closed mitosis (1-10). In Pf, karyokinesis precedes cytokinesis and cell body formation (6, 8-10). Regulation at the beginning of nu- clear division either through checkpoints or by importing serum components was largely unknown. At the trophozoite stage, PfP2 tetramer trafficked to the infected erythrocyte (IE) surface and the inacces- sibility of IE surface PfP2 to its bonafide ligand led to the arrest of nuclear division (11-13). Here we show that PfP2 tetramer localization on the IE surface and the beginning of nuclear division are con- comitant in nature. Synthetically induced denaturation resistant PfP2 tetramer interacts with human serum fatty acids and phospholipids for its import into IEs at the beginning of karyokinesis. In the na- tively folded denaturation resistant PfP2 tetramer cage, the Cys-Cys redox switch regulates the bind- ing and subsequent release of fatty acids on the IE surface. This mechanistic insight of fatty acids im- port inside IEs using synthetically induced denaturation resistant PfP2 tetramer provides an unique drug screening platform for novel small molecule screening against malaria.

show abstract

Molecular study of binding of Plasmodium ribosomal protein P2 to erythrocytes

Cited by 4 publications

References 58 publications

M-O-M mediated denaturation resistant P2 tetramer on the infected erythrocyte surface of malaria parasite imports serum fatty acids

M-O-M mediated denaturation resistant P2 tetramer on the infected erythrocyte surface of malaria parasite imports serum fatty acids

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

Denaturation resistant P2 tetramer is required to import fatty acids into intraerythrocytic Plasmodium falciparum

Contact Info

Product

Resources

About