scholarly journals Non-ribosomal insights into ribosomal P2 protein in Plasmodium falciparum-infected erythrocytes

2021 ◽  
Author(s):  
Sudipta Das ◽  
Bhaskar Roy ◽  
Saswata Chakrabarty
Keyword(s):  
Plasmodium Falciparum ◽  
Cell Biology ◽  
Ribosomal Proteins ◽  
Infected Erythrocyte ◽  
Mrna Translation ◽  
Trophozoite Stage ◽  
P2 Protein ◽  
P Proteins ◽  
Ribosomal P ◽  
Real Challenge

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 mid trophozoite stage. Inhibiting IE surface P2 either by monoclonal antibody or through genetic knockdown resulted in nuclear division arrest of the parasite. This very strange and serendipitous finding has led us to explore more about un-canonical cell biology and structural involvement of P2 protein in Plasmodium in the search for a novel biochemical role during parasite propagation in the human host.

scholarly journals Copper pathways in Plasmodium falciparum infected erythrocytes indicate an efflux role for the copper P-ATPase

2004 ◽  
Vol 381 (3) ◽  
pp. 803-811 ◽  
Author(s):  
Dominique RASOLOSON ◽  
Lirong SHI ◽  
Curtis R. CHONG ◽  
Bjorn F. KAFSACK ◽  
David J. SULLIVAN
Keyword(s):  
Plasmodium Falciparum ◽  
Infected Erythrocyte ◽  
Recombinant Expression ◽  
Binding Domain ◽  
Copper Binding ◽  
Trophozoite Stage ◽  
Total Copper ◽  
Metal Binding Domain ◽  
Atpase Gene ◽  
Copper Chelator

Copper, like iron, is a transition metal that can generate oxygen radicals by the Fenton reaction. The Plasmodium parasite invades an erythrocyte host cell containing 20 μM copper, of which 70% is contained in the Cu/Zn SOD (cuprozinc superoxide dismutase). In the present study, we follow the copper pathways in the Plasmodium-infected erythrocyte. Metal-determination analysis shows that the total copper content of Percoll-purified trophozoite-stage-infected erythrocytes is 66% that of uninfected erythrocytes. This decrease parallels the decrease seen in Cu/Zn SOD levels in parasite-infected erythrocytes. Neocuproine, an intracellular copper chelator, arrests parasites at the ring-to-trophozoite stage transition and also specifically decreases intraparasitic levels of Cu/Zn SOD and catalase. Up to 150 μM BCS (2,9-dimethyl-4,7-diphenyl-1,10-phenanthrolinedisulphonic acid), an extracellular copper chelator, has no effect on parasite growth. We characterized a single copy PfCuP-ATPase (Plasmodium falciparum copper P-ATPase) transporter, which, like the Crypto-sporidium parvum copper P-ATPase, has a single copper-binding domain: ‘Met-Xaa-Cys-Xaa-Xaa-Cys’. Recombinant expression of the N-terminal metal-binding domain reveals that the protein specifically binds reduced copper. Transcription of the PfCuP-ATPase gene is the highest at late ring stage/early trophozoite, and is down-regulated in the presence of neocuproine. Immunofluorescence and electron microscopy indicate the transporter to be both in the parasite and on the erythrocyte membrane. Both the decrease in total copper and the location of the PfCuP-ATPase gene indicate a copper-efflux pathway from the infected erythrocyte.

scholarly journals Extraribosomal function of the acidic ribosomal P1-protein YP1alpha from Saccharomyces cerevisiae.

1999 ◽  
Vol 46 (4) ◽  
pp. 901-910 ◽  
Author(s):  
M Tchórzewski ◽  
B Boldyreff ◽  
N Grankowski
Keyword(s):  
Ribosomal Proteins ◽  
Transcriptional Activity ◽  
Reporter Genes ◽  
Dna Binding Domain ◽  
Terminal Part ◽  
Transactivation Potential ◽  
Ribosomal Function ◽  
Moonlighting Proteins ◽  
P Proteins ◽  
Ribosomal P

The yeast acidic ribosomal P-proteins YP1alpha, YP1beta, YP2alpha and YP2beta were studied for a possible transactivation potential beside their ribosomal function. The fusions of P-proteins with the GAL4 DNA-binding domain were assayed toward their transcriptional activity with the aid of reporter genes in yeast. Two of the P-proteins, YP1alpha and YP1beta, exhibited transactivation potential, however, only YP1alpha can be regarded as a potent transactivator. This protein was able to transactivate a reporter gene associated with two distinct promoter systems, GAL1 or CYC1. Additionally, truncated proteins of YP1alpha and YP1beta were analyzed. The N-terminal part of YP1alpha fused to GAL4-BD showed transactivation potential but the C-terminal part did not. Our results suggest a putative extraribosomal function for these ribosomal proteins which consequently may be classified as "moonlighting" proteins.

Combinatorial Metabolism in Plasmodium falciparum-Infected Erythrocyte and Interplay of Glycosylation & Phosphorylation

2004 ◽  
Vol 8 (5) ◽  
pp. 453-461 ◽  
Author(s):  
Bentham Science Publisher Nasir-ud-Din ◽  
Ishtiaq Ahmad ◽  
Asma Iqbal ◽  
Daniel Hoessli
Keyword(s):  
Plasmodium Falciparum ◽  
Infected Erythrocyte

scholarly journals Identification of sulfenylation patterns in trophozoite stage Plasmodium falciparum using a non-dimedone based probe

2021 ◽  
Vol 242 ◽  
pp. 111362
Author(s):  
Susanne Schipper ◽  
Hanzhi Wu ◽  
Cristina M. Furdui ◽  
Leslie B. Poole ◽  
Claire M. Delahunty ◽  
...  
Keyword(s):  
Plasmodium Falciparum ◽  
Trophozoite Stage

scholarly journals Trafficking and Association of Plasmodium falciparum MC-2TM with the Maurer’s Clefts

Pathogens ◽  
2021 ◽  
Vol 10 (4) ◽  
pp. 431
Author(s):  
Raghavendra Yadavalli ◽  
John W. Peterson ◽  
Judith A. Drazba ◽  
Tobili Y. Sam-Yellowe
Keyword(s):  
Plasmodium Falciparum ◽  
Erythrocyte Membrane ◽  
Sodium Carbonate ◽  
Infected Erythrocyte ◽  
Brefeldin A ◽  
Specific Expression ◽  
Lipid Interactions ◽  
And Topology ◽  
Streptolysin O ◽  
Maurer's Clefts

In this study, we investigated stage specific expression, trafficking, solubility and topology of endogenous PfMC-2TM in P. falciparum (3D7) infected erythrocytes. Following Brefeldin A (BFA) treatment of parasites, PfMC-2TM traffic was evaluated using immunofluorescence with antibodies reactive with PfMC-2TM. PfMC-2TM is sensitive to BFA treatment and permeabilization of infected erythrocytes with streptolysin O (SLO) and saponin, showed that the N and C-termini of PfMC-2TM are exposed to the erythrocyte cytoplasm with the central portion of the protein protected in the MC membranes. PfMC-2TM was expressed as early as 4 h post invasion (hpi), was tightly colocalized with REX-1 and trafficked to the erythrocyte membrane without a change in solubility. PfMC-2TM associated with the MC and infected erythrocyte membrane and was resistant to extraction with alkaline sodium carbonate, suggestive of protein-lipid interactions with membranes of the MC and erythrocyte. PfMC-2TM is an additional marker of the nascent MCs.

scholarly journals Upregulation of 5′-terminal oligopyrimidine mRNA translation upon loss of the ARF tumor suppressor

2020 ◽  
Vol 10 (1) ◽  
Author(s):  
Kyle A. Cottrell ◽  
Ryan C. Chiou ◽  
Jason D. Weber
Keyword(s):  
Protein Synthesis ◽  
Tumor Cells ◽  
Ribosomal Proteins ◽  
Human Cancer ◽  
Mrna Translation ◽  
Ribosome Profiling ◽  
Translational Efficiency ◽  
Gene Encoding ◽  
Terminal Oligopyrimidine ◽  
Ribosome Export

AbstractTumor cells require nominal increases in protein synthesis in order to maintain high proliferation rates. As such, tumor cells must acquire enhanced ribosome production. How the numerous mutations in tumor cells ultimately achieve this aberrant production is largely unknown. The gene encoding ARF is the most commonly deleted gene in human cancer. ARF plays a significant role in regulating ribosomal RNA synthesis and processing, ribosome export into the cytoplasm, and global protein synthesis. Utilizing ribosome profiling, we show that ARF is a major suppressor of 5′-terminal oligopyrimidine mRNA translation. Genes with increased translational efficiency following loss of ARF include many ribosomal proteins and translation factors. Knockout of p53 largely phenocopies ARF loss, with increased protein synthesis and expression of 5′-TOP encoded proteins. The 5′-TOP regulators eIF4G1 and LARP1 are upregulated in Arf- and p53-null cells.

Use of self-assembling GFP to determine protein topology and compartmentalisation in the Plasmodium falciparum-infected erythrocyte

2013 ◽  
Vol 187 (2) ◽  
pp. 87-90 ◽  
Author(s):  
Simone Külzer ◽  
Wiebke Petersen ◽  
Avni Baser ◽  
Katharina Mandel ◽  
Jude M. Przyborski
Keyword(s):  
Plasmodium Falciparum ◽  
Infected Erythrocyte ◽  
Use Of Self ◽  
Protein Topology ◽  
Self Assembling

scholarly journals Antigenicity of the infected-erythrocyte and merozoite surfaces in Falciparum malaria.

1979 ◽  
Vol 150 (5) ◽  
pp. 1241-1254 ◽  
Author(s):  
S G Langreth ◽  
R T Reese
Keyword(s):  
Plasmodium Falciparum ◽  
Falciparum Malaria ◽  
Infected Erythrocyte ◽  
Falciparum Infection ◽  
Human Erythrocytes ◽  
Cross Linking ◽  
Common Antigens

The antigenicity of altered structures induced by Plasmodium falciparum in the membranes of infected Aotus monkey and human erythrocytes was examined. Antisera were obtained from monkeys made immune to malaria. Bound antibodies were shown to be localized on the knob protrusions of infected erythrocytes of both human and monkey origin and from both in vitro and in vivo infections. Therefore, P. falciparum infection has produced similar antigenic changes in the erythrocyte surfaces of both man and monkey. Uninfected erythrocytes and all knobless-infected erythrocytes bound no antibody from immune sera. Strains of P. falciparum from widely different geographic areas that were cultured in vitro in human erythrocytes induced structures (knobs) which have common antigenicity. Merozoites were agglutinated by cross-linking of their cell coats when incubated with immune sera. The binding of ferritin-labeled antibody was heavy on the coats of both homologous and heterologous strains of the parasite, indicating that the merozoite surfaces of these strains share common antigens.

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