scholarly journals Agglutination Assays of the Plasmodium falciparum-Infected Erythrocyte

2015 ◽  
pp. 115-129
Author(s):  
Joshua Tan ◽  
Peter C. Bull
Keyword(s):  
Plasmodium Falciparum ◽  
Infected Erythrocyte

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 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.

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.

Expression of the RESA gene in Plasmodium falciparum isolate FCR3 is prevented by a subtelomeric deletion

1989 ◽  
Vol 9 (8) ◽  
pp. 3584-3587
Author(s):  
R Cappai ◽  
M R van Schravendijk ◽  
R F Anders ◽  
M G Peterson ◽  
L M Thomas ◽  
...  
Keyword(s):  
Plasmodium Falciparum ◽  
Surface Antigen ◽  
Infected Erythrocyte ◽  
Falciparum Isolate ◽  
Erythrocyte Surface ◽  
Subtelomeric Deletion

We show here that the Plasmodium falciparum isolate FCR3 does not express the ring-infected erythrocyte surface antigen (RESA). This is because the 5' end of the RESA gene has been inverted and partly deleted and a telomere has been added to it. We propose a model to explain these events.

A and T homopolymeric stretches mediate a DNA inversion in Plasmodium falciparum which results in loss of gene expression

1990 ◽  
Vol 10 (6) ◽  
pp. 3243-3246
Author(s):  
L G Pologe ◽  
D de Bruin ◽  
J V Ravetch
Keyword(s):  
Gene Expression ◽  
Plasmodium Falciparum ◽  
Gene Structure ◽  
Infected Erythrocyte ◽  
Dna Rearrangement ◽  
Coding Sequences ◽  
Dna Inversion ◽  
Erythrocyte Surface ◽  
Stable Substrate ◽  
Flanking Sequences

Ring-infected erythrocyte surface antigen-negative isolates of Plasmodium falciparum demonstrate a complex DNA rearrangement with inversion of 5' coding sequences, deletion of upstream and flanking sequences, and healing of the truncated chromosome by telomere addition. An inversion intermediate that results in the telomeric gene structure for RESA has been identified in the pathway. This inversion creates a mitotically stable substrate for the sequence-specific addition of telomere repeats at the deletion breakpoint.

scholarly journals A and T homopolymeric stretches mediate a DNA inversion in Plasmodium falciparum which results in loss of gene expression.

1990 ◽  
Vol 10 (6) ◽  
pp. 3243-3246 ◽  
Author(s):  
L G Pologe ◽  
D de Bruin ◽  
J V Ravetch
Keyword(s):  
Gene Expression ◽  
Plasmodium Falciparum ◽  
Gene Structure ◽  
Infected Erythrocyte ◽  
Dna Rearrangement ◽  
Coding Sequences ◽  
Dna Inversion ◽  
Erythrocyte Surface ◽  
Stable Substrate ◽  
Flanking Sequences

Ring-infected erythrocyte surface antigen-negative isolates of Plasmodium falciparum demonstrate a complex DNA rearrangement with inversion of 5' coding sequences, deletion of upstream and flanking sequences, and healing of the truncated chromosome by telomere addition. An inversion intermediate that results in the telomeric gene structure for RESA has been identified in the pathway. This inversion creates a mitotically stable substrate for the sequence-specific addition of telomere repeats at the deletion breakpoint.

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