Identification of a Stomatin Orthologue in Vacuoles Induced in Human Erythrocytes by Malaria Parasites

Hiller, N. Luisa; Akompong, Thomas; Morrow, Jon S.; Holder, Anthony A.; Haldar, Kasturi

doi:10.1074/jbc.m307266200

Cited by 88 publications

(72 citation statements)

References 60 publications

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“…Following solubilisation in cold non-ionic detergent and fractionation by sucrose density gradient flotation, DRMs float within low density sucrose fractions whereas non-DRM components remain in the high density loading fraction (Hiller et al, 2003;Wang et al, 2003b). Following sucrose density gradient flotation, Pf34 was detected in low density fractions (2-4).…”

Section: Pf34 Is Recruited Into Drmsmentioning

confidence: 99%

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Plasmodium falciparum Pf34, a novel GPI-anchored rhoptry protein found in detergent-resistant microdomains

Proellocks

Kovacevic

Ferguson

et al. 2007

International Journal for Parasitology

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Apicomplexan parasites are characterised by the presence of specialised organelles, such as rhoptries, located at the apical end of invasive forms that play an important role in invasion of the host cell and formation of the parasitophorous vacuole. In this study, we have characterised a novel Plasmodium falciparum rhoptry protein, Pf34, encoded by a single exon gene located on chromosome 4 and expressed as a 34 kDa protein in mature asexual stage parasites. Pf34 is expressed later in the life cycle than the previously described rhoptry protein, Rhoptry Associated Membrane Antigen (RAMA). Orthologues of Pf34 are present in other Plasmodium species and a potential orthologue has also been identified in Toxoplasma gondii. Indirect immunofluorescence assays show that Pf34 is located at the merozoite apex and localises to the rhoptry neck. Pf34, previously demonstrated to be glutathione-S-transferase (GPI)-anchored (Gilson et al., 2006, Identification and stoichiometry of GPI-anchored membrane proteins of the human malaria parasite Plasmodium falciparum. Mol Cell Proteomics, 1286-1299), is associated with parasite-derived detergent-resistant microdomains (DRMs). Pf34 is carried into the newly invaded ring, consistent with a role for Pf34 in the formation of the parasitophorous vacuole. Pf34 is exposed to the human immune system during infection and is recognised by human immune sera collected from residents of malaria endemic areas of Vietnam and Papua New Guinea.

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Section: Pf34 Is Recruited Into Drmsmentioning

confidence: 99%

“…In P. falciparum-infected erythrocytes, DRMs are rich in cholesterol and sphingolipids and contain a sub-population of parasite-derived membrane proteins. (Salzer and Prohaska, 2001;Salzer et al, 2002;Hiller et al, 2003;Wang et al, 2003b;Sanders et al, 2005).…”

Section: Introductionmentioning

confidence: 99%

Plasmodium falciparum Pf34, a novel GPI-anchored rhoptry protein found in detergent-resistant microdomains

Proellocks

Kovacevic

Ferguson

et al. 2007

International Journal for Parasitology

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“…Tetanolysin O forms pores in RBC membranes and exposes proteins present in infected host cells ( Figure 2G). 44 Saponin exposes proteins of the RBC cytoplasm, the PVM and MC ( Figure 2G). Triton X-100 solubilizes all membranes and releases proteins from each compartment.…”

Section: Pfptp1 Is An Integral MC Membrane Proteinmentioning

confidence: 99%

Export of virulence proteins by malaria-infected erythrocytes involves remodeling of host actin cytoskeleton

Rug

Cyrklaff

Mikkonen

et al. 2014

Blood

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“…Red blood cells (RBCs) were pelleted and washed with PBS. Infected erythrocytes from both types of parasites were then treated with 0.05% saponin (Sigma Chemical Co., St. Louis, MO) for 10 min at 4°C to release the parasites from the host erythrocyte membrane (20). The parasite pellets were then sonicated in PBS containing 1% Triton X-100 and cocktail protease inhibitor (Roche Applied Science, Indianapolis, IN).…”

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Protective Properties and Surface Localization ofPlasmodium falciparumEnolase

et al. 2007

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The enolase protein of the human malarial parasite Plasmodium falciparum has recently been characterized. Apart from its glycolytic function, enolase has also been shown to possess antigenic properties and to be present on the cell wall of certain invasive organisms, such as Candida albicans. In order to assess whether enolase of P. falciparum is also antigenic, sera from residents of a region of Eastern India where malaria is endemic were tested against the recombinant P. falciparum enolase (r-Pfen) protein. About 96% of immune adult sera samples reacted with r-Pfen over and above the seronegative controls. Rabbit anti-r-Pfen antibodies inhibited the growth of in vitro cultures of P. falciparum. Mice immunized with r-Pfen showed protection against a challenge with the 17XL lethal strain of the mouse malarial parasite Plasmodium yoelii. The antibodies raised against r-Pfen were specific for Plasmodium and did not react to the host tissues. Immunofluorescence as well as electron microscopic examinations revealed localization of the enolase protein on the merozoite cell surface. These observations establish malaria enolase to be a potential protective antigen.Malaria continues to be a life-threatening infectious disease in the tropical world. Despite tremendous efforts to control the malaria epidemic, current prophylaxis and drug treatments are proving insufficient. The extensive spreading of drug-resistant Plasmodium strains as well as insecticide-resistant mosquitoes makes it urgent to develop an effective malaria vaccine. Long years of antigen identification and characterization have yielded many potential vaccine candidates, but developing an effective malaria vaccine has remained an incredibly difficult challenge (17). It has been observed that immunity to the disease develops gradually, after many attacks and over many years, in adults living in areas where malaria is endemic (2). The successful passive transfer of this immunity by injecting antibodies from malaria-immune persons to children susceptible to malaria has demonstrated that antibodies alone can trigger protection (5, 9, 58). These experiments have worked across geographical borders, as immunoglobulin G (IgG) from malaria-immune West Africans have cured East Africans as well as Thai malaria patients (5). The nature of this immunity is poorly understood at the molecular level. However, attempts have been made to identify antigens, the humoral response against which leads to protection. Seroepidemiological studies have identified several specific malarial blood-stage antigens including ring-infected erythrocyte surface antigen (10), apical membrane antigen (53), and PfP0, a conserved ribosomal protein (7,18,24), as protective antigens.Enolase has been reported to be present on the cell surface of several organisms (38). It is also considered to be a major immunostimulatory protein in the case of visceral leishmaniasis (19). Enolase has been demonstrated to play a protective role in Candida albicans infection (31, 41, 55). Recently, it has also been ...

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Identification of a Stomatin Orthologue in Vacuoles Induced in Human Erythrocytes by Malaria Parasites

Cited by 88 publications

References 60 publications

Plasmodium falciparum Pf34, a novel GPI-anchored rhoptry protein found in detergent-resistant microdomains

Plasmodium falciparum Pf34, a novel GPI-anchored rhoptry protein found in detergent-resistant microdomains

Export of virulence proteins by malaria-infected erythrocytes involves remodeling of host actin cytoskeleton

Protective Properties and Surface Localization ofPlasmodium falciparumEnolase

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