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Journal articles on the topic 'Erythrocytes Malaria Plasmodium falciparum'

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Published: 4 June 2021

Last updated: 1 February 2022

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1

Haldar, Kasturi, and Narla Mohandas. "Malaria, erythrocytic infection, and anemia." Hematology 2009, no. 1 (2009): 87–93. http://dx.doi.org/10.1182/asheducation-2009.1.87.

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Abstract Malaria is a major world health problem. It results from infection of parasites belonging to the genus Plasmodium. Plasmodium falciparum and Plasmodium vivax cause the major human malarias, with P falciparum being the more virulent. During their blood stages of infection, both P falciparum and P vivax induce anemia. Severe malarial anemia caused by P falciparum is responsible for approximately a third of the deaths associated with disease. Malarial anemia appears to be multi-factorial. It involves increased removal of circulating erythrocytes as well as decreased production of erythro

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2

Klotz, F. W., J. D. Chulay, W. Daniel, and L. H. Miller. "Invasion of mouse erythrocytes by the human malaria parasite, Plasmodium falciparum." Journal of Experimental Medicine 165, no. 6 (1987): 1713–18. http://dx.doi.org/10.1084/jem.165.6.1713.

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Plasmodium falciparum malaria merozoites require erythrocyte sialic acid for optimal invasion of human erythrocytes. Since mouse erythrocytes have the form of sialic acid found on human erythrocytes (N-acetyl neuraminic acid), mouse erythrocytes were tested for invasion in vitro. The Camp and 7G8 strains of P. falciparum invaded mouse erythrocytes at 17-45% of the invasion rate of human erythrocytes. Newly invaded mouse erythrocytes morphologically resembled parasitized human erythrocytes as shown on Giemsa-stained blood films and by electron microscopy. The rim of parasitized mouse erythrocyt

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3

Kirchgatter, Karin, and Hernando A. Del Portillo. "Clinical and molecular aspects of severe malaria." Anais da Academia Brasileira de Ciências 77, no. 3 (2005): 455–75. http://dx.doi.org/10.1590/s0001-37652005000300008.

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The erythrocytic cycle of Plasmodium falciparum presents a particularity in relation to other Plasmodium species that infect man. Mature trophozoites and schizonts are sequestered from the peripheral circulation due to adhesion of infected erythrocytes to host endothelial cells. Modifications in the surface of infected erythrocytes, termed knobs, seem to facilitate adhesion to endothelium and other erythrocytes. Adhesion provides better maturation in the microaerophilic venous atmosphere and allows the parasite to escape clearance by the spleen which recognizes the erythrocytes loss of deforma

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4

Willimann, K., H. Matile, N. A. Weiss, and B. A. Imhof. "In vivo sequestration of Plasmodium falciparum-infected human erythrocytes: a severe combined immunodeficiency mouse model for cerebral malaria." Journal of Experimental Medicine 182, no. 3 (1995): 643–53. http://dx.doi.org/10.1084/jem.182.3.643.

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Cerebral malaria is a fatal complication of infection by Plasmodium falciparum in man. The neurological symptoms that characterize this form of malarial disease are accompanied by the adhesion of infected erythrocytes to the vasculature of the brain. To study this phenomenon in vivo, an acute phase severe combined immunodeficiency (SCID) mouse model was developed in which sequestration of P. falciparum-infected human erythrocytes took place. During acute cerebral malaria in humans, the expression of intercellular adhesion molecule-1 (ICAM-1) is induced in vascular endothelium by inflammatory r

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5

Kaur, Prabhjot, Arun Bhatia, Kanav Midha, and Mampi Debnath. "Malaria: A Cause of Anemia and Its Effect on Pregnancy." World Journal of Anemia 1, no. 2 (2017): 51–62. http://dx.doi.org/10.5005/jp-journals-10065-0012.

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ABSTRACT Malaria is one of the major health problems in the world. It remains an important cause of very high human morbidity and mortality, especially, among children and pregnant women. It results from the infection of parasites belonging to the genus Plasmodium. Plasmodium falciparum and Plasmodium vivax are the major pathogens responsible for causing human malaria. Approximately 75% of cases are caused by P. falciparum and associated with the mortality rate of approximately 0.5 to 1.0%. Both P. falciparum and P. vivax induce anemia during their erythrocytic stages of infection. Most of the

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6

Muniz-Junqueira, Maria Imaculada, and Carlos Eduardo Tosta. "Stages of in vitro phagocytosis of Plasmodium falciparum-infected erythrocytes by human monocytes." Revista da Sociedade Brasileira de Medicina Tropical 42, no. 2 (2009): 103–6. http://dx.doi.org/10.1590/s0037-86822009000200001.

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Monocytes/macrophages play a critical role in the defense mechanisms against malaria parasites, and are the main cells responsible for the elimination of malaria parasites from the blood circulation. We carried out a microscope-aided evaluation of the stages of in vitro phagocytosis of Plasmodium falciparum-infected erythrocytes, by human monocytes. These cells were obtained from healthy adult individuals by means of centrifugation through a cushion of Percoll density medium and were incubated with erythrocytes infected with Plasmodium falciparum that had previously been incubated with a pool

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7

Kesely, Kristina, Panae Noomuna, Michal Vieth, et al. "Identification of tyrosine kinase inhibitors that halt Plasmodium falciparum parasitemia." PLOS ONE 15, no. 11 (2020): e0242372. http://dx.doi.org/10.1371/journal.pone.0242372.

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Although current malaria therapies inhibit pathways encoded in the parasite’s genome, we have looked for anti-malaria drugs that can target an erythrocyte component because development of drug resistance might be suppressed if the parasite cannot mutate the drug’s target. In search for such erythrocyte targets, we noted that human erythrocytes express tyrosine kinases, whereas the Plasmodium falciparum genome encodes no obvious tyrosine kinases. We therefore screened a library of tyrosine kinase inhibitors from Eli Lilly and Co. in a search for inhibitors with possible antimalarial activity. W

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8

Fujioka, H., and M. Aikawa. "Molecular Pathogenesis of Cerebral Malaria." Microscopy and Microanalysis 3, S2 (1997): 39–40. http://dx.doi.org/10.1017/s143192760000708x.

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Plasmodium falciparum, the most malignant human malaria, is responsible for 2-3 million deaths annually. These infections often involve blockage of the cerebral microvasculature by P. falciparum-infected erythrocytes (Fig. 1). This aspect is considered the major factor in the pathogenesis of cerebral malaria.Upon invasion of the erythrocyte, P. falciparum immediately begins to remodel the infected erythrocyte. The adherence points of infected erythrocytes, termed knobs (Fig. 2 and 3), contain antigenically diverse 200-350kDa surface proteins (PfEMPl; Fig. 4). The PfEMPl variant surface protein

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9

Murphy, Sean C., Souvik Bhattacharjee, Travis Harrison, and Kasturi Haldar. "Accessing the Erythrocyte Cytoplasm: A Method for Manipulating the Intracellular Environment of Erythrocytes for the Study of Malaria Invasion, Trafficking and Growth." Blood 104, no. 11 (2004): 3688. http://dx.doi.org/10.1182/blood.v104.11.3688.3688.

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Abstract Invasion of erythrocytes by malaria parasites requires participation of both parasite ligands and host determinants. Further recent studies show that erythrocyte G protein signaling regulates malarial infection. Many of the Gs-associated signaling components reside on the cytoplasmic leaflet of the erythrocyte plasma membrane, rendering them inaccessible to most extracellular probes. Since erythrocytes are enucleated and terminally differentiated, they cannot be transfected to express exogenous transgenes. We have modified methods of hypotonic lysis and isotonic resealing to generate

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10

López, José A. "Malignant malaria and microangiopathies: merging mechanisms." Blood 115, no. 7 (2010): 1317–18. http://dx.doi.org/10.1182/blood-2009-12-254060.

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Abstract In this issue of Blood, Bridges and colleagues report that Plasmodium falciparum–infected erythrocytes are able to attach to the endothelial surface by binding platelet-decorated VWF strands in a CD36-dependent fashion, revealing a new mechanism for erythrocyte cytoadherence in malaria.1

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11

Chitnis, C. E., and L. H. Miller. "Identification of the erythrocyte binding domains of Plasmodium vivax and Plasmodium knowlesi proteins involved in erythrocyte invasion." Journal of Experimental Medicine 180, no. 2 (1994): 497–506. http://dx.doi.org/10.1084/jem.180.2.497.

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Plasmodium vivax and the related monkey malaria, P. knowlesi, require interaction with the Duffy blood group antigen, a receptor for a family of chemokines that includes interleukin 8, to invade human erythrocytes. One P. vivax and three P. knowlesi proteins that serve as erythrocyte binding ligands in such interactions share sequence homology. Expression of different regions of the P. vivax protein in COS7 cells identified a cysteine-rich domain that bound Duffy blood group-positive but not Duffy blood group-negative human erythrocytes. The homologous domain of the P. knowlesi proteins also b

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12

Deans, Anne-Marie, Susana Nery, David J. Conway, Oscar Kai, Kevin Marsh, and J. Alexandra Rowe. "Invasion Pathways and Malaria Severity in Kenyan Plasmodium falciparum Clinical Isolates." Infection and Immunity 75, no. 6 (2007): 3014–20. http://dx.doi.org/10.1128/iai.00249-07.

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ABSTRACT The invasion of erythrocytes by Plasmodium falciparum occurs through multiple pathways that can be studied in vitro by examining the invasion of erythrocytes treated with enzymes such as neuraminidase, trypsin, and chymotrypsin. We have studied the invasion pathways used by 31 Kenyan P. falciparum isolates from children with uncomplicated or severe malaria. Six distinct invasion profiles were detected, out of eight possible profiles. The majority of isolates (23 of 31) showed neuraminidase-resistant, trypsin-sensitive invasion, characteristic of the pathway mediated by an unknown para

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13

Fernandez, Victor, Carl Johan Treutiger, Gerard B. Nash, and Mats Wahlgren. "Multiple Adhesive Phenotypes Linked to Rosetting Binding of Erythrocytes in Plasmodium falciparumMalaria." Infection and Immunity 66, no. 6 (1998): 2969–75. http://dx.doi.org/10.1128/iai.66.6.2969-2975.1998.

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ABSTRACT The cerebral form of severe malaria is associated with excessive intravascular sequestration of Plasmodium falciparum-infected erythrocytes (PRBC). Retention and accumulation of PRBC may lead to occlusion of brain microvessels and direct the triggering of acute pathologic changes. Here we report that by selection, cloning, and subcloning, we have identified rare P. falciparum parasites expressing a pan-adhesive phenotype linked to erythrocyte rosetting, a previously identified correlate of cerebral malaria. Rosetting PRBC not only bound uninfected erythrocytes but also formed autoaggl

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14

Omodeo-Salè, Fausta, Anna Motti, Nicoletta Basilico, Silvia Parapini, Piero Olliaro, and Donatella Taramelli. "Accelerated senescence of human erythrocytes cultured with Plasmodium falciparum." Blood 102, no. 2 (2003): 705–11. http://dx.doi.org/10.1182/blood-2002-08-2437.

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AbstractRed blood cells infected withPlasmodium falciparum(IRBCs) undergo changes primarily in their membrane composition that contribute to malaria pathogenesis. However, all manifestations (eg, anemia) cannot be accounted for by IRBCs alone. Uninfected erythrocytes (URBCs) may play a role, but they have been under-researched. We wanted to document changes in the erythrocyte membrane that could contribute to URBC reduced life span and malaria-associated anemia. Human erythrocytes were cultured withP falciparumand washed at the trophozoite stage. IRBCs and URBCs were separated on Percoll densi

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15

Moll, G. N., H. J. Vial, E. M. Bevers, et al. "Phospholipid asymmetry in the plasma membrane of malaria infected erythrocytes." Biochemistry and Cell Biology 68, no. 2 (1990): 579–85. http://dx.doi.org/10.1139/o90-083.

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The transbilayer distribution of glycerophospholipids in the plasma membrane of Plasmodium knowlesi infected erythrocytes was studied by using lysine-116-ε-N-palmitoyl amidinated pancreatic phospholipase A2. As a consequence of its superior membrane penetrating capacities, this modified enzyme rapidly degrades its substrates in the outer membrane leaflet of intact erythrocytes, a property that makes the enzyme an excellent tool to study the malaria parasitized red cell. The modified phospholipase A2 caused a nonlytic hydrolysis of up to 12–15% of the phosphatidylethanolamine and none of the ph

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16

Barrand, Margery A., Markus Winterberg, Frances Ng, Mai Nguyen, Kiaran Kirk, and Stephen B. Hladky. "Glutathione export from human erythrocytes and Plasmodium falciparum malaria parasites." Biochemical Journal 448, no. 3 (2012): 389–400. http://dx.doi.org/10.1042/bj20121050.

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Glutathione export from uninfected human erythrocytes was compared with that from cells infected with the malaria parasite Plasmodium falciparum using two separate methods that distinguish between oxidized (GSSG) and reduced (GSH) glutathione. One involved enzymatic recycling with or without thiol-masking; the other involved rapid derivatization followed by HPLC. Glutathione efflux from uninfected erythrocytes under physiological conditions occurred predominantly as GSH. On exposure of the cells to oxidative challenge, efflux of GSSG exceeded that of GSH. Efflux of both species was blocked by

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17

Lisk, Godfrey, and Sanjay A. Desai. "The Plasmodial Surface Anion Channel Is Functionally Conserved in Divergent Malaria Parasites." Eukaryotic Cell 4, no. 12 (2005): 2153–59. http://dx.doi.org/10.1128/ec.4.12.2153-2159.2005.

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ABSTRACT The plasmodial surface anion channel (PSAC), a novel ion channel induced on human erythrocytes infected with Plasmodium falciparum, mediates increased permeability to nutrients and presumably supports intracellular parasite growth. Isotope flux studies indicate that other malaria parasites also increase the permeability of their host erythrocytes, but the precise mechanisms are unknown. Channels similar to PSAC or alternative mechanisms, such as the upregulation of endogenous host transporters, might fulfill parasite nutrient demands. Here we evaluated these possibilities with rhesus

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18

Ch’ng, Jun-Hong, Kirsten Moll, Katja Wyss, et al. "Enhanced virulence of Plasmodium falciparum in blood of diabetic patients." PLOS ONE 16, no. 6 (2021): e0249666. http://dx.doi.org/10.1371/journal.pone.0249666.

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Rising prevalence of diabetes in sub-Saharan Africa, coupled with continued malaria transmission, has resulted more patients dealing with both communicable and non-communicable diseases. We previously reported that travelers with type 2 diabetes mellitus (T2DM) infected with Plasmodium falciparum were three times more likely to develop severe malaria than non-diabetics. Here we explore the biological basis for this by testing blood from uninfected subjects with type 1 and type 2 diabetes, ex vivo, for their effects on parasite growth and rosetting (binding of infected erythrocytes to uninfecte

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19

Chen, Qijun, Antonio Barragan, Victor Fernandez, et al. "Identification of Plasmodium falciparum Erythrocyte Membrane Protein 1 (PfEMP1) as the Rosetting Ligand of the Malaria Parasite P. falciparum." Journal of Experimental Medicine 187, no. 1 (1998): 15–23. http://dx.doi.org/10.1084/jem.187.1.15.

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Severe Plasmodium falciparum malaria is characterized by excessive sequestration of infected and uninfected erythrocytes in the microvasculature of the affected organ. Rosetting, the adhesion of P. falciparum–infected erythrocytes to uninfected erythrocytes is a virulent parasite phenotype associated with the occurrence of severe malaria. Here we report on the identification by single-cell reverse transcriptase PCR and cDNA cloning of the adhesive ligand P. falciparum erythrocyte membrane protein 1 (PfEMP1). Rosetting PfEMP1 contains clusters of glycosaminoglycan-binding motifs. A recombinant

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20

Pernod, Gilles, Benoît Polack, François Peyron, et al. "Monocyte Tissue Factor Expression Induced by Plasmodium falciparum-Infected Erythrocytes." Thrombosis and Haemostasis 68, no. 02 (1992): 111–14. http://dx.doi.org/10.1055/s-0038-1656333.

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SummaryMonocytes are active elements of the host response against Plasmodium falciparum. They are able to express tissue factor and trigger the extrinsic pathway of blood coagulation the activation of which remained unclear in malaria. Our aim was to assess the tissue factor expression of purified blood monocytes stimulated by cultured Plasmodium falciparum-infected erythrocytes. Malaria parasite induced an early generation of tissue factor with a peak between 8 and 12 h of stimulation. Maximum expression was observed for parasitemia ranging from 1 to 2%. Plasmodium falciparum culture supernat

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Kurniasih, Yulvina, and Reskiani Mulyani. "GAMBARAN ERITROSIT PADA SEDIAAN DARAH TEPI PASIEN MALARIA DI PUSKESMAS SUNGAI PANCUR." Jurnal Endurance 3, no. 2 (2018): 226. http://dx.doi.org/10.22216/jen.v3i2.1822.

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<p><em>Malaria is an infectious disease is acute or chronic, caused by Plasmodium that attack the erythrocytes, which erythrocytes are biconcave, basin (concave) function to provide a space in which hemoglobin would bind oxygen. Malaria is transmitted by the bite of a female Anopheles mosquito vectors that have been infected by Plasmodium sp. The research is descriptive cross sectional design of the research result description the shape, size, and color of blood cells, erythrocytes in blood clots malaria positive patients, using microscopy methods to manufacture thin blood smear st

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Aird, William C., Laurent O. Mosnier, and Rick M. Fairhurst. "Plasmodium falciparum picks (on) EPCR." Blood 123, no. 2 (2014): 163–67. http://dx.doi.org/10.1182/blood-2013-09-521005.

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Abstract Of all the outcomes of Plasmodium falciparum infection, the coma of cerebral malaria (CM) is particularly deadly. Malariologists have long wondered how some patients develop this organ-specific syndrome. Data from two recent publications support a novel mechanism of CM pathogenesis in which infected erythrocytes (IEs) express specific virulence proteins that mediate IE binding to the endothelial protein C receptor (EPCR). Malaria-associated depletion of EPCR, with subsequent impairment of the protein C system promotes a proinflammatory, procoagulant state in brain microvessels.

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23

Hsiao, L. L., R. J. Howard, M. Aikawa, and T. F. Taraschi. "Modification of host cell membrane lipid composition by the intra-erythrocytic human malaria parasite Plasmodium falciparum." Biochemical Journal 274, no. 1 (1991): 121–32. http://dx.doi.org/10.1042/bj2740121.

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The phospholipid and fatty acid compositions of the host infected erythrocyte plasma membrane (IEPM) have been determined for erythrocytes infected with the human malaria parasite Plasmodium falciparum. IEPM were prepared by selective lysis of the host erythrocyte (but not of the parasite membranes) with 0.1% saponin, followed by differential centrifugation. The purity of the IEPM was determined by measuring the membrane-specific enzyme markers acetylcholinesterase, glutamate dehydrogenase and lactate dehydrogenase, and by immunoelectron microscopy using monoclonal antibodies specific for huma

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Struik, Siske S., Fakhreldin M. Omer, Katerina Artavanis-Tsakonas, and Eleanor M. Riley. "Uninfected erythrocytes inhibit Plasmodium falciparum–induced cellular immune responses in whole-blood assays." Blood 103, no. 8 (2004): 3084–92. http://dx.doi.org/10.1182/blood-2003-08-2867.

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Abstract Whole-blood assays (WBAs) have been successfully used as a simple tool for immuno-epidemiological field studies evaluating cellular immune responses to mycobacterial and viral antigens. Rather unexpectedly, we found very poor cytokine responses to malaria antigens in WBAs in 2 immuno-epidemiological studies carried out in malaria endemic populations in Africa. We have therefore conducted a detailed comparison of cellular immune responses to live (intact) and lysed malaria-infected erythrocytes in WBAs and in peripheral blood mononuclear cell (PBMC) cultures. We observed profound inhib

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Staunton, D. E., C. F. Ockenhouse, and T. A. Springer. "Soluble intercellular adhesion molecule 1-immunoglobulin G1 immunoadhesin mediates phagocytosis of malaria-infected erythrocytes." Journal of Experimental Medicine 176, no. 5 (1992): 1471–76. http://dx.doi.org/10.1084/jem.176.5.1471.

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We describe an immunoadhesin molecule containing intercellular adhesion molecule 1 (ICAM-1) molecularly fused to hinge and CH2 and CH3 domains of the human immunoglobulin G1 H chain that binds Plasmodium falciparum-infected erythrocytes. This receptor-based immunoadhesin is an effective and specific inhibitor of P. falciparum-infected erythrocyte adhesion to ICAM-1-bearing surfaces, but does not inhibit leukocyte function antigen 1 (LFA-1) interaction with ICAM-1. Furthermore, the immunoadhesin promotes phagocytosis and destruction of parasitized erythrocytes by human monocytes. Each of these

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Lantero, Elena, Alexandros Belavilas-Trovas, Arnau Biosca, et al. "Development of DNA Aptamers Against Plasmodium falciparum Blood Stages Using Cell-Systematic Evolution of Ligands by EXponential Enrichment." Journal of Biomedical Nanotechnology 16, no. 3 (2020): 315–34. http://dx.doi.org/10.1166/jbn.2020.2901.

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New biomarkers have to be developed in order to increase the performance of current antigen-based malaria rapid diagnosis. Antibody production often involves the use of laboratory animals and is time-consuming and costly, especially when the target is Plasmodium, whose variable antigen expression complicates the development of long-lived biomarkers. To circumvent these obstacles, we have applied the Systematic Evolution of Ligands by EXponential enrichment method to the rapid identification of DNA aptamers against Plasmodium falciparum-infected red blood cells (pRBCs). Five 70 b-long ssDNA seq

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Donati, Daria, Li Ping Zhang, Qijun Chen, et al. "Identification of a Polyclonal B-Cell Activator in Plasmodium falciparum." Infection and Immunity 72, no. 9 (2004): 5412–18. http://dx.doi.org/10.1128/iai.72.9.5412-5418.2004.

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ABSTRACT Polyclonal B-cell activation and hypergammaglobulinemia are prominent features of human malaria. We report here that Plasmodium falciparum-infected erythrocytes directly adhere to and activate peripheral blood B cells from nonimmune donors. The infected erythrocytes employ the cysteine-rich interdomain region 1α (CIDR1α) of P. falciparum erythrocyte membrane protein 1 (PfEMP1) to interact with the B cells. Stimulation with recombinant CIDR1α induces proliferation, an increase in B-cell size, expression of activation molecules, and secretion of immunoglobulins (immunoglobulin M) and cy

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Templeton, Thomas J., David B. Keister, Olga Muratova, Jo Lynn Procter, and David C. Kaslow. "Adherence of Erythrocytes during Exflagellation of Plasmodium falciparum Microgametes Is Dependent on Erythrocyte Surface Sialic Acid and Glycophorins." Journal of Experimental Medicine 187, no. 10 (1998): 1599–609. http://dx.doi.org/10.1084/jem.187.10.1599.

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Malaria male gametocytes within a newly ingested infected blood meal in the mosquito midgut emerge from erythrocytes and extrude approximately eight flagellar microgametes in a process termed exflagellation. In culture, and in blood removed from infected patients, emerging microgametes avidly adhere to neighboring uninfected and infected erythrocytes, as well as to emerged female macrogametes, creating “exflagellation centers”. The mechanism of erythrocyte adherence is not known nor has it been determined for what purpose microgametes may bind to erythrocytes. The proposition of a function und

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Parker, Phillip D., Leann Tilley, and Nectarios Klonis. "Plasmodium falciparum induces reorganization of host membrane proteins during intraerythrocytic growth." Blood 103, no. 6 (2004): 2404–6. http://dx.doi.org/10.1182/blood-2003-08-2692.

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Abstract The virulence of the malaria parasite, Plasmodium falciparum, is due in large part to the way in which it modifies the membrane of its erythrocyte host. In this work we have used confocal microscopy and fluorescence recovery after photo-bleaching to examine the lateral mobility of host membrane proteins in erythrocytes infected with P falciparum at different stages of parasite growth. The erythrocyte membrane proteins band 3 and glycophorin show a marked decrease in mobility during the trophozoite stage of growth. Erythrocytes infected with a parasite strain that does not express the

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Adisa, Akinola, Frank R. Albano, John Reeder, Michael Foley, and Leann Tilley. "Evidence for a role for a Plasmodium falciparum homologue of Sec31p in the export of proteins to the surface of malaria parasite-infected erythrocytes." Journal of Cell Science 114, no. 18 (2001): 3377–86. http://dx.doi.org/10.1242/jcs.114.18.3377.

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The malaria parasite, Plasmodium falciparum, spends part of its life cycle inside the enucleated erythrocytes of its human host. The parasite modifies the cytoplasm and plasma membrane of its host cell by exporting proteins beyond the confines of its own plasma membrane. We have previously provided evidence that a plasmodial homologue of the COPII protein, Sar1p, is involved in the trafficking of proteins across the erythrocyte cytoplasm. We have now characterised an additional plasmodial COPII protein homologue, namely Sec31p. Recombinant proteins corresponding to the WD-40 and the intervenin

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Sanyal, Sohini, Stéphane Egée, Guillaume Bouyer, et al. "Plasmodium falciparum STEVOR proteins impact erythrocyte mechanical properties." Blood 119, no. 2 (2012): e1-e8. http://dx.doi.org/10.1182/blood-2011-08-370734.

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Infection of erythrocytes with the human malaria parasite, Plasmodium falciparum, results in dramatic changes to the host cell structure and morphology. The predicted functional localization of the STEVOR proteins at the erythrocyte surface suggests that they may be involved in parasite-induced modifications of the erythrocyte membrane during parasite development. To address the biologic function of STEVOR proteins, we subjected a panel of stevor transgenic parasites and wild-type clonal lines exhibiting different expression levels for stevor genes to functional assays exploring parasite-induc

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Garred, Peter, Morten A. Nielsen, Jørgen A. L. Kurtzhals, et al. "Mannose-Binding Lectin Is a Disease Modifier in Clinical Malaria and May Function as Opsonin for Plasmodium falciparum- Infected Erythrocytes." Infection and Immunity 71, no. 9 (2003): 5245–53. http://dx.doi.org/10.1128/iai.71.9.5245-5253.2003.

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ABSTRACT Variant alleles in the mannose-binding lectin (MBL) gene (mbl2) causing low levels of functional MBL are associated with susceptibility to different infections and are common in areas where malaria is endemic. Therefore, we investigated whether MBL variant alleles in 551 children from Ghana were associated with the occurrence and outcome parameters of Plasmodium falciparum malaria and asked whether MBL may function as an opsonin for P. falciparum. No difference in MBL genotype frequency was observed between infected and noninfected children or between children with cerebral malaria an

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Uskov, A. N., A. I. Soloviev, V. Yu Kravtsov, R. V. Gudkov, E. V. Kolomoets, and A. E. Levkovskiy. "MOLECULAR-GENETIC MECHANISMS OF PLASMODIUM FALCIPARUM VIRULENCE AND TROPICAL MALARIA PATHOGENESIS." Journal Infectology 10, no. 3 (2018): 23–29. http://dx.doi.org/10.22625/2072-6732-2018-10-3-23-29.

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There is introduced the analysis of molecular-genetic mechanisms of tropical malaria pathogenesis and P. falciparum virulence. It is shown, that pathogenesis of tropical malaria is associated with the properties of red blood cells membrane surface (RBCs or erythrocytes) that are infected by P. falciparum. There are «knobs structures» on membrane surface infected RBCs. Knobs structures contains a complex of P. falciparum proteins – PfEMP1 (Plasmodium falciparum erythrocyte membrane protein 1). PfEMP1 is associated with virulence of P. falciparum. Complex PfEMP1 has difficult polymorphous struct

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Mo, Min, Hooi Chen Lee, Masayo Kotaka, et al. "The C-Terminal Segment of the Cysteine-Rich Interdomain of Plasmodium falciparum Erythrocyte Membrane Protein 1 Determines CD36 Binding and Elicits Antibodies That Inhibit Adhesion of Parasite-Infected Erythrocytes." Infection and Immunity 76, no. 5 (2008): 1837–47. http://dx.doi.org/10.1128/iai.00480-07.

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ABSTRACT Attachment of erythrocytes infected by Plasmodium falciparum to receptors of the microvasculature is a major contributor to the pathology and morbidity associated with malaria. Adhesion is mediated by the P. falciparum erythrocyte membrane protein 1 (PfEMP-1), which is expressed at the surface of infected erythrocytes and is linked to both antigenic variation and cytoadherence. PfEMP-1 contains multiple adhesive modules, including the Duffy binding-like domain and the cysteine-rich interdomain region (CIDR). The interaction between CIDRα and CD36 promotes stable adherence of parasitiz

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Chattopadhyay, Rana, Amit Sharma, Vinod K. Srivastava, et al. "Plasmodium falciparum Infection Elicits Both Variant-Specific and Cross-Reactive Antibodies against Variant Surface Antigens." Infection and Immunity 71, no. 2 (2003): 597–604. http://dx.doi.org/10.1128/iai.71.2.597-604.2003.

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ABSTRACT Naturally acquired antibodies to Plasmodium falciparum erythrocyte membrane protein-1 (PfEMP-1), the variant surface antigens expressed on the surface of infected erythrocytes, are thought to play a role in protection against P. falciparum malaria. Here, we have studied the development of antibodies to PfEMP-1 in adult malaria patients living in Rourkela, India, an area with a low malaria transmission rate, and prevalence of antibodies to PfEMP-1 in residents of San Dulakudar, India, a village in which P. falciparum malaria is hyperendemic. Convalescent-phase sera from adult malaria p

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VOGT, Anna M., Gerhard WINTER, Mats WAHLGREN, and Dorothe SPILLMANN. "Heparan sulphate identified on human erythrocytes: a Plasmodium falciparum receptor." Biochemical Journal 381, no. 3 (2004): 593–97. http://dx.doi.org/10.1042/bj20040762.

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HS (heparan sulphate) has hitherto not been found on human red blood cells (RBCs, erythrocytes). However, malarial-parasite (Plasmodium falciparum)-infected RBCs adhere to uninfected RBCs via HS-like receptors. In the present paper we demonstrate that human RBCs carry epitopes for an anti-HS antibody. Glycans isolated from RBC membranes reacted to HS-specific degradations and adhered to an HS-binding malaria antigen. Additionally, an HS core protein was identified. This suggests that HS is present on human RBCs.

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Okoyeh, Jude Nnaemeka, C. R. Pillai, and Chetan E. Chitnis. "Plasmodium falciparum Field Isolates Commonly Use Erythrocyte Invasion Pathways That Are Independent of Sialic Acid Residues of Glycophorin A." Infection and Immunity 67, no. 11 (1999): 5784–91. http://dx.doi.org/10.1128/iai.67.11.5784-5791.1999.

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ABSTRACT Erythrocyte invasion by malaria parasites is mediated by specific molecular interactions. Sialic acid residues of glycophorin A are used as invasion receptors by Plasmodium falciparum. In vitro invasion studies have demonstrated that some cloned P. falciparum lines can use alternate receptors independent of sialic acid residues of glycophorin A. It is not known if invasion by alternate pathways occurs commonly in the field. In this study, we used in vitro growth assays and erythrocyte invasion assays to determine the invasion phenotypes of 15 P. falciparum field isolates. Of the 15 fi

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Moonah, Shannon, Natalie G. Sanders, Jason K. Persichetti, and David J. Sullivan. "Erythrocyte Lysis and Xenopus laevis Oocyte Rupture by Recombinant Plasmodium falciparum Hemolysin III." Eukaryotic Cell 13, no. 10 (2014): 1337–45. http://dx.doi.org/10.1128/ec.00088-14.

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ABSTRACTMalaria kills more than 1 million people per year worldwide, with severe malaria anemia accounting for the majority of the deaths. Malaria anemia is multifactorial in etiology, including infected erythrocyte destruction and decrease in erythrocyte production, as well as destruction or clearance of noninfected erythrocytes. We identified a panspeciesPlasmodiumhemolysin type III related to bacterial hemolysins. The identification of a hemolysin III homologue inPlasmodiumsuggests a potential role in host erythrocyte lysis. Here, we report the first characterization ofPlasmodium falciparum

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Dijkman, Patricia M., Tanja Marzluf, Yingyi Zhang, et al. "Structure of the merozoite surface protein 1 from Plasmodium falciparum." Science Advances 7, no. 23 (2021): eabg0465. http://dx.doi.org/10.1126/sciadv.abg0465.

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The merozoite surface protein 1 (MSP-1) is the most abundant protein on the surface of the erythrocyte-invading Plasmodium merozoite, the causative agent of malaria. MSP-1 is essential for merozoite formation, entry into and escape from erythrocytes, and is a promising vaccine candidate. Here, we present monomeric and dimeric structures of full-length MSP-1. MSP-1 adopts an unusual fold with a large central cavity. Its fold includes several coiled-coils and shows structural homology to proteins associated with membrane and cytoskeleton interactions. MSP-1 formed dimers through these domains in

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Tham, Wai-Hong, Danny W. Wilson, Linda Reiling, Lin Chen, James G. Beeson, and Alan F. Cowman. "Antibodies to Reticulocyte Binding Protein-Like Homologue 4 Inhibit Invasion of Plasmodium falciparum into Human Erythrocytes." Infection and Immunity 77, no. 6 (2009): 2427–35. http://dx.doi.org/10.1128/iai.00048-09.

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ABSTRACT Plasmodium falciparum invasion into human erythrocytes relies on the interaction between multiple parasite ligands and their respective erythrocyte receptors. The sialic acid-independent invasion pathway is dependent on the expression of P. falciparum reticulocyte binding protein-like homologue 4 (PfRh4), as disruption of the gene abolishes the ability of parasites to switch to this pathway. We show that PfRh4 is present as an invasion ligand in culture supernatants as a 160-kDa proteolytic fragment. We confirm that PfRh4 binds to the surfaces of erythrocytes through recognition of an

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Clough, B., F. A. Atilola, N. Healy, et al. "Plasmodium falciparum lacks sialidase and trans-sialidase activity." Parasitology 112, no. 5 (1996): 443–49. http://dx.doi.org/10.1017/s0031182000076903.

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SUMMARYSialic acid on the red cell surface plays a major role in invasion by the malaria parasite Plasmodium falciparum. The NeuAc(α2,3) Gal motif on the O-linked tetrasaccharides of the red cell glycophorins is a recognition site for the parasite erythrocyte-binding antigen (EBA-175). Consequently, the interaction of P. falciparum and the red cell might share homology with that of the influenza virus. The cellular interactions of P. falciparum were examined for their sensitivity to 4-guanidino-2,3-didehydro-D-N-acetyl neuraminic acid (4-guanidino Neu5Ac2en), a potent inhibitor of influenza vi

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Orjih, Augustine U. "Requirements for Maximal Enrichment of Viable Intraerythrocytic Plasmodium falciparum Rings by Saponin Hemolysis." Experimental Biology and Medicine 233, no. 11 (2008): 1359–67. http://dx.doi.org/10.3181/0804-rm-129.

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The purpose of the present study was to confirm the effectiveness of saponin hemolysis for concentrating ring-infected erythrocytes in Plasmodium falciparum cultures and to determine the actual numbers of the enriched parasites, not just percentage parasitemia. This is important because various molecular biology and vaccine development against malaria require useable quantities of pure culture with minimal number of uninfected erythrocytes at all stages. Synchronized cultures of three P. falciparum strains were exposed to 0.015% isotonic saponin solution for 30 minutes on ice. They were centri

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Arumugam, Thangavelu U., Satoru Takeo, Tsutomu Yamasaki, et al. "Discovery of GAMA, a Plasmodium falciparum Merozoite Micronemal Protein, as a Novel Blood-Stage Vaccine Candidate Antigen." Infection and Immunity 79, no. 11 (2011): 4523–32. http://dx.doi.org/10.1128/iai.05412-11.

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ABSTRACTOne of the solutions for reducing the global mortality and morbidity due to malaria is multivalent vaccines comprising antigens of several life cycle stages of the malarial parasite. Hence, there is a need for supplementing the current set of malaria vaccine candidate antigens. Here, we aimed to characterize glycosylphosphatidylinositol (GPI)-anchored micronemal antigen (GAMA) encoded by the PF08_0008 gene inPlasmodium falciparum. Antibodies were raised against recombinant GAMA synthesized by using a wheat germ cell-free system. Immunoelectron microscopy demonstrated for the first time

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Howard, R. J., J. A. Lyon, S. Uni, et al. "Transport of an Mr approximately 300,000 Plasmodium falciparum protein (Pf EMP 2) from the intraerythrocytic asexual parasite to the cytoplasmic face of the host cell membrane." Journal of Cell Biology 104, no. 5 (1987): 1269–80. http://dx.doi.org/10.1083/jcb.104.5.1269.

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The profound changes in the morphology, antigenicity, and functional properties of the host erythrocyte membrane induced by intraerythrocytic parasites of the human malaria Plasmodium falciparum are poorly understood at the molecular level. We have used mouse mAbs to identify a very large malarial protein (Mr approximately 300,000) that is exported from the parasite and deposited on the cytoplasmic face of the erythrocyte membrane. This protein is denoted P. falciparum erythrocyte membrane protein 2 (Pf EMP 2). The mAbs did not react with the surface of intact infected erythrocytes, nor was Pf

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Chen, Qijun, Andreas Heddini, Antonio Barragan, Victor Fernandez, S. Frieda A. Pearce, and Mats Wahlgren. "The Semiconserved Head Structure of Plasmodium falciparum Erythrocyte Membrane Protein 1 Mediates Binding to Multiple Independent Host Receptors." Journal of Experimental Medicine 192, no. 1 (2000): 1–10. http://dx.doi.org/10.1084/jem.192.1.1.

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Erythrocytes infected with mature forms of Plasmodium falciparum do not circulate but are withdrawn from the peripheral circulation; they are bound to the endothelial lining and to uninfected erythrocytes in the microvasculature. Blockage of the blood flow, hampered oxygen delivery, and severe malaria may follow if binding is excessive. The NH2-terminal head structure (Duffy binding–like domain 1 [DBL1α]–cysteine-rich interdomain region [CIDR1α]) of a single species of P. falciparum erythrocyte membrane protein 1 (PfEMP1) is here shown to mediate adherence to multiple host receptors including

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Mitchell, GH, TJ Hadley, MH McGinniss, FW Klotz, and LH Miller. "Invasion of erythrocytes by Plasmodium falciparum malaria parasites: evidence for receptor heterogeneity and two receptors." Blood 67, no. 5 (1986): 1519–21. http://dx.doi.org/10.1182/blood.v67.5.1519.1519.

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Abstract Plasmodium falciparum malaria parasites with different capabilities of invading sialic acid-deficient erythrocytes were identified. Thai-2 parasites cultured in Tn erythrocytes invaded neuraminidase-treated and Tn erythrocytes twice as efficiently as Thai-2 parasites cultured in normal erythrocytes and seven to ten times more efficiently than a cloned line of Camp parasites cultured in normal erythrocytes. All three parasite lines required sialic acid for optimal invasion, but Thai-2 parasites cultured in Tn erythrocytes invaded neuraminidase- treated erythrocytes with 45% efficiency

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Mitchell, GH, TJ Hadley, MH McGinniss, FW Klotz, and LH Miller. "Invasion of erythrocytes by Plasmodium falciparum malaria parasites: evidence for receptor heterogeneity and two receptors." Blood 67, no. 5 (1986): 1519–21. http://dx.doi.org/10.1182/blood.v67.5.1519.bloodjournal6751519.

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Plasmodium falciparum malaria parasites with different capabilities of invading sialic acid-deficient erythrocytes were identified. Thai-2 parasites cultured in Tn erythrocytes invaded neuraminidase-treated and Tn erythrocytes twice as efficiently as Thai-2 parasites cultured in normal erythrocytes and seven to ten times more efficiently than a cloned line of Camp parasites cultured in normal erythrocytes. All three parasite lines required sialic acid for optimal invasion, but Thai-2 parasites cultured in Tn erythrocytes invaded neuraminidase- treated erythrocytes with 45% efficiency whereas C

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Urban, Britta C., Tran T. Hien, Nicholas P. Day, et al. "Fatal Plasmodium falciparum Malaria Causes Specific Patterns of Splenic Architectural Disorganization." Infection and Immunity 73, no. 4 (2005): 1986–94. http://dx.doi.org/10.1128/iai.73.4.1986-1994.2005.

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ABSTRACT The spleen is critical for host defense against pathogens, including Plasmodium falciparum. It has a dual role, not only removing aged or antigenically altered erythrocytes from the blood but also as the major lymphoid organ for blood-borne or systemic infections. The human malaria parasite P. falciparum replicates within erythrocytes during asexual blood stages and causes repeated infections that can be associated with severe disease. In spite of the crucial role of the spleen in the innate and acquired immune response to malaria, there is little information on the pathology of the s

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Li, Xuerong, Sonja B. Lauterbach, Roberto Lanzillotti, et al. "Receptor-Based Identification of Novel Peptide Ligands as Inhibitors of Blood Stage Malaria." Blood 110, no. 11 (2007): 139. http://dx.doi.org/10.1182/blood.v110.11.139.139.

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Abstract Malaria parasite Plasmodium falciparum uses multiple receptors on the surface of human red blood cells to attach and invade host cells during blood stage infection. Glycophorins, including glycophorin A, B, and C have been implicated as host receptors and play an important role during Plasmodium falciparum invasion in human erythrocytes, particularly in the sialic acid-dependent parasite strains. To identify the parasite proteins that could bind to human glycophorins, we screened a phage display cDNA library of P. falciparum (FCR3 strain, a sialic acid-dependent strain) using human gl

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Mayor, Alfredo, Nivedita Bir, Ritica Sawhney, et al. "Receptor-binding residues lie in central regions of Duffy-binding–like domains involved in red cell invasion and cytoadherence by malaria parasites." Blood 105, no. 6 (2005): 2557–63. http://dx.doi.org/10.1182/blood-2004-05-1722.

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AbstractErythrocyte invasion by malaria parasites and cytoadherence of Plasmodium falciparum-infected erythrocytes to host capillaries are 2 key pathogenic mechanisms in malaria. The receptor-binding domains of erythrocyte-binding proteins (EBPs) such as Plasmodium falciparum EBA-175, which mediate invasion, and P falciparum erythrocyte membrane protein 1 (PfEMP-1) family members, which are encoded by var genes and mediate cytoadherence, have been mapped to conserved cysteine-rich domains referred to as Duffy-binding–like (DBL) domains. Here, we have mapped regions within DBL domains from EBPs

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