Malarial Proteins at the Membrane of Plasmodium falciparum-Infected Erythrocytes and Their Involvement in Cytoadherence to Endothelial Cells

2015 ◽  
pp. 98-147
Author(s):  
Russell J. Howard
Keyword(s):  
Endothelial Cells ◽  
Plasmodium Falciparum

scholarly journals Direct Activation of Human Endothelial Cells by Plasmodium falciparum-Infected Erythrocytes

2005 ◽  
Vol 73 (6) ◽  
pp. 3271-3277 ◽  
Author(s):  
Nicola K. Viebig ◽  
Ulrich Wulbrand ◽  
Reinhold Förster ◽  
Katherine T. Andrews ◽  
Michael Lanzer ◽  
...  
Keyword(s):  
Endothelial Cells ◽  
Plasmodium Falciparum ◽  
Endothelial Cell ◽  
Adhesion Molecule ◽  
Cell Activation ◽  
Physical Contact ◽  
Intercellular Adhesion Molecule ◽  
Immune Reactivity ◽  
Human Endothelial Cells ◽  
Tnf Α

ABSTRACT Cytoadherence of Plasmodium falciparum-infected erythrocytes (PRBC) to endothelial cells causes severe clinical disease, presumably as a of result perfusion failure and tissue hypoxia. Cytoadherence to endothelial cells is increased by endothelial cell activation, which is believed to occur in a paracrine fashion by mediators such as tumor necrosis factor alpha (TNF-α) released from macrophages that initially recognize PRBC. Here we provide evidence that PRBC directly stimulate human endothelial cells in the absence of macrophages, leading to increased expression of adhesion-promoting molecules, such as intercellular adhesion molecule 1. Endothelial cell stimulation by PRBC required direct physical contact for a short time (30 to 60 min) and was correlated with parasitemia. Gene expression profiling of endothelial cells stimulated by PRBC revealed increased expression levels of chemokine and adhesion molecule genes. PRBC-stimulated endothelial cells especially showed increased expression of molecules involved in parasite adhesion but failed to express molecules promoting leukocyte adhesion, such as E-selectin and vascular cell adhesion molecule 1, even after challenge with TNF-α. Collectively, our data suggest that stimulation of endothelial cells by PRBC may have two effects: prevention of parasite clearance through increased cytoadherence and attenuation of leukocyte binding to endothelial cells, thereby preventing deleterious immune reactivity.

scholarly journals CD36 Peptides That Block Cytoadherence Define the CD36 Binding Region for Plasmodium falciparum-Infected Erythrocytes

Blood ◽  
1999 ◽  
Vol 94 (6) ◽  
pp. 2121-2127 ◽  
Author(s):  
Dror I. Baruch ◽  
Xin C. Ma ◽  
Brittan Pasloske ◽  
Russell J. Howard ◽  
Louis H. Miller
Keyword(s):  
Endothelial Cells ◽  
Plasmodium Falciparum ◽  
Scavenger Receptor ◽  
Intercellular Adhesion Molecule ◽  
Microvascular Endothelial Cells ◽  
Binding Region ◽  
Intercellular Adhesion Molecule 1 ◽  
Severe Pathology ◽  
Variant Antigen ◽  
Micromolar Range

Abstract Mature Plasmodium falciparum parasitized erythrocytes (PE) sequester from the circulation by adhering to microvascular endothelial cells. PE sequestration contributes directly to the virulence and severe pathology of falciparum malaria. The scavenger receptor, CD36, is a major host receptor for PE adherence. PE adhesion to CD36 is mediated by the malarial variant antigen, P. falciparumerythrocyte membrane protein 1 (PfEMP1), and particularly by its cysteine-rich interdomain region 1 (CIDR-1). Several peptides from the extended immunodominant domain of CD36 (residues 139-184), including CD36 139-155, CD36 145-171, CD36 146-164, and CD36 156-184 interfered with the CD36-PfEMP1 interaction. Each of these peptides affected binding at the low micromolar range in 2 independent assays. Two peptides, CD36 145-171 and CD36 156-184, specifically blocked PE adhesion to CD36 without affecting binding to the host receptor intercellular adhesion molecule-1 (ICAM-1). Moreover, an adhesion blocking peptide from the ICAM-1 sequence inhibits the PfEMP1–ICAM-1 interaction without affecting adhesion to CD36. These results confirm earlier observations that PfEMP1 is also a receptor for ICAM-1. Thus, the region 139-184 and particularly the 146-164 or the 145-171 regions of CD36 form the adhesion region for P. falciparum PE. Adherence blocking peptides from this region may be useful for modeling the PE/PfEMP1 interaction with CD36 and for development of potential anti-adhesion therapeutics.

Circulating endothelial cells in severe Plasmodium falciparum infection

2019 ◽  
Vol 72 ◽  
pp. 101926 ◽  
Author(s):  
Bahaa El-Deen W. El-Aswad ◽  
Ahmed A. Sonbol ◽  
Ismail M. Moharm ◽  
Samar A. El-Refai ◽  
Hosam El-Din M. Seleem ◽  
...  
Keyword(s):  
Endothelial Cells ◽  
Plasmodium Falciparum ◽  
Falciparum Infection ◽  
Circulating Endothelial Cells ◽  
Plasmodium Falciparum Infection

Adhesion of normal and Plasmodium falciparum ring–infected erythrocytes to endothelial cells and the placenta involves the rhoptry-derived ring surface protein-2

Blood ◽  
2003 ◽  
Vol 101 (12) ◽  
pp. 5025-5032 ◽  
Author(s):  
Jean-Bernard Lekana Douki ◽  
Yvon Sterkers ◽  
Catherine Lépolard ◽  
Boubacar Traoré ◽  
Fabio T. M. Costa ◽  
...  
Keyword(s):  
Endothelial Cells ◽  
Plasmodium Falciparum ◽  
Erythrocyte Membrane ◽  
Time Course ◽  
Surface Protein ◽  
Blood Stage ◽  
Current View ◽  
Ring Stage ◽  
Surface Fluorescence ◽  
Falciparum Erythrocyte Membrane Protein

Abstract Recent findings have challenged the current view of Plasmodium falciparum (P falciparum) blood-stage biology by demonstrating the cytoadhesion of early ring-stage–infected erythrocytes (rIEs) to host endothelial cells and placental syncytiotrophoblasts. The adhesion of rIEs was observed only in parasites that bind to the placenta via chondroitin sulfate A (CSA). In this work, a panel of mouse monoclonal antibodies (mAbs) that specifically inhibit cytoadhesion of rIEs but not of mature IEs was generated The previously described ring surface protein 2 (RSP-2), a 42-kDa protein, was identified as the target of the ring-stage–specific mAbs. Time course surface fluorescence experiments revealed a short overlap (approximately 4 hours) of expression between RSP-2 and P falciparum erythrocyte membrane protein 1 (PfEMP1). Their consecutive expression enables IEs to adhere to endothelial cells during the entire blood-stage cycle. During this study, a new phenotype was detected in parasite cultures, the adhesion of normal erythrocytes (nEs) to endothelial cells. All adherent nEs were coated with RSP-2. Immunolocalization studies show that RSP-2 is a rhoptry-derived protein that is discharged onto the erythrocyte membrane during contact with merozoites. Our results identify RSP-2 as a key molecule in sequestration of young blood-stage forms and nEs to endothelial cells.

Studies of Plasmodium falciparum cytoadherence using immortalized human brain capillary endothelial cells

1996 ◽  
Vol 26 (6) ◽  
pp. 647-655 ◽  
Author(s):  
Jacques G. Prudhomme ◽  
Irwin W. Sherman ◽  
Kirkwood M. Land ◽  
Ashlee V. Moses ◽  
Stephan Stenglein ◽  
...  
Keyword(s):  
Endothelial Cells ◽  
Plasmodium Falciparum ◽  
Human Brain ◽  
Brain Capillary ◽  
Brain Capillary Endothelial Cells ◽  
Capillary Endothelial Cells

scholarly journals Whole-Body Imaging of Sequestration of Plasmodium falciparum in the Rat

2005 ◽  
Vol 73 (11) ◽  
pp. 7736-7746 ◽  
Author(s):  
Fredrik Pettersson ◽  
Anna M. Vogt ◽  
Cathrine Jonsson ◽  
Bobo W. Mok ◽  
Alireza Shamaei-Tousi ◽  
...  
Keyword(s):  
Endothelial Cells ◽  
Plasmodium Falciparum ◽  
Severe Malaria ◽  
Whole Body ◽  
Surgical Removal ◽  
Whole Body Imaging ◽  
Rat Lung ◽  
Body Imaging

ABSTRACT The occlusion of vessels by packed Plasmodium falciparum-infected (iRBC) and uninfected erythrocytes is a characteristic postmortem finding in the microvasculature of patients with severe malaria. Here we have employed immunocompetent Sprague-Dawley rats to establish sequestration in vivo. Human iRBC cultivated in vitro and purified in a single step over a magnet were labeled with 99mtechnetium, injected into the tail vein of the rat, and monitored dynamically for adhesion in the microvasculature using whole-body imaging or imaging of the lungs subsequent to surgical removal. iRBC of different lines and clones sequester avidly in vivo while uninfected erythrocytes did not. Histological examination revealed that a multiadhesive parasite adhered in the larger microvasculature, inducing extensive intravascular changes while CD36- and chondroitin sulfate A-specific parasites predominantly sequester in capillaries, inducing no or minor pathology. Removal of the adhesive ligand Plasmodium falciparum erythrocyte membrane protein 1 (PfEMP1), preincubation of the iRBC with sera to PfEMP1 or preincubation with soluble PfEMP1-receptors prior to injection significantly reduced the sequestration. The specificity of iRBC binding to the heterologous murine receptors was confirmed in vitro, using primary rat lung endothelial cells and rat lung cryosections. In offering flow dynamics, nonmanipulated endothelial cells, and an intact immune system, we believe this syngeneic animal model to be an important complement to existing in vitro systems for the screening of vaccines and adjunct therapies aiming at the prevention and treatment of severe malaria.

Down-regulation of tight junction mRNAs in human endothelial cells co-cultured with Plasmodium falciparum-infected erythrocytes

2006 ◽  
Vol 55 (2) ◽  
pp. 107-112 ◽  
Author(s):  
Pannapa Susomboon ◽  
Yaowapa Maneerat ◽  
Paron Dekumyoy ◽  
Thareerat Kalambaheti ◽  
Moritoshi Iwagami ◽  
...  
Keyword(s):  
Endothelial Cells ◽  
Plasmodium Falciparum ◽  
Tight Junction ◽  
Human Endothelial Cells ◽  
Down Regulation
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