Characterization of Plasmodium falciparum-Infected Erythrocyte and P-Selectin Interaction Under Flow Conditions

Blood ◽  
1998 ◽  
Vol 91 (12) ◽  
pp. 4803-4809 ◽  
Author(s):  
May Ho ◽  
Tineke Schollaardt ◽  
Xiaofei Niu ◽  
Sornchai Looareesuwan ◽  
Kamala D. Patel ◽  
...  
Keyword(s):  
Plasmodium Falciparum ◽  
Adhesion Molecule ◽  
Sialic Acid Residue ◽  
Intercellular Adhesion Molecule ◽  
Flow Conditions ◽  
Intercellular Adhesion Molecule 1 ◽  
Adhesive Interaction ◽  
Lectin Domain

Plasmodium falciparum-infected erythrocytes (IRBC) roll on the adhesion molecule P-selectin in vitro under flow conditions that approximate the shear stress in capillary and postcapillary venules in which cytoadherence occurs in vivo. The pathological significance of this adhesive interaction is currently unknown. In this study, we further investigated the molecular interactions between IRBC and P-selectin by using a laminar flow system that allowed for the direct visualization of IRBC-substratum interactions. The results showed that the IRBC–P-selectin interaction was Ca2+-dependent and involved the lectin domain of P-selectin and a sialic acid residue on IRBC. The sialylated P-selectin ligand was trypsin-sensitive, which suggests that it could be part of the parasite antigen PfEMP1 that interacts with CD36 and intercellular adhesion molecule-1 (ICAM-1), but different from a trypsin-resistant IRBC ligand that adheres selectively to chondroitin sulfate A. Studies on the rolling and adhesion of IRBC on activated platelets that express both CD36 and P-selectin showed that inhibition of rolling on P-selectin reduced the adhesion of some clinical parasite isolates to CD36, whereas other parasite isolates appeared to interact directly with CD36. Thus, cytoadherence under physiological flow conditions may be mediated by multiple IRBC ligands that interact with different adhesion molecules in a cooperative fashion. These findings underscore the complexity of the interactions betweeen IRBC and vascular endothelium.

Characterization of Plasmodium falciparum-Infected Erythrocyte and P-Selectin Interaction Under Flow Conditions

Blood ◽  
1998 ◽  
Vol 91 (12) ◽  
pp. 4803-4809 ◽  
Author(s):  
May Ho ◽  
Tineke Schollaardt ◽  
Xiaofei Niu ◽  
Sornchai Looareesuwan ◽  
Kamala D. Patel ◽  
...  
Keyword(s):  
Plasmodium Falciparum ◽  
Adhesion Molecule ◽  
Sialic Acid Residue ◽  
Intercellular Adhesion Molecule ◽  
Flow Conditions ◽  
Intercellular Adhesion Molecule 1 ◽  
Adhesive Interaction ◽  
Lectin Domain

Abstract Plasmodium falciparum-infected erythrocytes (IRBC) roll on the adhesion molecule P-selectin in vitro under flow conditions that approximate the shear stress in capillary and postcapillary venules in which cytoadherence occurs in vivo. The pathological significance of this adhesive interaction is currently unknown. In this study, we further investigated the molecular interactions between IRBC and P-selectin by using a laminar flow system that allowed for the direct visualization of IRBC-substratum interactions. The results showed that the IRBC–P-selectin interaction was Ca2+-dependent and involved the lectin domain of P-selectin and a sialic acid residue on IRBC. The sialylated P-selectin ligand was trypsin-sensitive, which suggests that it could be part of the parasite antigen PfEMP1 that interacts with CD36 and intercellular adhesion molecule-1 (ICAM-1), but different from a trypsin-resistant IRBC ligand that adheres selectively to chondroitin sulfate A. Studies on the rolling and adhesion of IRBC on activated platelets that express both CD36 and P-selectin showed that inhibition of rolling on P-selectin reduced the adhesion of some clinical parasite isolates to CD36, whereas other parasite isolates appeared to interact directly with CD36. Thus, cytoadherence under physiological flow conditions may be mediated by multiple IRBC ligands that interact with different adhesion molecules in a cooperative fashion. These findings underscore the complexity of the interactions betweeen IRBC and vascular endothelium.

scholarly journals Visualization of Plasmodium falciparum–Endothelium Interactions in Human Microvasculature

2000 ◽  
Vol 192 (8) ◽  
pp. 1205-1212 ◽  
Author(s):  
May Ho ◽  
Michael J. Hickey ◽  
Allan G. Murray ◽  
Graciela Andonegui ◽  
Paul Kubes
Keyword(s):  
Plasmodium Falciparum ◽  
Adhesion Molecule ◽  
Cell Adhesion Molecule ◽  
Conclusive Evidence ◽  
Intercellular Adhesion Molecule ◽  
Adherent Cells ◽  
Vascular Cell Adhesion ◽  
Rapid Reduction

Plasmodium falciparum–infected erythrocytes roll on and/or adhere to CD36, intercellular adhesion molecule (ICAM)-1, vascular cell adhesion molecule (VCAM)-1, and P-selectin under shear conditions in vitro. However, the lack of an adequate animal model has made it difficult to determine whether infected erythrocytes do indeed interact in vivo in microvessels. Therefore, we made use of an established model of human skin grafted onto severe combined immunodeficient (SCID) mice to directly visualize the human microvasculature by epifluorescence intravital microscopy. In all grafts examined, infected erythrocytes were observed to roll and/or adhere in not just postcapillary venules but also in arterioles. In contrast, occlusion of capillaries by infected erythrocytes was noted only in approximately half of the experiments. Administration of an anti-CD36 antibody resulted in a rapid reduction of rolling and adhesion. More importantly, already adherent cells quickly detached. The residual rolling after anti-CD36 treatment was largely inhibited by an anti–ICAM-1 antibody. Anti–ICAM-1 alone reduced the ability of infected erythrocytes to sustain rolling and subsequent adhesion. These findings provide conclusive evidence that infected erythrocytes interact within the human microvasculature in vivo by a multistep adhesive cascade that mimics the process of leukocyte recruitment.

scholarly journals Knob-independent cytoadherence of Plasmodium falciparum to the leukocyte differentiation antigen CD36.

1990 ◽  
Vol 171 (6) ◽  
pp. 1883-1892 ◽  
Author(s):  
B A Biggs ◽  
L Goozé ◽  
K Wycherley ◽  
D Wilkinson ◽  
A W Boyd ◽  
...  
Keyword(s):  
Plasmodium Falciparum ◽  
Peripheral Circulation ◽  
Melanoma Cells ◽  
Intercellular Adhesion Molecule ◽  
Intercellular Adhesion Molecule 1 ◽  
Differentiation Antigen ◽  
Erythrocyte Surface ◽  
Falciparum Erythrocyte Membrane Protein

The survival of Plasmodium falciparum-infected erythrocytes is enhanced by the sequestration of mature trophozoites and schizonts from the peripheral circulation. Cytoadherence of infected erythrocytes in vivo is associated with the presence of knobs on the erythrocyte surface, but we and others have shown recently that cytoadherence to C32 melanoma cells may occur in vitro in the absence of knobs. We show here that a knobless clone of P. falciparum adheres to the leukocyte differentiation antigen, CD36, suggesting that binding to CD36 is independent of the presence of knobs on the surface of the infected erythrocyte. This clone showed little cytoadherence to immobilized thrombospondin or to endothelial cells expressing the intercellular adhesion molecule 1. Furthermore, an Mr approximately 300-kD trypsin-sensitive protein doublet was immunoprecipitated from knobless trophozoite-infected erythrocytes. Finding a P. falciparum erythrocyte membrane protein 1 (PfEMP1)-like molecule on these infected erythrocytes is consistent with a role for PfEMP1 in cytoadherence to CD36 and C32 melanoma cells.

scholarly journals Fibrinogen Binding to Intercellular Adhesion Molecule 1: Implications for Plasmodium falciparum Adhesion

2002 ◽  
Vol 70 (7) ◽  
pp. 3962-3964 ◽  
Author(s):  
Carolyn Gray ◽  
Alister Craig
Keyword(s):  
Plasmodium Falciparum ◽  
Adhesion Molecule ◽  
Binding Sites ◽  
Cell Adhesion Molecule ◽  
Intercellular Adhesion ◽  
Intercellular Adhesion Molecule ◽  
Flow Conditions ◽  
Intercellular Adhesion Molecule 1 ◽  
Fibrinogen Binding ◽  
Endothelial Cell Adhesion

ABSTRACT Intercellular adhesion molecule 1 (ICAM-1) is an endothelial cell adhesion molecule implicated in cerebral malaria. We investigated whether fibrinogen affects Plasmodium falciparum binding to ICAM-1, as the ICAM-1 binding sites of P. falciparum and fibrinogen overlap. We show that fibrinogen dramatically reduces P. falciparum adhesion to ICAM-1 under flow conditions.

Intercellular adhesion molecule-1-deficient mice have antibody responses but impaired leukocyte recruitment

1997 ◽  
Vol 273 (3) ◽  
pp. L513-L523 ◽  
Author(s):  
C. A. Hatfield ◽  
J. R. Brashler ◽  
G. E. Winterrowd ◽  
F. P. Bell ◽  
R. L. Griffin ◽  
...  
Keyword(s):  
Lung Tissue ◽  
Adhesion Molecule ◽  
Lavage Fluid ◽  
Intercellular Adhesion ◽  
Antibody Responses ◽  
Intercellular Adhesion Molecule ◽  
Enzyme Linked Immunosorbent Assay ◽  
Intercellular Adhesion Molecule 1

The role of intercellular adhesion molecule-1 (ICAM-1) in murine lung inflammation was examined in vivo. Ovalbumin (Ova)-sensitized and -challenged ICAM-1-deficient (KO) mice had decreased accumulation of leukocytes in the bronchoalveolar lavage fluid compared with wild-type (WT) mice. Lung tissue inflammation was also attenuated. Ova immunization and challenge produced equivalent plasma levels of Ova-specific immunoglobulin (Ig) G1 and higher concentrations of IgE in KO versus WT mice. Ova-dependent induction of cytokines in vitro, as measured by enzyme-linked immunosorbent assay, was impaired in splenocytes from KO mice compared with the comparable release of interleukin (IL)-5 and IL-10 from anti-CD3-stimulated WT and KO splenocytes. Methacholine-induced increases in trapped gas in lungs of Ova-sensitized and -challenged WT mice were greater than those of KO mice. The activation of lung tissue nuclear factor-kappa B was diminished in KO mice after Ova provocation. This suggests that ICAM-1 was important for activation of the inflammatory cascade leading to the recruitment of leukocytes but was not critical for the generation of antibody responses in vivo.

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