Studies on Immunogenicity and Antigenicity of Baculovirus-Expressed Binding Region of Plasmodium falciparum EBA-140 Merozoite Ligand

Zerka, Agata; Rydzak, Joanna; Lass, Anna; Szostakowska, Beata; Nahorski, W; Wroczyńska, Agnieszka; Myjak, P; Krotkiewski, Hubert; Jaśkiewicz, Ewa

doi:10.1007/s00005-015-0367-5

Cited by 7 publications

(5 citation statements)

References 52 publications

(74 reference statements)

Supporting

Mentioning

Contrasting

Order By: Relevance

“…16 The reorientation stage is thought to be mediated by merozoite ligands released from apical organelles to erythrocytes, including 2 ligand families, P falciparum reticulocyte-binding protein homologs (PfRhs) and erythrocyte-binding-like proteins. [17][18][19][20] Among those, 4 receptor-ligand pairs, glycophorin A-EBA175, 21 glycophorin C-EBA140, [22][23][24] complement receptor 1 (CR1)-PfRh4, 25 and CD147-PfRh5 11,26,27 are involved at this stage, of which the CD147-PfRh5 interaction is the only one that is essential for the parasite invasion. The TJ formation and motility involve 2 parasitesecreted proteins, P. falciparum apical membrane antigen (PfAMA1) and rhoptry neck protein 2 (RON2), to form an AMA1-RON2 complex.…”

Section: Introductionmentioning

confidence: 99%

Disrupting CD147-RAP2 interaction abrogates erythrocyte invasion by Plasmodium falciparum

Zhang

et al. 2018

Blood

View full text Add to dashboard Cite

show abstract

Section: Introductionmentioning

confidence: 99%

Disrupting CD147-RAP2 interaction abrogates erythrocyte invasion by Plasmodium falciparum

Zhang

et al. 2018

Blood

View full text Add to dashboard Cite

show abstract

“…The heat-denatured Region II was used as the negative binding control. The cells were washed three times with PBS and incubated for 1 h at 4 °C with rabbit serum (diluted 1:200) raised against the whole P. falciparum EBA-140 Region II [ 45 ]. The cells were washed three times with PBS and incubated for 45 min at 4 °C with FITC-conjugated swine anti-rabbit Ig antibody (DakoCytomation, Glostrup, Denmark) and analyzed for fluorescence intensity using flow cytometry (FACSCalibur, BD Biosciences, San Jose, USA).…”

Section: Methodsmentioning

confidence: 99%

Plasmodium reichenowi EBA-140 merozoite ligand binds to glycophorin D on chimpanzee red blood cells, shedding new light on origins of Plasmodium falciparum

et al. 2017

Self Cite

View full text Add to dashboard Cite

BackgroundAll symptoms of malaria are caused by the intraerythrocytic proliferation of Plasmodium merozoites. Merozoites invade erythrocytes using multiple binding ligands that recognise specific surface receptors. It has been suggested that adaptation of Plasmodium parasites to infect specific hosts is driven by changes in genes encoding Plasmodium erythrocyte-binding ligands (EBL) and reticulocyte-binding ligands (RBL). Homologs of both EBL and RBL, including the EBA-140 merozoite ligand, have been identified in P. falciparum and P. reichenowi, which infect humans and chimpanzees, respectively. The P. falciparum EBA-140 was shown to bind human glycophorin C, a minor erythrocyte sialoglycoprotein. Until now, the erythrocyte receptor for the P. reichenowi EBA-140 remained unknown.MethodsThe baculovirus expression vector system was used to obtain the recombinant EBA-140 Region II, and flow cytometry and immunoblotting methods were applied to characterise its specificity.ResultsWe showed that the chimpanzee glycophorin D is the receptor for the P. reichenowi EBA-140 ligand on chimpanzee red blood cells.ConclusionsWe propose that the development of glycophorin C specificity is spurred by the P. falciparum lineage. We speculate that the P. falciparum EBA-140 evolved to hijack GPC on human erythrocytes during divergence from its ape ancestor.

show abstract

“…As discussed above, there is a general agreement that GPC but not GPD is P. falciparum EBA-140 receptor on human RBCs [79, 81–83, 97, 98]. However, evaluation of the binding of the homologous P. reichenowi EBA-140 ligand binding to chimpanzee RBCs [99] unexpectedly demonstrated that the chimpanzee homolog of human GPD is probably the receptor for that ligand [4, 100].…”

Section: Introductionmentioning

confidence: 99%

Erythrocyte glycophorins as receptors for Plasmodium merozoites

et al. 2019

Self Cite

View full text Add to dashboard Cite

Glycophorins are heavily glycosylated sialoglycoproteins of human and animal erythrocytes. In humans, there are four glycophorins: A, B, C and D. Glycophorins play an important role in the invasion of red blood cells (RBCs) by malaria parasites, which involves several ligands binding to RBC receptors. Four Plasmodium falciparum merozoite EBL ligands have been identified: erythrocyte-binding antigen-175 (EBA-175), erythrocyte-binding antigen-181 (EBA-181), erythrocyte-binding ligand-1 (EBL-1) and erythrocyte-binding antigen-140 (EBA-140). It is generally accepted that glycophorin A (GPA) is the receptor for P. falciparum EBA-175 ligand. It has been shown that α(2,3) sialic acid residues of GPA O-glycans form conformation-dependent clusters on GPA polypeptide chain which facilitate binding. P. falciparum can also invade erythrocytes using glycophorin B (GPB), which is structurally similar to GPA. It has been shown that P. falciparum EBL-1 ligand binds to GPB. Interestingly, a hybrid GPB-GPA molecule called Dantu is associated with a reduced risk of severe malaria and ameliorates malaria-related morbidity. Glycophorin C (GPC) is a receptor for P. falciparum EBA-140 ligand. Likewise, successful binding of EBA-140 depends on sialic acid residues of N- and O-linked oligosaccharides of GPC, which form a cluster or a conformational structure depending on the presence of peptide fragment encompassing amino acids (aa) 36–63. Evaluation of the homologous P. reichenowi EBA-140 unexpectedly revealed that the chimpanzee homolog of human glycophorin D (GPD) is probably the receptor for this ligand. In this review, we concentrate on the role of glycophorins as erythrocyte receptors for Plasmodium parasites. The presented data support the long-lasting idea of high evolutionary pressure exerted by Plasmodium on the human glycophorins, which emerge as important receptors for these parasites.

show abstract

Studies on Immunogenicity and Antigenicity of Baculovirus-Expressed Binding Region of Plasmodium falciparum EBA-140 Merozoite Ligand

Cited by 7 publications

References 52 publications

Disrupting CD147-RAP2 interaction abrogates erythrocyte invasion by Plasmodium falciparum

Disrupting CD147-RAP2 interaction abrogates erythrocyte invasion by Plasmodium falciparum

Plasmodium reichenowi EBA-140 merozoite ligand binds to glycophorin D on chimpanzee red blood cells, shedding new light on origins of Plasmodium falciparum

Erythrocyte glycophorins as receptors for Plasmodium merozoites

Contact Info

Product

Resources

About