Tumor Cell Invasion
|
0.100 |
Biomarker
|
phenotype |
BEFREE |
Erythrocyte Binding Antigen of 175 kDa (EBA-175) has a well-defined role in binding to glycophorin A (GpA) during <i>Plasmodium falciparum</i> invasion of erythrocytes.
|
30556808 |
2018 |
Tumor Cell Invasion
|
0.100 |
Biomarker
|
phenotype |
BEFREE |
Erythrocyte binding antigens 175 (EBA-175) and 140 (EBA-140) play key roles in erythrocyte invasion by binding to glycophorin A (GPA) and C (GPC) respectively in human malaria.
|
29128519 |
2018 |
Tumor Cell Invasion
|
0.100 |
Biomarker
|
phenotype |
BEFREE |
Most interesting was the inhibition of genes of the glycophorins A and B (GYPA/B) family, which are the major sialoglycoproteins of the human erythrocyte membrane and receptor of several viruses for host invasion.
|
27491455 |
2016 |
Tumor Cell Invasion
|
0.100 |
Biomarker
|
phenotype |
BEFREE |
These findings suggest an essential role of the MSP1-GPA-band 3 complex during the initial adhesion phase of malaria parasite invasion of RBCs.
|
25778531 |
2015 |
Tumor Cell Invasion
|
0.100 |
Biomarker
|
phenotype |
BEFREE |
The molecular mechanism(s) responsible for these host restrictions are not understood, although the interaction between the parasite blood-stage invasion ligand EBA175 and the host erythrocyte receptor Glycophorin-A (GYPA) has been implicated previously.
|
24297912 |
2013 |
Tumor Cell Invasion
|
0.100 |
Biomarker
|
phenotype |
BEFREE |
By comparison, the RII fragment alone bound GYPA with a lower affinity demonstrating that regions outside of the DBL domains are important for interactions with GYPA; antibodies directed to these other regions also contributed to the inhibition of parasite invasion.
|
24043627 |
2013 |
Tumor Cell Invasion
|
0.100 |
Biomarker
|
phenotype |
BEFREE |
The Erythrocyte Binding Antigen (EBA) 175 has been considered as one of the most important Plasmodium falciparum (P. falciparum) merozoite ligands that mediate invasion of the erythrocytes through their sialated receptor: Glycophorin A (GPA).
|
24103447 |
2013 |
Tumor Cell Invasion
|
0.100 |
Biomarker
|
phenotype |
BEFREE |
EBA-175 mediates sialic acid-dependent binding to glycophorin A on the erythrocytes playing a crucial role during invasion of the P. falciparum in the host cell.
|
21615944 |
2011 |
Tumor Cell Invasion
|
0.100 |
Biomarker
|
phenotype |
BEFREE |
Brazilian field isolates were shown to mostly utilize glycophorin A-independent invasion pathways via glycophorin B (GPB) and/or other receptors.
|
21283638 |
2011 |
Tumor Cell Invasion
|
0.100 |
Biomarker
|
phenotype |
BEFREE |
We genetically demonstrate, in an isogenic background, that glycophorin A is required for efficient strain-specific parasite invasion.
|
20958212 |
2010 |
Tumor Cell Invasion
|
0.100 |
Biomarker
|
phenotype |
BEFREE |
The neuraminidase-sensitive, trypsin-sensitive phenotype consistent with invasion mediated by the binding of parasite ligand erythrocyte binding antigen 175 to glycophorin A, the most common invasion profile in a previous study of Gambian field isolates, was seen in only 3 of 31 Kenyan isolates.
|
17438038 |
2007 |
Tumor Cell Invasion
|
0.100 |
Biomarker
|
phenotype |
BEFREE |
These results support the hypothesis that African P. falciparum parasites use GYPA as a primary receptor for invasion.
|
12654801 |
2003 |
Tumor Cell Invasion
|
0.100 |
Biomarker
|
phenotype |
BEFREE |
A 175 kDa Plasmodium falciparum erythrocyte binding antigen (EBA-175) binds sialic acid residues on glycophorin A during invasion of human erythrocytes.
|
12165386 |
2002 |
Tumor Cell Invasion
|
0.100 |
GeneticVariation
|
phenotype |
BEFREE |
The protease-resistant properties of the erythrocyte receptor suggests that it is not glycophorin A or C. Additionally, analysis of mutant erythrocytes from humans has shown that EBA140 does not bind glycophorin B. Interestingly, we have identified a parasite line that lacks the eba140 gene, suggesting that this protein is not essential for in vitro invasion.
|
11454199 |
2001 |
Tumor Cell Invasion
|
0.100 |
Biomarker
|
phenotype |
BEFREE |
EBA-175 is a Plasmodium falciparum micronemal protein that binds to sialic acid in the context of the peptide backbone of glycophorin A and has been implicated in sialic acid-dependent invasion of erythrocytes.
|
10989151 |
2000 |
Tumor Cell Invasion
|
0.100 |
Biomarker
|
phenotype |
BEFREE |
In contrast, erythrocyte invasion via the EBA-175/glycophorin A route appears to have been disrupted to such a degree that the mutant lines have undergone a stable switch in invasion phenotype.
|
10861015 |
2000 |