Tumor Cell Invasion
|
0.100 |
AlteredExpression
|
phenotype |
BEFREE |
We found that all laboratory strains and the majority of field strains tested were dependent on GPB expression level for invasion.
|
28760933 |
2017 |
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 |
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 |
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 |
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 |
Most culture-adapted parasite isolates use a mechanism of invasion that depends primarily on the erythrocyte sialoglycoprotein glycophorin A (GYPA) and erythrocyte-binding antigen 175 (EBA-175) of the parasite blood-stage merozoite.
|
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 |
Biomarker
|
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 |
Tumor Cell Invasion
|
0.100 |
Biomarker
|
phenotype |
BEFREE |
Clone 7G8, which cannot invade trypsin-treated erythrocytes, may be missing the ligand for invasion via glycophorin B.(ABSTRACT TRUNCATED AT 250 WORDS)
|
8078523 |
1994 |