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Fei Wen Cheong - One of the best experts on this subject based on the ideXlab platform.
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erythrocyte binding assays reveal higher binding of plasmodium knowlesi duffy binding protein to human fy a b Erythrocytes than to fy a b Erythrocytes
Parasites & Vectors, 2018Co-Authors: Mun Yik Fong, Fei Wen CheongAbstract:Background The merozoite of the zoonotic Plasmodium knowlesi invades human Erythrocytes via the binding of its Duffy binding protein (PkDBPαII) to the Duffy antigen on the eythrocytes. The Duffy antigen has two immunologically distinct forms, Fya and Fyb. In this study, the erythrocyte-binding assay was used to quantitatively determine and compare the binding level of PkDBPαII to Fya+/b+ and Fya+/b- human Erythrocytes. Results In the erythrocyte-binding assay, binding level was determined by scoring the number of rosettes that were formed by Erythrocytes surrounding transfected mammalian COS-7 cells which expressed PkDBPαII. The assay result revealed a significant difference in the binding level. The number of rosettes scored for Fya+/b+ was 1.64-fold higher than that of Fya+/b- (155.50 ± 34.32 and 94.75 ± 23.16 rosettes, respectively; t(6) = -2.935, P = 0.026). Conclusions The erythrocyte-binding assay provided a simple approach to quantitatively determine the binding level of PkDBPαII to the erythrocyte Duffy antigen. Using this assay, PkDBPαII was found to display higher binding to Fya+/b+ Erythrocytes than to Fya+/b- Erythrocytes.
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Erythrocyte-binding assays reveal higher binding of Plasmodium knowlesi Duffy binding protein to human Fy a+/b+ Erythrocytes than to Fy a+/b- Erythrocytes
Parasites & Vectors, 2018Co-Authors: Mun Yik Fong, Fei Wen CheongAbstract:BACKGROUND: The merozoite of the zoonotic Plasmodium knowlesi invades human Erythrocytes via the binding of its Duffy binding protein (PkDBPαII) to the Duffy antigen on the eythrocytes. The Duffy antigen has two immunologically distinct forms, Fya and Fyb. In this study, the erythrocyte-binding assay was used to quantitatively determine and compare the binding level of PkDBPαII to Fya+/b+ and Fya+/b- human Erythrocytes. RESULTS: In the erythrocyte-binding assay, binding level was determined by scoring the number of rosettes that were formed by Erythrocytes surrounding transfected mammalian COS-7 cells which expressed PkDBPαII. The assay result revealed a significant difference in the binding level. The number of rosettes scored for Fya+/b+ was 1.64-fold higher than that of Fya+/b- (155.50 ± 34.32 and 94.75 ± 23.16 rosettes, respectively; t(6) = -2.935, P = 0.026). CONCLUSIONS: The erythrocyte-binding assay provided a simple approach to quantitatively determine the binding level of PkDBPαII to the erythrocyte Duffy antigen. Using this assay, PkDBPαII was found to display higher binding to Fya+/b+ Erythrocytes than to Fya+/b- Erythrocytes.
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Erythrocyte-binding Assays Reveal Higher Binding of Plasmodium Knowlesi Duffy Binding Protein to Human Fy a+/b+ Erythrocytes Than to Fy a+/b- Erythrocytes
Parasites & vectors, 2018Co-Authors: Mun Yik Fong, Fei Wen Cheong, Yee Ling LauAbstract:The merozoite of the zoonotic Plasmodium knowlesi invades human Erythrocytes via the binding of its Duffy binding protein (PkDBPαII) to the Duffy antigen on the eythrocytes. The Duffy antigen has two immunologically distinct forms, Fya and Fyb. In this study, the erythrocyte-binding assay was used to quantitatively determine and compare the binding level of PkDBPαII to Fya+/b+ and Fya+/b- human Erythrocytes. In the erythrocyte-binding assay, binding level was determined by scoring the number of rosettes that were formed by Erythrocytes surrounding transfected mammalian COS-7 cells which expressed PkDBPαII. The assay result revealed a significant difference in the binding level. The number of rosettes scored for Fya+/b+ was 1.64-fold higher than that of Fya+/b- (155.50 ± 34.32 and 94.75 ± 23.16 rosettes, respectively; t(6) = -2.935, P = 0.026). The erythrocyte-binding assay provided a simple approach to quantitatively determine the binding level of PkDBPαII to the erythrocyte Duffy antigen. Using this assay, PkDBPαII was found to display higher binding to Fya+/b+ Erythrocytes than to Fya+/b- Erythrocytes.
Mun Yik Fong - One of the best experts on this subject based on the ideXlab platform.
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erythrocyte binding assays reveal higher binding of plasmodium knowlesi duffy binding protein to human fy a b Erythrocytes than to fy a b Erythrocytes
Parasites & Vectors, 2018Co-Authors: Mun Yik Fong, Fei Wen CheongAbstract:Background The merozoite of the zoonotic Plasmodium knowlesi invades human Erythrocytes via the binding of its Duffy binding protein (PkDBPαII) to the Duffy antigen on the eythrocytes. The Duffy antigen has two immunologically distinct forms, Fya and Fyb. In this study, the erythrocyte-binding assay was used to quantitatively determine and compare the binding level of PkDBPαII to Fya+/b+ and Fya+/b- human Erythrocytes. Results In the erythrocyte-binding assay, binding level was determined by scoring the number of rosettes that were formed by Erythrocytes surrounding transfected mammalian COS-7 cells which expressed PkDBPαII. The assay result revealed a significant difference in the binding level. The number of rosettes scored for Fya+/b+ was 1.64-fold higher than that of Fya+/b- (155.50 ± 34.32 and 94.75 ± 23.16 rosettes, respectively; t(6) = -2.935, P = 0.026). Conclusions The erythrocyte-binding assay provided a simple approach to quantitatively determine the binding level of PkDBPαII to the erythrocyte Duffy antigen. Using this assay, PkDBPαII was found to display higher binding to Fya+/b+ Erythrocytes than to Fya+/b- Erythrocytes.
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Erythrocyte-binding assays reveal higher binding of Plasmodium knowlesi Duffy binding protein to human Fy a+/b+ Erythrocytes than to Fy a+/b- Erythrocytes
Parasites & Vectors, 2018Co-Authors: Mun Yik Fong, Fei Wen CheongAbstract:BACKGROUND: The merozoite of the zoonotic Plasmodium knowlesi invades human Erythrocytes via the binding of its Duffy binding protein (PkDBPαII) to the Duffy antigen on the eythrocytes. The Duffy antigen has two immunologically distinct forms, Fya and Fyb. In this study, the erythrocyte-binding assay was used to quantitatively determine and compare the binding level of PkDBPαII to Fya+/b+ and Fya+/b- human Erythrocytes. RESULTS: In the erythrocyte-binding assay, binding level was determined by scoring the number of rosettes that were formed by Erythrocytes surrounding transfected mammalian COS-7 cells which expressed PkDBPαII. The assay result revealed a significant difference in the binding level. The number of rosettes scored for Fya+/b+ was 1.64-fold higher than that of Fya+/b- (155.50 ± 34.32 and 94.75 ± 23.16 rosettes, respectively; t(6) = -2.935, P = 0.026). CONCLUSIONS: The erythrocyte-binding assay provided a simple approach to quantitatively determine the binding level of PkDBPαII to the erythrocyte Duffy antigen. Using this assay, PkDBPαII was found to display higher binding to Fya+/b+ Erythrocytes than to Fya+/b- Erythrocytes.
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Erythrocyte-binding Assays Reveal Higher Binding of Plasmodium Knowlesi Duffy Binding Protein to Human Fy a+/b+ Erythrocytes Than to Fy a+/b- Erythrocytes
Parasites & vectors, 2018Co-Authors: Mun Yik Fong, Fei Wen Cheong, Yee Ling LauAbstract:The merozoite of the zoonotic Plasmodium knowlesi invades human Erythrocytes via the binding of its Duffy binding protein (PkDBPαII) to the Duffy antigen on the eythrocytes. The Duffy antigen has two immunologically distinct forms, Fya and Fyb. In this study, the erythrocyte-binding assay was used to quantitatively determine and compare the binding level of PkDBPαII to Fya+/b+ and Fya+/b- human Erythrocytes. In the erythrocyte-binding assay, binding level was determined by scoring the number of rosettes that were formed by Erythrocytes surrounding transfected mammalian COS-7 cells which expressed PkDBPαII. The assay result revealed a significant difference in the binding level. The number of rosettes scored for Fya+/b+ was 1.64-fold higher than that of Fya+/b- (155.50 ± 34.32 and 94.75 ± 23.16 rosettes, respectively; t(6) = -2.935, P = 0.026). The erythrocyte-binding assay provided a simple approach to quantitatively determine the binding level of PkDBPαII to the erythrocyte Duffy antigen. Using this assay, PkDBPαII was found to display higher binding to Fya+/b+ Erythrocytes than to Fya+/b- Erythrocytes.
Mikko Nikinmaa - One of the best experts on this subject based on the ideXlab platform.
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influence of band 3 protein absence and skeletal structures on amphiphile and ca2 induced shape alterations in Erythrocytes a study with lamprey lampetra fluviatilis trout onchorhynchus mykiss and human Erythrocytes
Biochimica et Biophysica Acta, 2000Co-Authors: Henry Hagerstrand, Malgorzata Danieluk, Malgorzata Bobrowskahagerstrand, Ales Iglic, Anna Wrobel, Boris Isomaa, Mikko NikinmaaAbstract:Amphiphiles which induce either spiculated (echinocytic) or invaginated (stomatocytic) shapes in human Erythrocytes, and ionophore A23187 plus Ca 2a , were studied for their capacity to induce shape alterations, vesiculation and hemolysis in the morphologically and structurally different lamprey and trout Erythrocytes. Both qualitative and quantitative differences were found. Amphiphiles induced no gross morphological changes in the non-axisymmetric stomatocyte-like lamprey erythrocyte or in the flat ellipsoidal trout erythrocyte, besides a rounding up at higher amphiphile concentrations. No shapes with large broad spicula were seen. Nevertheless, some of the ‘echinocytogenic’ amphiphiles induced plasma membrane protrusions in lamprey and trout Erythrocytes, from where exovesicles were shed. In trout Erythrocytes, occurrence of corrugations at the cell rim preceded protrusion formation. Other ‘echinocytogenic’ amphiphiles induced invaginations in lamprey Erythrocytes. The ‘stomatocytogenic’ amphiphiles induced invaginations in both lamprey and trout Erythrocytes. Surprisingly, in trout Erythrocytes, some protrusions also occurred. Some of the amphiphiles hemolyzed lamprey, trout and human Erythrocytes at a significantly different concentration/membrane area. Ionophore A23187 plus Ca 2a induced membrane protrusions and sphering in human and trout Erythrocytes ; however, the lamprey erythrocyte remained unperturbed. The shape alterations in lamprey Erythrocytes, we suggest, are characterized by weak membrane skeleton^lipid bilayer interactions, due to band 3 protein and ankyrin deficiency. In trout erythrocyte, the marginal band of microtubules appears to strongly influence cell shape. Furthermore, the presence of intermediate filaments and nuclei, additionally affecting the cell membrane shear elasticity, apparently influences cell shape changes in lamprey and trout Erythrocytes. The different types of shape alterations induced by certain amphiphiles in the cell types indicates that their plasma membrane phospholipid composition differs. fl 2000 Elsevier Science B.V. All rights reserved.
Yee Ling Lau - One of the best experts on this subject based on the ideXlab platform.
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Erythrocyte-binding Assays Reveal Higher Binding of Plasmodium Knowlesi Duffy Binding Protein to Human Fy a+/b+ Erythrocytes Than to Fy a+/b- Erythrocytes
Parasites & vectors, 2018Co-Authors: Mun Yik Fong, Fei Wen Cheong, Yee Ling LauAbstract:The merozoite of the zoonotic Plasmodium knowlesi invades human Erythrocytes via the binding of its Duffy binding protein (PkDBPαII) to the Duffy antigen on the eythrocytes. The Duffy antigen has two immunologically distinct forms, Fya and Fyb. In this study, the erythrocyte-binding assay was used to quantitatively determine and compare the binding level of PkDBPαII to Fya+/b+ and Fya+/b- human Erythrocytes. In the erythrocyte-binding assay, binding level was determined by scoring the number of rosettes that were formed by Erythrocytes surrounding transfected mammalian COS-7 cells which expressed PkDBPαII. The assay result revealed a significant difference in the binding level. The number of rosettes scored for Fya+/b+ was 1.64-fold higher than that of Fya+/b- (155.50 ± 34.32 and 94.75 ± 23.16 rosettes, respectively; t(6) = -2.935, P = 0.026). The erythrocyte-binding assay provided a simple approach to quantitatively determine the binding level of PkDBPαII to the erythrocyte Duffy antigen. Using this assay, PkDBPαII was found to display higher binding to Fya+/b+ Erythrocytes than to Fya+/b- Erythrocytes.
Henry Hagerstrand - One of the best experts on this subject based on the ideXlab platform.
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influence of band 3 protein absence and skeletal structures on amphiphile and ca2 induced shape alterations in Erythrocytes a study with lamprey lampetra fluviatilis trout onchorhynchus mykiss and human Erythrocytes
Biochimica et Biophysica Acta, 2000Co-Authors: Henry Hagerstrand, Malgorzata Danieluk, Malgorzata Bobrowskahagerstrand, Ales Iglic, Anna Wrobel, Boris Isomaa, Mikko NikinmaaAbstract:Amphiphiles which induce either spiculated (echinocytic) or invaginated (stomatocytic) shapes in human Erythrocytes, and ionophore A23187 plus Ca 2a , were studied for their capacity to induce shape alterations, vesiculation and hemolysis in the morphologically and structurally different lamprey and trout Erythrocytes. Both qualitative and quantitative differences were found. Amphiphiles induced no gross morphological changes in the non-axisymmetric stomatocyte-like lamprey erythrocyte or in the flat ellipsoidal trout erythrocyte, besides a rounding up at higher amphiphile concentrations. No shapes with large broad spicula were seen. Nevertheless, some of the ‘echinocytogenic’ amphiphiles induced plasma membrane protrusions in lamprey and trout Erythrocytes, from where exovesicles were shed. In trout Erythrocytes, occurrence of corrugations at the cell rim preceded protrusion formation. Other ‘echinocytogenic’ amphiphiles induced invaginations in lamprey Erythrocytes. The ‘stomatocytogenic’ amphiphiles induced invaginations in both lamprey and trout Erythrocytes. Surprisingly, in trout Erythrocytes, some protrusions also occurred. Some of the amphiphiles hemolyzed lamprey, trout and human Erythrocytes at a significantly different concentration/membrane area. Ionophore A23187 plus Ca 2a induced membrane protrusions and sphering in human and trout Erythrocytes ; however, the lamprey erythrocyte remained unperturbed. The shape alterations in lamprey Erythrocytes, we suggest, are characterized by weak membrane skeleton^lipid bilayer interactions, due to band 3 protein and ankyrin deficiency. In trout erythrocyte, the marginal band of microtubules appears to strongly influence cell shape. Furthermore, the presence of intermediate filaments and nuclei, additionally affecting the cell membrane shear elasticity, apparently influences cell shape changes in lamprey and trout Erythrocytes. The different types of shape alterations induced by certain amphiphiles in the cell types indicates that their plasma membrane phospholipid composition differs. fl 2000 Elsevier Science B.V. All rights reserved.
