N-linked glycoproteins are related to schizogony of the intraerythrocytic stage in Plasmodium falciparum
Although the existence of O-linked oligosaccharide residues in glycoproteins of Plasmodium falciparum has been shown, the existence of N- linked glycoproteins is still a matter of controversy and skepticism. This report demonstrates the unequivocal presence of N-linked glycoproteins in P. falciparum...
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todo:paper_00219258_v271_n24_p14452_Kimura2023-10-03T14:22:57Z N-linked glycoproteins are related to schizogony of the intraerythrocytic stage in Plasmodium falciparum Kimura, E.A. Couto, A.S. Peres, V.J. Casal, O.L. Katzin, A.M. asparagine linked oligosaccharide concanavalin a glucan synthase glycoprotein sepharose tunicamycin article controlled study erythrocyte life cycle nonhuman plasmodium falciparum priority journal protein glycosylation protein synthesis schizont trophozoite Amidohydrolases Animals Carbon Radioisotopes Chromatography, Affinity Chromatography, Gel Chromatography, Paper Chromatography, Thin Layer Cycloheximide Electrophoresis, Polyacrylamide Gel Erythrocytes Glucose Glycoproteins Humans Kinetics Malaria, Falciparum Mannose Methionine Molecular Weight Oligosaccharides Parasitemia Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase Plasmodium falciparum Protozoan Proteins Sulfur Radioisotopes Tunicamycin Although the existence of O-linked oligosaccharide residues in glycoproteins of Plasmodium falciparum has been shown, the existence of N- linked glycoproteins is still a matter of controversy and skepticism. This report demonstrates the unequivocal presence of N-linked glycoproteins in P. falciparum, principally in the ring and young trophozoite stages of the intraerythrocytic cycle. These glycoproteins lose their capacity to bind to concanavalin A-Sepharose after treatment of cultures with tunicamycin under conditions that do not affect protein synthesis. When the glycoproteins were treated with N-Glycanase®, oligosaccharides were released. It was possible to identify an N-linked glycoprotein of >200 kDa in the ring stage and also N-linked glycoproteins in the range of 200-30 kDa in the trophozoite stage. Treatment of trophozoites with 12 μM tunicamycin inhibited differentiation to the schizont stage. To our knowledge, this is the first report in the literature unequivocally showing N-linked glycoproteins in trophozoites of P. falciparum as well as their importance for the differentiation of the intraerythrocytic stages of this parasite. Fil:Couto, A.S. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Casal, O.L. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar http://hdl.handle.net/20.500.12110/paper_00219258_v271_n24_p14452_Kimura |
institution |
Universidad de Buenos Aires |
institution_str |
I-28 |
repository_str |
R-134 |
collection |
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
topic |
asparagine linked oligosaccharide concanavalin a glucan synthase glycoprotein sepharose tunicamycin article controlled study erythrocyte life cycle nonhuman plasmodium falciparum priority journal protein glycosylation protein synthesis schizont trophozoite Amidohydrolases Animals Carbon Radioisotopes Chromatography, Affinity Chromatography, Gel Chromatography, Paper Chromatography, Thin Layer Cycloheximide Electrophoresis, Polyacrylamide Gel Erythrocytes Glucose Glycoproteins Humans Kinetics Malaria, Falciparum Mannose Methionine Molecular Weight Oligosaccharides Parasitemia Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase Plasmodium falciparum Protozoan Proteins Sulfur Radioisotopes Tunicamycin |
spellingShingle |
asparagine linked oligosaccharide concanavalin a glucan synthase glycoprotein sepharose tunicamycin article controlled study erythrocyte life cycle nonhuman plasmodium falciparum priority journal protein glycosylation protein synthesis schizont trophozoite Amidohydrolases Animals Carbon Radioisotopes Chromatography, Affinity Chromatography, Gel Chromatography, Paper Chromatography, Thin Layer Cycloheximide Electrophoresis, Polyacrylamide Gel Erythrocytes Glucose Glycoproteins Humans Kinetics Malaria, Falciparum Mannose Methionine Molecular Weight Oligosaccharides Parasitemia Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase Plasmodium falciparum Protozoan Proteins Sulfur Radioisotopes Tunicamycin Kimura, E.A. Couto, A.S. Peres, V.J. Casal, O.L. Katzin, A.M. N-linked glycoproteins are related to schizogony of the intraerythrocytic stage in Plasmodium falciparum |
topic_facet |
asparagine linked oligosaccharide concanavalin a glucan synthase glycoprotein sepharose tunicamycin article controlled study erythrocyte life cycle nonhuman plasmodium falciparum priority journal protein glycosylation protein synthesis schizont trophozoite Amidohydrolases Animals Carbon Radioisotopes Chromatography, Affinity Chromatography, Gel Chromatography, Paper Chromatography, Thin Layer Cycloheximide Electrophoresis, Polyacrylamide Gel Erythrocytes Glucose Glycoproteins Humans Kinetics Malaria, Falciparum Mannose Methionine Molecular Weight Oligosaccharides Parasitemia Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase Plasmodium falciparum Protozoan Proteins Sulfur Radioisotopes Tunicamycin |
description |
Although the existence of O-linked oligosaccharide residues in glycoproteins of Plasmodium falciparum has been shown, the existence of N- linked glycoproteins is still a matter of controversy and skepticism. This report demonstrates the unequivocal presence of N-linked glycoproteins in P. falciparum, principally in the ring and young trophozoite stages of the intraerythrocytic cycle. These glycoproteins lose their capacity to bind to concanavalin A-Sepharose after treatment of cultures with tunicamycin under conditions that do not affect protein synthesis. When the glycoproteins were treated with N-Glycanase®, oligosaccharides were released. It was possible to identify an N-linked glycoprotein of >200 kDa in the ring stage and also N-linked glycoproteins in the range of 200-30 kDa in the trophozoite stage. Treatment of trophozoites with 12 μM tunicamycin inhibited differentiation to the schizont stage. To our knowledge, this is the first report in the literature unequivocally showing N-linked glycoproteins in trophozoites of P. falciparum as well as their importance for the differentiation of the intraerythrocytic stages of this parasite. |
format |
JOUR |
author |
Kimura, E.A. Couto, A.S. Peres, V.J. Casal, O.L. Katzin, A.M. |
author_facet |
Kimura, E.A. Couto, A.S. Peres, V.J. Casal, O.L. Katzin, A.M. |
author_sort |
Kimura, E.A. |
title |
N-linked glycoproteins are related to schizogony of the intraerythrocytic stage in Plasmodium falciparum |
title_short |
N-linked glycoproteins are related to schizogony of the intraerythrocytic stage in Plasmodium falciparum |
title_full |
N-linked glycoproteins are related to schizogony of the intraerythrocytic stage in Plasmodium falciparum |
title_fullStr |
N-linked glycoproteins are related to schizogony of the intraerythrocytic stage in Plasmodium falciparum |
title_full_unstemmed |
N-linked glycoproteins are related to schizogony of the intraerythrocytic stage in Plasmodium falciparum |
title_sort |
n-linked glycoproteins are related to schizogony of the intraerythrocytic stage in plasmodium falciparum |
url |
http://hdl.handle.net/20.500.12110/paper_00219258_v271_n24_p14452_Kimura |
work_keys_str_mv |
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