N-linked glycoproteins are related to schizogony of the intraerythrocytic stage in Plasmodium falciparum

Mostrar todas las versiones(3)

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...

Descripción completa

Guardado en:

Detalles Bibliográficos
Autores principales:	Kimura, E.A., Couto, A.S., Peres, V.J., Casal, O.L., Katzin, A.M.
Formato:	Artículo publishedVersion
Publicado:	1996
Materias:	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
Acceso en línea:	http://hdl.handle.net/20.500.12110/paper_00219258_v271_n24_p14452_Kimura https://repositoriouba.sisbi.uba.ar/gsdl/cgi-bin/library.cgi?a=d&c=artiaex&d=paper_00219258_v271_n24_p14452_Kimura_oai
Aporte de:	Repositorio Digital de la Universidad de Buenos Aires (UBA) de Universidad de Buenos Aires

id	I28-R145-paper_00219258_v271_n24_p14452_Kimura_oai
record_format	dspace
spelling	I28-R145-paper_00219258_v271_n24_p14452_Kimura_oai2024-08-16 Kimura, E.A. Couto, A.S. Peres, V.J. Casal, O.L. Katzin, A.M. 1996 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. application/pdf http://hdl.handle.net/20.500.12110/paper_00219258_v271_n24_p14452_Kimura info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar J. BIOL. CHEM. 1996;271(24):14452-14461 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 N-linked glycoproteins are related to schizogony of the intraerythrocytic stage in Plasmodium falciparum info:eu-repo/semantics/article info:ar-repo/semantics/artículo info:eu-repo/semantics/publishedVersion https://repositoriouba.sisbi.uba.ar/gsdl/cgi-bin/library.cgi?a=d&c=artiaex&d=paper_00219258_v271_n24_p14452_Kimura_oai
institution	Universidad de Buenos Aires
institution_str	I-28
repository_str	R-145
collection	Repositorio Digital de la Universidad de Buenos Aires (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	Artículo Artículo publishedVersion
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
publishDate	1996
url	http://hdl.handle.net/20.500.12110/paper_00219258_v271_n24_p14452_Kimura https://repositoriouba.sisbi.uba.ar/gsdl/cgi-bin/library.cgi?a=d&c=artiaex&d=paper_00219258_v271_n24_p14452_Kimura_oai
work_keys_str_mv	AT kimuraea nlinkedglycoproteinsarerelatedtoschizogonyoftheintraerythrocyticstageinplasmodiumfalciparum AT coutoas nlinkedglycoproteinsarerelatedtoschizogonyoftheintraerythrocyticstageinplasmodiumfalciparum AT peresvj nlinkedglycoproteinsarerelatedtoschizogonyoftheintraerythrocyticstageinplasmodiumfalciparum AT casalol nlinkedglycoproteinsarerelatedtoschizogonyoftheintraerythrocyticstageinplasmodiumfalciparum AT katzinam nlinkedglycoproteinsarerelatedtoschizogonyoftheintraerythrocyticstageinplasmodiumfalciparum
_version_	1809357196239044608

N-linked glycoproteins are related to schizogony of the intraerythrocytic stage in Plasmodium falciparum

Ejemplares similares