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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Autores principales: Kimura, E.A., Couto, A.S., Peres, V.J., Casal, O.L., Katzin, A.M.
Formato: JOUR
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spelling 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 AT kimuraea nlinkedglycoproteinsarerelatedtoschizogonyoftheintraerythrocyticstageinplasmodiumfalciparum
AT coutoas nlinkedglycoproteinsarerelatedtoschizogonyoftheintraerythrocyticstageinplasmodiumfalciparum
AT peresvj nlinkedglycoproteinsarerelatedtoschizogonyoftheintraerythrocyticstageinplasmodiumfalciparum
AT casalol nlinkedglycoproteinsarerelatedtoschizogonyoftheintraerythrocyticstageinplasmodiumfalciparum
AT katzinam nlinkedglycoproteinsarerelatedtoschizogonyoftheintraerythrocyticstageinplasmodiumfalciparum
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