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

Autores
Kimura, E.A.; Couto, A.S.; Peres, V.J.; Casal, O.L.; Katzin, A.M.
Año de publicación
1996
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
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.
Fuente
J. BIOL. CHEM. 1996;271(24):14452-14461
Materia
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
Nivel de accesibilidad
acceso abierto
Condiciones de uso
http://creativecommons.org/licenses/by/2.5/ar
Repositorio
Biblioteca Digital (UBA-FCEN)
Institución
Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturales
OAI Identificador
paperaa:paper_00219258_v271_n24_p14452_Kimura

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oai_identifier_str paperaa:paper_00219258_v271_n24_p14452_Kimura
network_acronym_str BDUBAFCEN
repository_id_str 1896
network_name_str Biblioteca Digital (UBA-FCEN)
spelling N-linked glycoproteins are related to schizogony of the intraerythrocytic stage in Plasmodium falciparumKimura, E.A.Couto, A.S.Peres, V.J.Casal, O.L.Katzin, A.M.asparagine linked oligosaccharideconcanavalin aglucan synthaseglycoproteinsepharosetunicamycinarticlecontrolled studyerythrocytelife cyclenonhumanplasmodium falciparumpriority journalprotein glycosylationprotein synthesisschizonttrophozoiteAmidohydrolasesAnimalsCarbon RadioisotopesChromatography, AffinityChromatography, GelChromatography, PaperChromatography, Thin LayerCycloheximideElectrophoresis, Polyacrylamide GelErythrocytesGlucoseGlycoproteinsHumansKineticsMalaria, FalciparumMannoseMethionineMolecular WeightOligosaccharidesParasitemiaPeptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine AmidasePlasmodium falciparumProtozoan ProteinsSulfur RadioisotopesTunicamycinAlthough 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.1996info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfhttp://hdl.handle.net/20.500.12110/paper_00219258_v271_n24_p14452_KimuraJ. BIOL. CHEM. 1996;271(24):14452-14461reponame:Biblioteca Digital (UBA-FCEN)instname:Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturalesinstacron:UBA-FCENenginfo:eu-repo/semantics/openAccesshttp://creativecommons.org/licenses/by/2.5/ar2025-11-13T08:45:29Zpaperaa:paper_00219258_v271_n24_p14452_KimuraInstitucionalhttps://digital.bl.fcen.uba.ar/Universidad públicaNo correspondehttps://digital.bl.fcen.uba.ar/cgi-bin/oaiserver.cgiana@bl.fcen.uba.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:18962025-11-13 08:45:30.7Biblioteca Digital (UBA-FCEN) - Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturalesfalse
dc.title.none.fl_str_mv N-linked glycoproteins are related to schizogony of the intraerythrocytic stage in Plasmodium falciparum
title N-linked glycoproteins are related to schizogony of the intraerythrocytic stage in Plasmodium falciparum
spellingShingle N-linked glycoproteins are related to schizogony of the intraerythrocytic stage in Plasmodium falciparum
Kimura, E.A.
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
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
dc.creator.none.fl_str_mv Kimura, E.A.
Couto, A.S.
Peres, V.J.
Casal, O.L.
Katzin, A.M.
author Kimura, E.A.
author_facet Kimura, E.A.
Couto, A.S.
Peres, V.J.
Casal, O.L.
Katzin, A.M.
author_role author
author2 Couto, A.S.
Peres, V.J.
Casal, O.L.
Katzin, A.M.
author2_role author
author
author
author
dc.subject.none.fl_str_mv 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
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
dc.description.none.fl_txt_mv 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.
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.
publishDate 1996
dc.date.none.fl_str_mv 1996
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/20.500.12110/paper_00219258_v271_n24_p14452_Kimura
url http://hdl.handle.net/20.500.12110/paper_00219258_v271_n24_p14452_Kimura
dc.language.none.fl_str_mv eng
language eng
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
http://creativecommons.org/licenses/by/2.5/ar
eu_rights_str_mv openAccess
rights_invalid_str_mv http://creativecommons.org/licenses/by/2.5/ar
dc.format.none.fl_str_mv application/pdf
dc.source.none.fl_str_mv J. BIOL. CHEM. 1996;271(24):14452-14461
reponame:Biblioteca Digital (UBA-FCEN)
instname:Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturales
instacron:UBA-FCEN
reponame_str Biblioteca Digital (UBA-FCEN)
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instname_str Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturales
instacron_str UBA-FCEN
institution UBA-FCEN
repository.name.fl_str_mv Biblioteca Digital (UBA-FCEN) - Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturales
repository.mail.fl_str_mv ana@bl.fcen.uba.ar
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