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
.jpg)
- Institución
- Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturales
- OAI Identificador
- paperaa:paper_00219258_v271_n24_p14452_Kimura
Ver los metadatos del registro completo
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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 |
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openAccess |
| rights_invalid_str_mv |
http://creativecommons.org/licenses/by/2.5/ar |
| dc.format.none.fl_str_mv |
application/pdf |
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