title: N-linked glycoproteins are related to schizogony of the intraerythrocytic stage in Plasmodium falciparum.
abstract: 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(R), 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 microM 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.
authors.affiliation: Departamento de Parasitologia, Instituto de Ciências Biomédicas, Universidade de São Paulo, São Paulo, Brazil.
authors.forename: E A
authors.initials: EA
authors.lastname: Kimura
authors.forename: A S
authors.initials: AS
authors.lastname: Couto
authors.forename: V J
authors.initials: VJ
authors.lastname: Peres
authors.forename: O L
authors.initials: OL
authors.lastname: Casal
authors.forename: A M
authors.initials: AM
authors.lastname: Katzin
mesh_terms: D000581:Amidohydrolases; D000818:Animals; D002250:Carbon Radioisotopes; D002846:Chromatography, Affinity; D002850:Chromatography, Gel; D002854:Chromatography, Paper; D002855:Chromatography, Thin Layer; D003513:Cycloheximide / Q000494:pharmacology; D004591:Electrophoresis, Polyacrylamide Gel; D004912:Erythrocytes / Q000469:parasitology*; D005947:Glucose / Q000378:metabolism; D006023:Glycoproteins / Q000096:biosynthesis* / Q000302:isolation & purification; D006801:Humans; D007700:Kinetics; D016778:Malaria, Falciparum / Q000097:blood; D008358:Mannose / Q000378:metabolism; D008715:Methionine / Q000378:metabolism; D008970:Molecular Weight; D009844:Oligosaccharides / Q000737:chemistry / Q000302:isolation & purification; D018512:Parasitemia / Q000097:blood; D043524:Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase; D010963:Plasmodium falciparum / Q000187:drug effects / Q000472:pathogenicity / Q000502:physiology*; D015800:Protozoan Proteins / Q000096:biosynthesis* / Q000302:isolation & purification; D013462:Sulfur Radioisotopes; D014415:Tunicamycin / Q000494:pharmacology
chemical_list: D002250:Carbon Radioisotopes; D006023:Glycoproteins; D009844:Oligosaccharides; D015800:Protozoan Proteins; D013462:Sulfur Radioisotopes; D014415:Tunicamycin; D003513:Cycloheximide; D008715:Methionine; D000581:Amidohydrolases; D043524:Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase; D005947:Glucose; D008358:Mannose