Genes for glycosylphosphatidylinositol toxin biosynthesis in Plasmodium falciparum.

Détails

ID Serval
serval:BIB_581833C4A297
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Titre
Genes for glycosylphosphatidylinositol toxin biosynthesis in Plasmodium falciparum.
Périodique
Infection and Immunity
Auteur⸱e⸱s
Delorenzi M., Sexton A., Shams-Eldin H., Schwarz R.T., Speed T., Schofield L.
ISSN
0019-9567 (Print)
ISSN-L
0019-9567
Statut éditorial
Publié
Date de publication
2002
Volume
70
Numéro
8
Pages
4510-4522
Langue
anglais
Résumé
About 2.5 million people die of Plasmodium falciparum malaria every year. Fatalities are associated with systemic and organ-specific inflammation initiated by a parasite toxin. Recent studies show that glycosylphosphatidylinositol (GPI) functions as the dominant parasite toxin in the context of infection. GPIs also serve as membrane anchors for several of the most important surface antigens of parasite invasive stages. GPI anchoring is a complex posttranslational modification produced through the coordinated action of a multicomponent biosynthetic pathway. Here we present eight new genes of P. falciparum selected for encoding homologs of proteins essential for GPI synthesis: PIG-A, PIG-B, PIG-M, PIG-O, GPI1, GPI8, GAA-1, and DPM1. We describe the experimentally verified mRNA and predicted amino acid sequences and in situ localization of the gene products to the parasite endoplasmic reticulum. Moreover, we show preliminary evidence for the PIG-L and PIG-C genes. The biosynthetic pathway of the malaria parasite GPI offers potential targets for drug development and may be useful for studying parasite cell biology and the molecular basis for the pathophysiology of parasitic diseases.
Mots-clé
Acetylation, Acetylglucosamine/metabolism, Amino Acid Sequence, Animals, Base Sequence, Cell Adhesion Molecules/genetics, DNA, Protozoan, Genes, Protozoan, Glycosylphosphatidylinositols/biosynthesis, Humans, Mannosyltransferases/genetics, Membrane Glycoproteins/genetics, Membrane Proteins/genetics, Molecular Sequence Data, Phosphatidylinositols/metabolism, Plasmodium falciparum/genetics, Protozoan Proteins/genetics, Saccharomyces cerevisiae Proteins, Sequence Homology, Amino Acid, Uridine Diphosphate N-Acetylglucosamine/metabolism
Pubmed
Web of science
Open Access
Oui
Création de la notice
22/04/2013 9:26
Dernière modification de la notice
20/08/2019 15:11
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