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Activation of TLR2 and TLR4 by Glycosylphosphatidylinositols Derived from Toxoplasma gondii1
- F. Debierre-Grockiego, M. A. Campos, +9 authors R. Schwarz
- Biology, MedicineThe Journal of Immunology
- 15 July 2007
Both TLR2 and TLR4 receptors may participate in the host defense against T. gondii infection through their activation by the GPIs and could work together with other MyD88-dependent receptors, like other TLRs or even IL-18R or IL-1R, to obtain an effective host response against the parasite.
Glycosylphosphatidylinositol toxin of Plasmodium induces nitric oxide synthase expression in macrophages and vascular endothelial cells by a protein tyrosine kinase-dependent and protein kinase…
In this study, we demonstrate that glycosylphosphatidylinositol (GPI) is a major toxin of Plasmodium falciparum origin responsible for nitric oxide (NO) production in host cells. Purified malarial…
Glycosylphosphatidylinositol toxin of Plasmodium up-regulates intercellular adhesion molecule-1, vascular cell adhesion molecule-1, and E-selectin expression in vascular endothelial cells and…
- L. Schofield, S. Novakovic, P. Gerold, R. Schwarz, M. McConville, S. Tachado
- Biology, MedicineJournal of immunology
- 1 March 1996
A parasite-derived GPI toxin activates vascular endothelial cells by tyrosine kinase-mediated signal transduction, leading to NF kappa B/c-rel activation and downstream expression of adhesins, events that may play a central role in the etiology of cerebral malaria.
Primary structure of the precursor to the three major surface antigens of Plasmodium falciparum merozoites
The complete structure of the P195 gene determined from further DNA clones is described, its organization within genomic DNA and the location of the specific processing fragments within the primary amino-acid sequence are described.
Structural analysis of the glycosyl-phosphatidylinositol membrane anchor of the merozoite surface proteins-1 and -2 of Plasmodium falciparum.
- P. Gerold, L. Schofield, M. Blackman, A. Holder, R. Schwarz
- Biology, MedicineMolecular and biochemical parasitology
Detailed structural analysis of the core-glycans showed that the GPI-anchors of both proteins possess an extra alpha 1-2 linked mannose at the conserved trimannosyl-core-glycan.
Interference with glycosylation of glycoproteins. Inhibition of formation of lipid-linked oligosaccharides in vivo.
Kinetic analysis showed that the inhibitors affected first the assembly of lipid-linked oligosaccharides and then protein glycosylation after a lag period, and the reversible effects of these inhibitors exemplify their usefulness as tools in the study of gly cosylation processes.
Roles of Glycosylphosphatidylinositols of Toxoplasma gondii
- F. Debierre-Grockiego, N. Azzouz, +6 authors R. Schwarz
- Biology, MedicineJournal of Biological Chemistry
- 29 August 2003
It is shown that GPIs highly purified from T. gondii tachyzoites, as well as their core glycans, induce TNFα production in macrophages, supporting the idea that T. Gondii GPIs are bioactive factors that participate in the production of TNF α during toxoplasmal pathogenesis.
Saccharomyces cerevisiae GPI10, the functional homologue of human PIG-B, is required for glycosylphosphatidylinositol-anchor synthesis.
- C. Sütterlin, M. V. Escribano, +5 authors H. Riezman
- Biology, MedicineThe Biochemical journal
- 15 May 1998
Overexpression of GPI10 gives partial resistance to the GPI-synthesis inhibitor YW3548, suggesting that this gene product may affect the target of the inhibitor.
Neutralizing monoclonal antibodies to glycosylphosphatidylinositol, the dominant TNF-alpha-inducing toxin of Plasmodium falciparum: prospects for the immunotherapy of severe malaria.
- L. Schofield, L. Vivas, F. Hackett, P. Gerold, R. Schwarz, S. Tachado
- Biology, MedicineAnnals of tropical medicine and parasitology
A central role for glycosylphosphatidylinositol of parasite origin in the aetiology of severe malaria is suggested and novel approaches for the immunotherapy or immunoprophylaxis of disease are suggested.
Sequencing of the smallest Apicomplexan genome from the human pathogen Babesia microti†
- E. Cornillot, K. Hadj-Kaddour, +23 authors Choukri Ben Mamoun
- Biology, MedicineNucleic acids research
- 24 July 2012
The genomic sequencing of Babesia microti identified several targets suitable for the development of diagnostic assays and novel therapies for human babesiosis, including the minimal metabolic requirement for intraerythrocytic protozoan parasitism.