Department of Medicine, Division of Infectious Diseases and Immunology
Immunity | Parasitic Diseases | Parasitology
Glycosylphosphatidylinositols (GPIs) from several protozoan parasites are thought to elicit a detrimental stimulation of the host innate immune system aside their main function to anchor surface proteins. Here we analyzed the GPI biosynthesis of an avirulent Toxoplasma gondii type 2 strain (PTG) by metabolic radioactive labeling. We determined the biological function of individual GPI species in the PTG strain in comparison with previously characterized GPI-anchors of a virulent strain (RH). The GPI intermediates of both strains were structurally similar, however the abundance of two of six GPI intermediates was significantly reduced in the PTG strain. The side-by-side comparison of GPI-anchor content revealed that the PTG strain had only approximately 34% of the protein-free GPIs as well as approximately 70% of the GPI-anchored proteins with significantly lower rates of protein N-glycosylation compared to the RH strain. All mature GPIs from both strains induced comparable secretion levels of TNF-alpha and IL-12p40, and initiated TLR4/MyD88-dependent NF-kappaBp65 activation in macrophages. Taken together, these results demonstrate that PTG and RH strains differ in their GPI biosynthesis and possess significantly different GPI-anchor content, while individual GPI species of both strains induce similar biological functions in macrophages.
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Citation: PLoS One. 2014 Jan 28;9(1):e85386. doi: 10.1371/journal.pone.0085386. eCollection 2014.Link to article on publisher's site
Niehus, Sebastian; Smith, Terry K.; Azzouz, Nahid; Campos, Marco A.; Dubremetz, Jean-Francois; Gazzinelli, Ricardo T.; Schwarz, Ralph T.; and -Grockiego, Francoise Debierre, "Virulent and avirulent strains of Toxoplasma gondii which differ in their glycosylphosphatidylinositol content induce similar biological functions in macrophages" (2014). University of Massachusetts Medical School Faculty Publications. 438.
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