Vinet, Adrien F.; Fukuda, Mitsunori; Turco, Salvatore J. et Descoteaux, Albert . The Leishmania donovani lipophosphoglycan excludes the vesicular proton-ATPase from phagosomes by impairing the recruitment of Synaptotagmin V In: 9e symposium annuel de parasitologie moléculaire du Québec, 18-19 juin 2009, Université McGill.
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Upon their internalization by macrophages, Leishmania donovani promastigotes inhibit phagolysosome biogenesis. This inhibition is mediated by the virulence glycolipid lipophosphoglycan (LPG), a polymer of the Galβ1,4Manα1-PO4 units attached to the promastigote surface via an unusual glycosylphosphatidylinositol anchor. We recently showed that the exocytosis regulator Synaptotagmin (Syt) V controls early steps of phagocytosis, and remains associated to the phagosome during the maturation process. Here, we show that Syt V contributes to phagolysosome biogenesis by regulating the acquisition of cathepsin D and the vesicular proton-ATPase. Insertion of LPG into ganglioside GM1-containing microdomains excluded Syt V from phagosome membranes, enabling L. donovani promatigotes to inhibit the recruitment of the vesicular proton-ATPase to phagosomes, preventing their acidification. Collectively, these results reveal a novel function for Syt V in phagolysosome biogenesis and provide novel insight into the mechanism of vesicular proton-ATPase recruitment to maturing phagosomes. We also provide novel finding into the mechanism of Leishmania pathogenesis, whereby targeting of Syt V is part of the strategy used by L. donovani promastigotes to prevent phagosome acidification.
| Type de document: | Document issu d'une conférence ou d'un atelier |
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| Mots-clés libres: | - |
| Centre: | Centre INRS-Institut Armand Frappier |
| Date de dépôt: | 02 mai 2018 21:11 |
| Dernière modification: | 02 mai 2018 21:11 |
| URI: | https://espace.inrs.ca/id/eprint/7106 |
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