期刊
SCIENTIFIC REPORTS
卷 6, 期 -, 页码 -出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/srep38842
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资金
- Laboratoire d'Excellence (LabEx) ParaFrap from the National Agency for Research [ANR-11-LABX-0024, ANR-14-CE14-0002-01]
- INSERM
- Pasteur Institute of Lille
- CNRS
- DFG/ANR [GO 284/8-1]
- LabEx ParaFrap
- European Research Council (ERC Consolidator grant) [614880]
- European Research Council (ERC) [614880] Funding Source: European Research Council (ERC)
Accurate sorting of proteins to the three types of parasite-specific secretory organelles namely rhoptry, microneme and dense granule in Toxoplasma gondii is crucial for successful host cell invasion by this obligate intracellular parasite. Despite its tiny body architecture and limited trafficking machinery, T. gondii relies heavily on transport of vesicles containing proteins, lipids and important virulence-like factors that are delivered to these secretory organelles. However, our understanding on how trafficking of vesicles operates in the parasite is still limited. Here, we show that the T. gondii vacuolar protein sorting 9 (TgVps9), has guanine nucleotide exchange factor (GEF) activity towards Rab5a and is crucial for sorting of proteins destined to secretory organelles. Our results illuminate features of TgVps9 protein as a key trafficking facilitator that regulates protein maturation, secretory organelle formation and secretion, thereby ensuring a primary role in host infection by T. gondii.
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