Pellé KG1,
Jiang RH1,2,
Mantel PY1,
Xiao YP3,
Hjelmqvist D1,
Gallego-Lopez GM4,
Lau AO4,
Kang BH5,
Allred DR3,6,
Marti M1.
Abstract
Apicomplexans are a diverse group of obligate parasites occupying different intracellular niches that require modification to meet the needs of the parasite. To efficiently manipulate their environment, apicomplexans translocate numerous parasite proteins into the host cell. Whereas some parasites remain contained within a parasitophorous vacuole membrane (PVM) throughout their developmental cycle, others do not, a difference that affects the machinery needed for protein export. A signal-mediated pathway for protein export into the host cell has been characterized in malaria parasites, which maintain the PVM. Here, we functionally demonstrate an analogous host-targeting pathway involving organellar staging prior to secretion in the related bovine parasite, Babesia bovis, a parasite that destroys the PVM shortly after invasion. Taking into account recent identification of a similar signal-mediated pathway in the coccidian parasite Toxoplasma gondii, we suggest a model in which this conserved pathway has evolved in multiple steps from signal-mediated trafficking to specific secretory organelles for controlled secretion to a complex protein translocation process across the PVM.
This article is protected by copyright. All rights reserved.
KEYWORDS:
Bioinformatics; Diversity; Microbial-cell interaction; Protozoa
- PMID:
- 25996544
- [PubMed - as supplied by publisher]
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