Source:http://linkedlifedata.com/resource/pubmed/id/16262724
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
12
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pubmed:dateCreated |
2005-11-2
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pubmed:abstractText |
The intracellular protozoan Toxoplasma gondii is auxotrophic for low-density lipoprotein (LDL)-derived cholesterol (C). We previously showed that T. gondii scavenges this essential lipid from host endolysosomal compartments and that C delivery to the parasitophorous vacuole (PV) does not require transit through host Golgi or endoplasmic reticulum. In this study, we explore the itinerary of C from the host endolysosomes to the PV. Labeled C incorporated into LDL is rapidly detected in intravacuolar parasites and partially esterified by the parasites. In contrast to diverse mammalian organelles, the post-endolysosomal transfer of C to the PV does not involve the host plasma membrane as an intermediate. Nevertheless, the PV membrane is accessible to extracellular sterol acceptors, suggesting C trafficking from intracellular parasites to host plasma membrane. C movement to the PV requires temperatures permissive for vesicular transport, metabolic energy and functional microtubules. Host caveolae vesicles and the sterol carrier protein-2 do not participate in this process. Proteolytic treatment of purified PV or free parasites abolishes C acquisition by the parasites. Altogether, these results support a vesicular transport system from host endolysosomes to the PV, and a requirement for PV membrane and parasite plasma membrane proteins in C delivery to T. gondii.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Caveolin 1,
http://linkedlifedata.com/resource/pubmed/chemical/Cholesterol,
http://linkedlifedata.com/resource/pubmed/chemical/Cholesterol, LDL,
http://linkedlifedata.com/resource/pubmed/chemical/Cholesterol Esters,
http://linkedlifedata.com/resource/pubmed/chemical/sterol carrier proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
1398-9219
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
6
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1125-41
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:16262724-Animals,
pubmed-meshheading:16262724-Carrier Proteins,
pubmed-meshheading:16262724-Caveolin 1,
pubmed-meshheading:16262724-Cell Membrane,
pubmed-meshheading:16262724-Cercopithecus aethiops,
pubmed-meshheading:16262724-Cholesterol,
pubmed-meshheading:16262724-Cholesterol, LDL,
pubmed-meshheading:16262724-Cholesterol Esters,
pubmed-meshheading:16262724-Gene Expression Profiling,
pubmed-meshheading:16262724-Toxoplasma,
pubmed-meshheading:16262724-Toxoplasmosis,
pubmed-meshheading:16262724-Vacuoles,
pubmed-meshheading:16262724-Vero Cells
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pubmed:year |
2005
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pubmed:articleTitle |
Peculiarities of host cholesterol transport to the unique intracellular vacuole containing Toxoplasma.
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pubmed:affiliation |
Department of Internal Medicine, Yale University School of Medicine, 333 Cedar Street, New Haven, CT 06520, USA.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't,
Research Support, N.I.H., Extramural
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