Source:http://linkedlifedata.com/resource/pubmed/id/17960733
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
21
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pubmed:dateCreated |
2007-10-31
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pubmed:abstractText |
Parasitic organisms are incapable of de novo fatty acid synthesis due to a down-regulated expression of enzymes involved in the oxygen-dependent pathway. We investigated the uptake of host lipids by a 150-kDa hydrophobic ligand-binding protein (HLBP) of Taenia solium metacestode, an agent causative of neurocysticercosis. The protein was found to be a hetero-oligomeric complex consisting of multiple subunits (M(r) 7, 10, and 15 kDa within pH 8.0-9.7), which may originate from four unique genes of 7- and 10-kDa gene families with 2-3 polymorphic alleles/paralogs. The 15-kDa protein represented glycosylated forms of the 10-kDa. With high binding affinity to lipid analogs, these subunits evidenced high-level sequence identity with other cestode HLBPs and form a novel clade associated with excretory-secretory type HLBP. In vitro experiments with viable worms suggested that the excreted 150-kDa protein might bind to lipids, and participate in the translocation of host lipids across the syncytial membrane. This process was substantially inhibited by the specific anti-150 kDa antibodies. The protein was localized in the parasite syncytium and in the lipid droplets within host granuloma wall, where significant lipase activity was expressed. HLBP-mediated uptake of the host lipid may be critical for the parasite survival and thus could be targeted by chemotherapeutics and/or vaccine.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
1615-9853
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
7
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
4016-30
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pubmed:dateRevised |
2010-11-18
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pubmed:meshHeading |
pubmed-meshheading:17960733-Amino Acid Sequence,
pubmed-meshheading:17960733-Animals,
pubmed-meshheading:17960733-Carrier Proteins,
pubmed-meshheading:17960733-Genes, Helminth,
pubmed-meshheading:17960733-Helminth Proteins,
pubmed-meshheading:17960733-Homeostasis,
pubmed-meshheading:17960733-Humans,
pubmed-meshheading:17960733-Hydrophobic and Hydrophilic Interactions,
pubmed-meshheading:17960733-Ligands,
pubmed-meshheading:17960733-Lipid Metabolism,
pubmed-meshheading:17960733-Molecular Sequence Data,
pubmed-meshheading:17960733-Molecular Weight,
pubmed-meshheading:17960733-Multigene Family,
pubmed-meshheading:17960733-Neurocysticercosis,
pubmed-meshheading:17960733-Phylogeny,
pubmed-meshheading:17960733-Sequence Homology, Amino Acid,
pubmed-meshheading:17960733-Taenia solium
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pubmed:year |
2007
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pubmed:articleTitle |
A hydrophobic ligand-binding protein of the Taenia solium metacestode mediates uptake of the host lipid: implication for the maintenance of parasitic cellular homeostasis.
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pubmed:affiliation |
Department of Molecular Parasitology, Sungkyunkwan University School of Medicine, Suwon, Korea.
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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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