Source:http://linkedlifedata.com/resource/pubmed/id/10838226
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
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pubmed:dateCreated |
2000-8-30
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pubmed:databankReference | |
pubmed:abstractText |
A distinctive pathological feature of Plasmodium falciparum malaria is the endothelial attachment of erythrocytes infected with mature asexual-stage parasites in microvessels of the major organs. Electron-dense protrusions described as knobs are displayed on the surface of parasitized erythrocytes and act as attachment points in cytoadherence. Parasite-encoded knob-associated histidine-rich protein (KAHRP) is a major component of knobs found on the cytoplasmic side of the host cell membrane. P. falciparum erythrocyte membrane protein 1 (PfEMP1) is a family of parasite-encoded cytoadherence receptors localized to knobs on the surface of parasitized erythrocytes. Despite its high antigenic diversity, PfEMP1 has a remarkably conserved cytoplasmic domain. We demonstrate in this study that the cytoplasmic domain of PfEMP1 (VAR(CD)) binds to host spectrin and actin and to full-length KAHRP in vitro. Apparent dissociation constants determined for VAR(CD)/F-actin and VAR(CD)/KAHRP interactions are 44.9+/-6.4 and 10. 7+/-2.2 nM, respectively. Further, we provide evidence that KAHRP polypeptides self-associate in solution to form structures similar to knobs and show binding of self-associated KAHRP clusters to spectrin-actin-protein 4.1 complexes. Findings in this study suggest that PfEMP1 is localized to the knob in P. falciparum-infected erythrocytes by binding to the host spectrin-actin junction and to self-associated KAHRP through its conserved cytoplasmic domain.
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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/Actins,
http://linkedlifedata.com/resource/pubmed/chemical/Cell Cycle Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/MAK16 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/Peptides,
http://linkedlifedata.com/resource/pubmed/chemical/Protozoan Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Spectrin,
http://linkedlifedata.com/resource/pubmed/chemical/erythrocyte membrane protein 1...,
http://linkedlifedata.com/resource/pubmed/chemical/knob protein, Plasmodium falciparum
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
0166-6851
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
108
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
237-47
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:10838226-Actins,
pubmed-meshheading:10838226-Animals,
pubmed-meshheading:10838226-Cell Cycle Proteins,
pubmed-meshheading:10838226-Cloning, Molecular,
pubmed-meshheading:10838226-Erythrocyte Membrane,
pubmed-meshheading:10838226-Molecular Sequence Data,
pubmed-meshheading:10838226-Peptides,
pubmed-meshheading:10838226-Plasmodium falciparum,
pubmed-meshheading:10838226-Protozoan Proteins,
pubmed-meshheading:10838226-Saccharomyces cerevisiae Proteins,
pubmed-meshheading:10838226-Spectrin
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pubmed:year |
2000
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pubmed:articleTitle |
Plasmodium falciparum erythrocyte membrane protein 1 is anchored to the actin-spectrin junction and knob-associated histidine-rich protein in the erythrocyte skeleton.
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pubmed:affiliation |
Department of Medicine, Section of Hematology-Oncology Research, St. Elizabeth's Medical Center, Tufts University School of Medicine, 736 Cambridge Street, 02135, Boston, MA, USA. stevenoh@semc.org
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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