Source:http://linkedlifedata.com/resource/pubmed/id/18047571
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
1
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| pubmed:dateCreated |
2007-12-14
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| pubmed:abstractText |
The Duffy binding-like (DBL) domain is a key adhesive module in Plasmodium falciparum, present in both erythrocyte invasion ligands (EBLs) and the large and diverse P. falciparum erythrocyte membrane protein 1 (PfEMP1) family of cytoadherence receptors. DBL domains bind a variety of different host receptors, including intercellular adhesion molecule 1 (ICAM-1), a receptor interaction that may have a role in infected erythrocyte binding to cerebral blood vessels and cerebral malaria. In this study, we expressed the nearly full complement of DBLbeta-C2 domains from the IT4/25/5 (IT4) parasite isolate and showed that ICAM-1-binding domains (DBLbeta-C2(ICAM-1)) were confined to group B and group C PfEMP1 proteins and were not present in group A, suggesting that ICAM-1 selection pressure differs between PfEMP1 groups. To further dissect the molecular determinants of binding, we modelled a DBLbeta-C2(ICAM-1) domain on a solved DBL structure and created alanine substitution mutants in two DBLbeta-C2(ICAM-1) domains. This analysis indicates that the DBLbeta-C2::ICAM-1 interaction maps to the equivalent glycan binding region of EBLs, and suggests a general model for how DBL domains evolve under dual selection for host receptor binding and immune evasion.
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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/Antigens, Protozoan,
http://linkedlifedata.com/resource/pubmed/chemical/Duffy antigen binding protein...,
http://linkedlifedata.com/resource/pubmed/chemical/Intercellular Adhesion Molecule-1,
http://linkedlifedata.com/resource/pubmed/chemical/Protozoan Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Cell Surface,
http://linkedlifedata.com/resource/pubmed/chemical/erythrocyte membrane protein 1...
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| pubmed:status |
MEDLINE
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| pubmed:month |
Jan
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| pubmed:issn |
0950-382X
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| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:volume |
67
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| pubmed:owner |
NLM
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| pubmed:authorsComplete |
Y
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| pubmed:pagination |
78-87
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| pubmed:meshHeading |
pubmed-meshheading:18047571-Amino Acid Sequence,
pubmed-meshheading:18047571-Animals,
pubmed-meshheading:18047571-Antigens, Protozoan,
pubmed-meshheading:18047571-Binding Sites,
pubmed-meshheading:18047571-COS Cells,
pubmed-meshheading:18047571-Cercopithecus aethiops,
pubmed-meshheading:18047571-Host-Parasite Interactions,
pubmed-meshheading:18047571-Intercellular Adhesion Molecule-1,
pubmed-meshheading:18047571-Models, Molecular,
pubmed-meshheading:18047571-Molecular Sequence Data,
pubmed-meshheading:18047571-Mutagenesis, Site-Directed,
pubmed-meshheading:18047571-Phylogeny,
pubmed-meshheading:18047571-Plasmodium falciparum,
pubmed-meshheading:18047571-Protein Binding,
pubmed-meshheading:18047571-Protein Interaction Mapping,
pubmed-meshheading:18047571-Protein Structure, Tertiary,
pubmed-meshheading:18047571-Protozoan Proteins,
pubmed-meshheading:18047571-Receptors, Cell Surface,
pubmed-meshheading:18047571-Sequence Alignment,
pubmed-meshheading:18047571-Sequence Analysis
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| pubmed:year |
2008
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| pubmed:articleTitle |
Mapping a common interaction site used by Plasmodium falciparum Duffy binding-like domains to bind diverse host receptors.
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| pubmed:affiliation |
Seattle Biomedical Research Institute, 307 Westlake Ave N, Ste 500, Seattle, WA 98109-5219, 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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