Source:http://linkedlifedata.com/resource/pubmed/id/12802682
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
6
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pubmed:dateCreated |
2003-8-25
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pubmed:abstractText |
Plasmodium falciparum parasites remodel the surface of human erythrocytes on invasion by the insertion of parasite-derived proteins in knob-like protrusions. P. falciparum erythrocyte membrane protein 1 (PfEMP-1), a variant surface antigen, has been shown to be anchored in these knobs and mediates adhesion to various host endothelial receptors. These proteins also undergo clonal antigenic variation as a means of immune evasion. Duffy binding-like-alpha(DBL-alpha) domain together with the cysteine-rich interdomain region form the head structure of the PfEMP1 molecule. In this report, we used ten different recombinant DBL-alpha fusion proteins expressed in Escherichia coli to generate antibodies in experimental animals. Five out of ten recombinant DBL-alpha fusion proteins were immunogenic and induced antibodies that reacted with conserved peptides derived from PfEMP1. Indirect immunofluorescence assay was used to localise PfEMP-1-DBL-alpha expressed in parasitised erythrocytes. Positive fluorescence reactivity was observed within the cytoplasm and with membrane structures but not on the surface of intact P. falciparum-infected erythrocytes.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Antibodies, Protozoan,
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, Protozoan,
http://linkedlifedata.com/resource/pubmed/chemical/Duffy Blood-Group System,
http://linkedlifedata.com/resource/pubmed/chemical/Protozoan Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/erythrocyte membrane protein 1...
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
0932-0113
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
90
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
467-72
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pubmed:dateRevised |
2007-11-15
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pubmed:meshHeading |
pubmed-meshheading:12802682-Amino Acid Sequence,
pubmed-meshheading:12802682-Animals,
pubmed-meshheading:12802682-Antibodies, Protozoan,
pubmed-meshheading:12802682-Antigens, Protozoan,
pubmed-meshheading:12802682-Duffy Blood-Group System,
pubmed-meshheading:12802682-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:12802682-Enzyme-Linked Immunosorbent Assay,
pubmed-meshheading:12802682-Erythrocyte Membrane,
pubmed-meshheading:12802682-Host-Parasite Interactions,
pubmed-meshheading:12802682-Molecular Sequence Data,
pubmed-meshheading:12802682-Plasmodium falciparum,
pubmed-meshheading:12802682-Protozoan Proteins,
pubmed-meshheading:12802682-Rats,
pubmed-meshheading:12802682-Recombinant Fusion Proteins,
pubmed-meshheading:12802682-Sequence Alignment
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pubmed:year |
2003
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pubmed:articleTitle |
Recombinant Duffy binding-like-alpha domains of Plasmodium falciparum erythrocyte membrane protein 1 elicit antibodies in rats that recognise conserved epitopes.
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pubmed:affiliation |
Department of Parasitology, Institute for Tropical Medicine, University of Tübingen, 72074 Tübingen, Germany.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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