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pubmed-article:12802682pubmed:abstractTextPlasmodium 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.lld:pubmed
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pubmed-article:12802682pubmed:pagination467-72lld:pubmed
pubmed-article:12802682pubmed:dateRevised2007-11-15lld:pubmed
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pubmed-article:12802682pubmed:articleTitleRecombinant Duffy binding-like-alpha domains of Plasmodium falciparum erythrocyte membrane protein 1 elicit antibodies in rats that recognise conserved epitopes.lld:pubmed
pubmed-article:12802682pubmed:affiliationDepartment of Parasitology, Institute for Tropical Medicine, University of Tübingen, 72074 Tübingen, Germany.lld:pubmed
pubmed-article:12802682pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:12802682pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed
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