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© Artur Scherf
Scanning Electron Microscopy of Red Blood Cell infected by Plasmodium falciparum.
Publication : Parasitology research

Recombinant Duffy binding-like-alpha domains of Plasmodium falciparum erythrocyte membrane protein 1 elicit antibodies in rats that recognise conserved epitopes

Scientific Fields
Diseases
Organisms
Applications
Technique

Published in Parasitology research - 12 Jun 2003

Oguariri RM, Mattei D, Tena-Tomás C, Uhlemann AC, Kremsner PG, Kun JF

Link to Pubmed [PMID] – 12802682

Parasitol. Res. 2003 Aug;90(6):467-72

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.

http://www.ncbi.nlm.nih.gov/pubmed/12802682