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Summary    P   lasmodium falciparum  virulence is linked to its ability to sequester in post‐capillary venules in the human host.   P   lasmodium falciparum  erythrocyte membrane protein 1 ( PfEMP 1) is the main variant surface antigen implicated in this process. Complete loss of parasite adhesion is linked to a large subtelomeric deletion on chromosome 9 in a number of laboratory strains such as  D 10 and  T 9‐96. Similar to the cytoadherent reference line  FCR 3,  D 10 strain expresses  PfEMP 1 on the surface of parasitized erythrocytes, however without any detectable cytoadhesion. To investigate which of the deleted subtelomeric genes may be implicated in parasite adhesion, we selected 12 genes for  D 10 complementation studies that are predicted to code for proteins exported to the red blood cell. We identified a novel single copy gene ( PF 3 D 7_0936500) restricted to   P   . falciparum  that restores adhesion to  CD 36, termed here virulence‐associated protein 1 (  Pfvap1  ). Protein knockdown and gene knockout experiments confirmed a role of  PfVAP 1 in the adhesion process in  FCR 3 parasites.  PfVAP 1 is co‐exported with  PfEMP 1 into the host cell via vesicle‐like structures called  M aurer's clefts. This study identifies a novel highly conserved parasite molecule that contributes to parasite virulence possibly by assisting  PfEMP 1 to establish functional adhesion at the host cell surface.

cellular microbiology

Discovery of a novel and conserved   P   lasmodium falciparum  exported protein that is important for adhesion of  PfEMP 1 at the surface of infected erythrocytes