Abstract
The genomes of Plasmodium spp. encode a number of different multigene families that are thought to play a critical role for survival. However, with the exception of the P. falciparum var genes, very little is known about the biological roles of any of the other multigene families. Using the recently developed Selection Linked Integration method, we have been able to activate the expression of a single member of a multigene family of our choice in Plasmodium spp. from its endogenous promoter. We demonstrate the usefulness of this approach by activating the expression of a unique var, rifin and stevor in P. falciparum as well as yir in P. yoelii. Characterization of the selected parasites reveals differences between the different families in terms of mutual exclusive control, co-regulation, and host adaptation. Our results further support the application of the approach for the study of multigene families in Plasmodium and other organisms.
Highlights
The genomes of Plasmodium spp. encode a number of different multigene families that are thought to play a critical role for survival
This finding suggests that stevor, like var genes, are under some mutual exclusive control
One obvious shortcoming of these approaches is that they will fail to detect regulatory mechanisms arising from genomic loci not included in the constructs such as enhancer like elements, GCrich ncRNA or long non-coding RNA arising from introns, all of which can be found in P. falciparum[71,72,73]
Summary
The genomes of Plasmodium spp. encode a number of different multigene families that are thought to play a critical role for survival. In addition to a predicted role in host immune evasion[42,43], it has been shown that certain members of the var multigene family bind to receptors on the surface of human red blood cells or endothelial cells. Among those are chondroitin sulfate (CSA), CD36, thrombospondin, intercellular adhesion molecule1(ICAM1) and complement receptor 1 (CR1)[44,45,46]. In P. vivax VIRs have been suggested to be involved in binding to endothelial cells through interaction with ICAM149 while in the rodent Plasmodium species, P. chabaudi CIRs have been shown to interact with rodent red blood cells[50]
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