Mutant/mutation
The mutant lacks expression of PoFUT2

Protein (function)
Thrombospondin type 1 repeat (TSR) domains are small (50–60 amino acid residues) cysteine-knot motifs with 3 conserved disulfide bonds that play important roles in cell adhesion and motility. Plasmodium parasites express several TSR domain- containing proteins throughout the different stages of their life cycle that are critical for host cell recognition, motility, and invasion. These proteins include circumsporozoite protein (CSP) and thrombospondin-related anonymous protein (TRAP) in the sporozoite stage and circumsporozoite and TRAP-related protein (CTRP) in the ookinete stage. TSR domains are O-fucosylated by protein O-fucosyltransferase 2 (PoFUT2). That fucose can be further elongated with a glucose residue, generating an O-linked disaccharide. This modification is important for the secretion of TSR domain- containing proteins. CSP and TRAP TSR domains are also O-fucosylated in the Plasmodium sporozoite stage. A homolog of PoFUT2 is conserved in all the Plasmodium species sequenced, and the parasite synthesizes the GDP-fucose (GDP-Fuc) precursor required for O-fucosylation. It has been shown that the P. falciparum protein O-fucosyltransferase (PoFUT2) is involved in the O-fucosylation of parasite TSR domains. 
It was reported by Lopaticki et al. (2017) that PoFUT2 genetic disruption in P. falciparum resulted in a reduction in the ability of ookinetes to traverse the mosquito midgut to form oocysts and evidence was provided that mosquitoes infected with PoFUT2 KO parasites harbored significantly  fewer sporozoites in the mosquito salivary glands compared to mosquitoes infected with  the wild type P. falciparum parental line, NF54. Finally, they assessed the infectivity of salivary gland sporozoites by analyzing their motility, cell traversal activity, and hepatocyte invasion and by carrying out co-infection experiments using wild type and mutant parasites in a humanized chimeric liver mouse model; these assays revealed an apparent lower fitness of ΔPoFUT2 parasites in completing development in the mosquito and infecting mammalian hepatocytes compared to wild type NF54. Here, we report a robust study that differs from the central results of the previous report and reveals that under laboratory conditions, that PoFUT2 is not essential for murine parasite development and transmission.

Phenotype
No phenotype was detected throughout the life cycle. Normal oocyst and sporozoite production. Normal sporozoite motility and infectivity (in vitro and in vivo).

Additional information
It was reported by Lopaticki et al. (2017) that PoFUT2 genetic disruption in P. falciparum resulted in a reduction in the ability of ookinetes to traverse the mosquito midgut to form oocysts and evidence was provided that mosquitoes infected with PoFUT2 KO parasites harbored significantly  fewer sporozoites in the mosquito salivary glands compared to mosquitoes infected with  the wild type P. falciparum parental line, NF54. Finally, they assessed the infectivity of salivary gland sporozoites by analyzing their motility, cell traversal activity, and hepatocyte invasion and by carrying out co-infection experiments using wild type and mutant parasites in a humanized chimeric liver mouse model; these assays revealed an apparent lower fitness of ΔPoFUT2 parasites in completing development in the mosquito and infecting mammalian hepatocytes compared to wild type NF54. Here, we report a robust study that differs from the central results of the previous report and reveals that under laboratory conditions, that PoFUT2 is not essential for murine parasite development and transmission.

In this study also a P. falciparum mutant that lacks expression of PoFUT2. This mutant shows normal oocyst and sporozoite production in An. gambiae

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