A Plasmodium falciparum C-mannosyltransferase is dispensable for parasite asexual blood stage development.

López-Gutiérrez B1, Cova M1, Izquierdo L1.
Source: Parassitologia
Publication Date: (2019)
Issue: :
Research Area:
Cells used in publication:
Plasmodium falciparum
Species: unicellular
Tissue Origin:
4D-Nucleofector™ X-Unit

Methods: Plasmodium falciparum 3D7 1.2B line  was used for transfection and parasite maintenance. Co-transfection of 2 CRSIRP/Cas9 vector systems into Percoll-purified segmented schizonts by electroporation with the Amaxa 4D system, as previously
described (Moon et al., 2013).


C-mannosylation was recently identified in the thrombospondin-related anonymous protein (TRAP) from Plasmodium falciparum salivary gland sporozoites. A candidate P. falciparum C-mannosyltransferase (PfDPY-19) was demonstrated to modify thrombospondin type 1 repeat (TSR) domains in vitro, exhibiting a different acceptor specificity than their mammalian counterparts. According to the described minimal acceptor of PfDPY19, several TSR domain-containing proteins of P. falciparum could be C-mannosylated in vivo. However, the relevance of this protein modification for the parasite viability remains unknown. In the present study, we used CRISPR/Cas9 technology to generate a PfDPY19 null mutant, demonstrating that this glycosyltransferase is not essential for the asexual blood development of the parasite. PfDPY19 gene disruption was not associated with a growth phenotype, not even under endoplasmic reticulum-stressing conditions that could impair protein folding. The data presented in this work strongly suggest that PfDPY19 is unlikely to play a critical role in the asexual blood stages of the parasite, at least under in vitro conditions.