Mutant/mutation
The mutant expresses a C-terminal 3xHA-tagged version of Scd.

Protein (function)
The malaria parasite can modify fatty acids, and stearoyl-CoA Δ9-desaturase (Scd) is an enzyme that catalyzes the synthesis of oleic acid by desaturation of stearic acid. Plasmodium parasites can modify de novo synthesized or scavenged fatty acids into long unsaturated fatty acids. An endoplasmic reticulum (ER)-localized stearoyl-CoA desaturase (Scd) was identified in P. falciparum that catalyzes the formation of oleic acid from stearic acid by the insertion of a cis double bond at the Δ9 position of fatty acyl-CoAs.

Phenotype
Analysis of a mutant expressing a C-terminal 3xHA tagged version of Scd showed the following: Scd was expressed in the blood stage and post 48 h in the liver stage. P. berghei Scd primarily colocalized to the ER in asexual blood stages and partially during liver stages.

Analysis of a mutant lacking expression of Scd (RMgm-5550) showed the following:
Scd KO liver stages grow normally but do not form hepatic merozoites. There was abnormal DNA segregation in Scd KO parasites and merozoite formation was abolished.

Additional information

Other mutants