Mutant/mutation
The mutant lacks expression of GPI16

Protein (function)
Glycosylphosphatidylinositols (GPIs) and GPI anchors are transported to the cell surface via a process called GPI transamidation, which involves the GPI transamidase (GPI-T) complex. Before GPIs and GPI anchors are transported to the cell surface, the GPI attachment signal peptide is replaced by a preassembled GPI in the endoplasmic reticulum through a transamidation reaction that results in the formation of a carbonyl intermediate. The GPI transamidase is a key enzyme of this posttranslational modification. The GPI transamidase complex consists of five different subunits and is conserved among different species. In this study, we characterized the GPI transamidase subunit16 (Gpi16)  (PBANKA_0926200) homolog in P. berghei (PbGPI16), a highly conserved GPI-T subunit among Plasmodium species.

Phenotype
C57Bl6 mice were infected with Δpbgpi16 and wild type (WT) PbA. In both groups parasitemia rose steadily after infection and did not show statistically significant difference by day 7 (P > 0.05, two-way ANOVA), albeit the day 7 parasitemia in the WT-infected group (7.4%) was higher than that in the Δpbgpi6-infected mice (6.0%).
Reduced mortality due to complications of ECM in Δpbgpi16 infected mice.

Additional information
Evidence is presented that:
- total GPIs in blood stages of Δpbgpi16 were slightly less than in wild type (WT) PbA
- GPIs associated with proteins extracted from merozoite membranes were significantly less in Δpbgpi16 than in WT parasites
- Proteins were analyzed in Western blots using antibodies against PbMSP1, PbMSP4 and PbMSP10, respectively. The results showed that the amounts of all three proteins were significantly reduced in the merozoite membrane of Δpbgpi16 parasites.

Other mutants