Mutant/mutation
The mutant expresses a C-terminal cMyc(4x)-tagged version of PDEγ

Protein (function)
The cyclic nucleotides cAMP and cyclic GMP (cGMP) function as signaling second messengers downstream of surface receptor-ligand interactions by activating cAMP-dependent protein kinase (PKA) and cGMP-dependent protein kinase (PKG), respectively. Signaling through cAMP and cGMP is regulated by phosphodiesterases (PDEs), metal ion-dependent enzymes that hydrolyze the 3"-phosphoester bond of cAMP and cGMP. The Plasmodium genome encodes four PDEs (α, β, γ, and δ).
PDEγ is predicted to be a 782-amino-acid type II membrane protein with six transmembrane domains. A search for the presence of domains using the PDE sequence on Prosite (http://prosite.expasy.org/) predicted the protein to possess the conserved catalytic domain amino acid signature H-D-I-g-H-f-G-r-t-N-m-F for PDEs.

Phenotype analyses of a mutant lacking expression of PDEγ (RMgm-1231) indicate an essential role for sporozoite motility (and invasion of salivary glands). Blood stages of the mutant show a slightly reduced growth rate.

Phenotype
Phenotype analyses of a mutant lacking expression of PDEγ (RMgm-1231) indicate an essential role for sporozoite motility (and invasion of salivary glands). Blood stages of the mutant show a slightly reduced growth rate.

Immunofluorescence analysys of the mutant expressing c-Myc tagged PDEγ showed PDEγ expression to be low in blood stages  and high in salivary gland sporozoites. The expression in blood stages appeared internal and partially colocalized with the endoplasmic reticulum (ER) marker BiP. The protein also displayed an intracellular localization in sporozoites and high in salivary gland sporozoites. The expression in BS appeared internal and partially colocalized with the endoplasmic reticulum (ER) marker BiP. The protein also displayed an intracellular localization in sporozoites.

Additional information

Other mutants
A mutant lacking expression of PDEγ (RMgm-1231)