| Protein (localization) |
Phosphorylation status in infected cells |
Functional category |
| Caldesmon |
Unphosphorylated |
Mitosis |
| Calreticulin |
Unphosphorylated |
Protein folding |
| Nucleobindin |
Unphosphorylated |
Protein fate |
| Protein disulphide isomerase |
Unphosphorylated |
Structural |
| Thyroid hormone binding protein |
Unphosphorylated |
Signal transduction/cellular communication |
| Chaperonin HSP60 (mitochondria) |
Phosphorylated |
Energy metabolism |
| Lamin A protein (mitochondria) |
Phosphorylated |
Unknown |
| Vimentin (mitochondria) |
Phosphorylated |
Structural |
T. gondii kinase activity is involved in phosphorylation of host IκBα and this unusual
mechanism can be utilized in manipulating the NF-κB pathway [415]. Moreover, a
novel parasite kinase activity at the T. gondii parasitophorus vacuole membrane is
also capable of phosphorylating host IκB [416]. There is biochemical evidence for
the presence of an oxidative phosphorylation and functional respiratory chain in
the mitochondrion of tachyzoites [417]. Recently, cAMP dependent protein kinase
important for the tachyzoite growth was identified in the parasite [95], and protein
phosphorylation is a key event in the process of T. gondii-host cell interaction [418].
Changes in the proteomes of human foreskin fibroblasts following infection with T.
gondii included, e.g. protein kinase C (delta binding protein) (modulated),protein
kinase NYD-Sp9 (↑, up-regulated in expression), protein serine/threonine kinase
(↓,down-regulated),glutathione synthetase (↑), glutathione-S-transferase chain A
(↓), as well as several enzymes involved in glycolysis (Table 17) [368]. |
