| 2005 |
TgHsp90 transcript and protein levels increase under stress or bradyzoite differentiation conditions. Fluorescence microscopy revealed that Hsp90 is cytosolic in tachyzoites but present in both nucleus and cytosol in mature bradyzoites, indicating developmentally regulated subcellular redistribution. Geldanamycin (a benzoquinone ansamycin that binds and disrupts Hsp90 function) blocked conversion both from tachyzoite to bradyzoite and bradyzoite to tachyzoite stages, establishing an essential role for Hsp90 in stage interconversion. |
Fluorescence microscopy, Western blot, geldanamycin pharmacological inhibition in RH ΔUPRT and ME49/PK strains |
Journal of molecular biology |
Medium |
15967463
|
| 2003 |
TgHsp90 (82 kDa) is a cytoplasmic protein secreted from extracellular tachyzoites but not released into the parasitophorous vacuole after invasion. Geldanamycin treatment did not affect TgHsp90 secretion from extracellular tachyzoites but significantly disturbed host cell entry and intracellular parasite growth, indicating TgHsp90 function is required for invasion and intracellular replication. |
Monoclonal antibody characterization, cDNA cloning and sequencing, geldanamycin pharmacological inhibition, invasion and growth assays |
Biochemical and biophysical research communications |
Medium |
14623321
|
| 2017 |
Genetic knockout of TgHsp90 (ΔHsp90) resulted in defective host-cell invasion, failure to proliferate in vitro in Vero cells, and loss of long-term survival in mice in vivo. These defects were rescued by complementation with TgHsp90, establishing that TgHsp90 is essential for invasion, replication, and parasite viability in vivo. |
Gene knockout (ΔHsp90), complementation strain, in vitro invasion and proliferation assays, mouse survival model |
Parasite (Paris, France) |
High |
28627357
|
| 2011 |
TgSis1 (a Hsp40/J-domain protein) co-immunoprecipitated with both TgHsp70 and TgHsp90, indicating that TgHsp90 participates in a cytosolic chaperone complex with TgHsp70 and TgSis1. |
Co-immunoprecipitation, immunofluorescence localization |
International journal of biological macromolecules |
Medium |
22209934
|
| 2014 |
TgUNC (a UCS-family myosin co-chaperone) enables functional expression of TgMyoA (class XIVa myosin) in Sf9 cells; its tetratricopeptide repeat (TPR) domain was not essential for obtaining functional myosin, implying alternative mechanisms exist for Hsp90 recruitment to TgMyoA during folding. |
Baculovirus/Sf9 heterologous expression, co-expression with TgUNC, in vitro actin motility assay, domain deletion analysis |
The Journal of biological chemistry |
Medium |
25231988
|
| 1998 |
Quercetin, a bioflavonoid that inhibits synthesis of Hsp90, Hsp70, and Hsp27, suppresses induction of bradyzoite development in vitro, implicating heat shock proteins including Hsp90 in the process of bradyzoite differentiation. |
Quercetin pharmacological inhibition, immunofluorescence with bradyzoite-specific antibodies, Western blot, RT-PCR |
Infection and immunity |
Low |
9632598
|
| 2024 |
Following bag1 (HSP30) knockout in ME49, transcription of HSP90 (along with HSP20, HSP21, HSP40, HSP60, HSP70, and BFD1) was significantly upregulated, indicating that TgHsp90 participates in a compensatory stress-response network that partially rescues bradyzoite differentiation in the absence of BAG1. |
Gene knockout (ME49Δbag1), qPCR for HSP family transcript levels, Western blot, cyst formation assay |
Parasites & vectors |
Low |
39080770
|
| 2026 |
In a murine ocular toxoplasmosis model, HDAC6 inhibition by Tubastatin A regulated the HDAC6-Hsp90 pathway, leading to decreased VEGF and HSF1 expression. This places TgHsp90 (or the host Hsp90 pathway) downstream of HDAC6 in the context of retinal infection pathology. |
Intravitreal injection of Tubastatin A (HDAC6 inhibitor), immunofluorescence, cytokine measurement, histopathology in murine OT model |
ACS infectious diseases |
Low |
41533437
|