Analysis of the interactome of the Toxoplasma gondii TgJ1 HSP40 chaperone

JONATHAN MUNERA LOPEZ; ANDRES MARIANO ALONSO; MARIA JULIA FIGUERAS LOPEZ; ANA M. SALDARRIAGA CARTAGENA; MIRYAM A. HORTUA TRIANA; LUIS DIAMBRA; LAURA VANAGAS; BING DENG; SILVIA J. MORENO; SERGIO O. ANGEL

Proteomes

MDPI

Año: 2023

2227-7382

Toxoplasmagondiiis an obligate intracellular apicomplexan that causes toxoplasmosis in humansand animals. Central to its dissemination and pathogenicity is the ability to rapidlydivide in the tachyzoite stage and infect any type of nucleated cell.Adaptation to different cell contexts requires high plasticity in which heatshock proteins (Hsps) could play a fundamental role. Tgj1 is a type I Hsp40 of T. gondii, an ortholog of the DNAJA1group, which is essential during the tachyzoite lytic cycle. Tgj1 consists of aJ-domain, ZFD, and DNAJ_C domains with a CRQQ C-terminal motif, which isusually prone to lipidation. Tgj1 presented a mostly cytosolic subcellularlocalization overlapping partially withendoplasmic reticulum. Protein-Protein Interaction (PPI) analysis showed thatTgj1 could be implicated in various biological pathways, mainly translation,protein folding, energy metabolism, membrane transport and protein translocation,invasion/pathogenesis, cell signaling, chromatin and transcription regulationand cell redox homeostasis among others. The combination of Tgj1 and Hsp90 PPIsretrieved only 70 interactors linked to the Tgj1-Hsp90 axis, suggesting thatTgj1 would present specific functions in addition to those of the Hsp70/Hsp90cycle, standing out invasion/pathogenesis, cell shape motility and energypathway. Within the Hsp70/Hsp90 cycle, translation-associated pathways, cellredox homeostasis and protein folding were highly enriched in the Tgj1-Hsp90axis. In conclusion, Tgj1 would interact with a wide range of proteins fromdifferent biological pathways, which could suggest a relevant role in them.