Vern B. Carruthers

The paper analyzes lipid asymmetry in parasitophorous vacuole membranes of Toxoplasma gondii and Plasmodium falciparum, finding symmetric distribution of key lipids unlike host cell membranes.

This paper determines the structure of Toxoplasma gondii ribosomes bound to mRNA and tRNA, revealing how emetine inhibits translation by disrupting mRNA translocation.

This paper identifies TgGRA8 as a Toxoplasma protein that recruits ALG-2 to the parasitophorous vacuole, essential for parasite metabolism and ESCRT hijacking.

This paper identifies TgATG2 as a key component of the Toxoplasma gondii autophagy machinery required for bradyzoite survival and cyst persistence.

The paper identifies EAF1 as a Toxoplasma gondii effector that modulates ESCRT subversion using a pooled image-based CRISPR screening framework called spaCR.

The paper identifies MIC11 as an essential gene for Toxoplasma gondii egress, showing it interacts with PLP1 to disrupt host cell membranes.

This study investigates the role of equilibrative nucleoside transporters in Toxoplasma gondii, showing that TgENT1 is critical for bradyzoite differentiation and identifying it as a therapeutic target.

This study investigates the role of the ingestion pathway in Toxoplasma gondii nutrient acquisition by analyzing mutants lacking key pathway components, revealing reliance on biosynthetic pathways and highlighting the pathway's role in nutrient scarcity.

This study identifies TgPROP1 as essential for autophagy and chronic infection of Toxoplasma gondii bradyzoites, while TgPROP2 is not involved in bradyzoite autophagy.

This study uses the AsGM1 membrane lipid signature to distinguish NK cells and ILC1s, capturing their plasticity across tissues and conditions.

This study identifies TgATG9 as essential for autophagosome formation and chronic Toxoplasma gondii infection.

This study identifies eIF1.2 as a regulator of Toxoplasma gondii differentiation by controlling the translation of key bradyzoite factors.

This study identifies TgAAT1, a putative arginine transporter in Toxoplasma gondii, which localizes to the PLVAC and is essential for extracellular survival and bradyzoite differentiation.

This study shows that O-glycosylation of MIC2 by TgPOFUT2 is not essential for Toxoplasma gondii tachyzoite infectivity and plaque formation.