Myristoylation of a secreted protein, identified in a global myristoylation analysis of the eukaryotic parasite Toxoplasma gondii, is important for host cell invasion.

Partially overlapping functions of a limited subset of actin binding proteins allow the parasite Toxoplasma gondii to achieve actin regulation required for complex cellular processes.

Single-cell RNA-sequencing resolves the transcriptional landscape of asexual development in Toxoplasma gondii, revealing concerted genetic programs to Plasmodiumfalciparum and a novel transcriptional factor that controls antigen switching.

A derived stress response trait may have contributed to the emergence of a globally dominant and promiscuous parasite.

The Toxoplasma parasite requires an enzyme called ASP5 to cleave proteins for export into host cells.

Overexpression of interferon-stimulated genes revealed a role for RARRES3 in restricting growth of Toxoplasma gondii by inducing early egress from human cells.

Multi-level profiling of Toxoplasma gondii-injected neurons identifies brain regions and neuron subtype predilections as well as the effect of Toxoplasma interactions on neuron physiology and health.

Apicomplexan parasites secrete proteins to manipulate their hosts from sub-apical openings in their cell pellicle that are distinct from the apical complex from where invasion factors are secreted.

An aspartyl protease is essential for the lytic cycle of Toxoplasma gondii and is involved in the maturation of proteins critical for invasion and egress, and it can be targeted selectively with an ethylamine scaffold based peptidomimetic inhibitor.

Genetic and proteomic analyses reveal that the SPARK kinase, which is a regulator of key life-cycle transitions in the parasite Toxoplasma gondii, complexes with an elongin-like protein to regulate several important AGC-family kinases.