The convergent evolution of unusually strict substrate specificity in apicomplexan LDHs arose by classic neofunctionalization of a duplicated MDH gene via few mutations of large effect.

Analysis of chromerid algal genomes reveals how apicomplexans have evolved from free-living algae into successful eukaryotic parasites via massive losses and re-inventing functional roles of genes.

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.

A versatile acetylation-methylation switch at lysine 31 on the lateral surface of histone H4 contributes to chromatin structure in apicomplexan parasites.

Intracellular amastigotes of the Chagas disease agent Trypanosoma cruzi can spontaneously enter an extended state of replicative dormancy, during which time they are resistant to drug treatment both in vitro and in vivo.

A phylum-specific ATP synthase subunit is needed for proper mitochondrial function and stability of the complex in Toxoplasma gondii.

The proteins found in the mitochondria of apicomplexan parasites, including key proteins involved in energy generation, are very different from mitochondrial proteins of the animals these parasites infect.

Toxoplasma gondii formins have several non-overlapping roles including generating an apico-basal flux of F-actin that is controlled by phosphorylation and methylation and is essential for motility.

Apicomplexan-like parasites originated several times independently and many of them contain cryptic plastid organelles, which demonstrate that the parasites evolved from photosynthetic algae.

Among children in low-resource settings, diverse enteropathogens share common, population-level antibody dynamics, which creates a new opportunity to estimate transmission through serologic surveillance.