Super-resolution microscopy reveals, at nanometric-scale, the highly organized protein structure of viroplasms, the viral factories used by rotavirus to replicate its genome and assemble new viral particles.

A cytorhabdovirus phosphoprotein hijacks host CCR4 to trigger turnover of viral nucleoprotein (N)-bound cellular RNAs, thereby releasing nascent RNA-free N protein molecules to bind viral genomic RNAs for optimal replication.

In rotaviruses, the selective packaging of eleven distinct genomic RNA segments requires virus-encoded protein NSP2 to alter the RNA structures, facilitating their interactions with each other.

Rice dwarf virus Pns11 protein increases rice susceptibility to virus infection by enhancing OsSAMS1 enzymatic activity and ethylene production.

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.

Multiple steps of the atypical cell cycles underlying Plasmodium gametogony are controlled by a divergent cyclin/cyclin-dependent complex.

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

An important rice reovirus hijacks exosomes to traverse the apical plasmalemma into saliva-stored cavities in the salivary glands of insect vectors, facilitating viral horizontal transmission into rice phloem.

In triple-layered rotavirus particles, strong interaction between the external and middle layers provides high mechanical strength for protection tasks, while weaker interaction between the middle and inner layers favors transcription.

The structure, function and mechanism of the malaria vaccine candidate CelTOS reveal a unique pore-forming and membrane-disrupting protein with specificity for the inner leaflet of host and vector cells.