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.
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.