Viruses clearly rely on the host biomachinery for their essential viral processes. Their functional versatility lies in their ability to acquire complex, multifunctional, three-dimensional, structured RNAs to molecularly hijack host proteins. However, their mechanisms can be obscured by the difficulty of solving conformationally dynamic RNA structures. Hence, designing effective strategies to uncover the novel structure-function rules of viral RNAs and their close interactions with host machinery has gained much attention recently.

In a breakthrough study published recently in Science, researchers from the University of Colorado Anschutz Medical campus have revealed how viral RNAs use a combination of static and dynamic RNA structures to bind host machinery through highly noncanonical interactions.

Using cryogenic electron microscopy (cryo-EM), the investigators have visualized the structure of the mysterious viral transfer RNA (tRNA)-like structure (TLS) from the brome mosaic virus (BMV), which affects essential viral processes, including viral replication, translation, and genome encapsidation.