Rotavirus genome replication occurs within dynamic cytoplasmic condensates known as viroplasms, yet the molecular mechanisms that organize these compartments remain poorly understood. To explore how these condensates coordinate replication, we present early biochemical, biophysical, and structural insights into the interplay between the viral polymerase VP1, the non-structural protein NSP5, and the viral positive-strand RNA. Interaction assays reveal that VP1 and NSP5 form complexes mediated by the NSP5 C-terminal domain, while biophysical analyses indicate that this interaction is transient and influences VP1–RNA association. These findings suggest that NSP5 may modulate RNA engagement by VP1 or transiently sequester RNA, consistent with the fluid and multivalent behaviour characteristic of viral condensates. Cryo-electron microscopy supports RNA binding by VP1 and indicates largely weak multivalent interactions under conditions mimicking condensate environments. Ongoing hydrogen–deuterium exchange mass spectrometry will help elucidate conformational changes and contact regions within these complexes. Together, these results lay the groundwork for dissecting how multivalency and molecular flexibility among viral proteins and RNA drive genome replication within condensates.