Interactions among capsid proteins orchestrate rotavirus particle functions

Rotaviruses are members of the Reoviridae family of non-enveloped viruses and important etiologic agents of acute gastroenteritis in infants and young children. In recent years, high-resolution structures of triple-layered rotavirus virions and the constituent proteins have provided valuable insights into functions. Of note, structural studies have revealed the position of the viral RNA-dependent RNA polymerase, VP1, within the inner capsid, which in turn provides clues about the location of the viral capping machinery and the route of viral transcript egress. Mechanisms by which the viral spike protein, VP4, mediates receptor binding and membrane penetration have also been aided by high-resolution structural studies. Future work may serve to fill the remaining gaps in understanding of rotavirus particle structure and function.

► Structures of rotavirus have greatly informed studies of replication and entry. ► The Reoviridae may have a conserved capsid–polymerase interaction mechanism. ► The rotavirus polymerase orientation suggests the location of the capping enzyme. ► The conformation of the rotavirus spike is regulated by the outer capsid protein. ► New methods are needed to study the rotavirus spike precursor and capping enzyme.