Reoviruses: Entry, Assembly and Morphogenesis (Current Topics in Microbiology and Immunology, 309)

Mammalian reovirus had been the major focus for molecular understanding of the Reoviridae and has served as a model system for the other members of the family. Indeed, most of our initial understanding of molecular biology and processes involved in virus replication and pathogenesis for the members of the family was generated from reovirus studies. With this platform two other members of the family causing disease in human and/or animals have gained in prominence and the molecular interactions from a structural level through to host-virus interactions as well as the function of the structural and non-structural proteins in the virus life cycle has been investigated in detail.

This book reviews our current understanding of Reoviridae entry, disassembly/assembly and egress in addition to updating high resolution structures of virus proteins and capsids from three different genera of the family.

Reoviridae family members are large, complex viruses that infect human, animals, plants and insects. They are unique in that they lack lipid envelopes and package their genomes of discrete double-stranded segments of RNA within multi-layered capsids. Lack of a lipid envelope has allowed three-dimensional structures of these large complex viruses to be obtained. The capsids of these viruses undergo cell entry, uncoating, the enzymatic functions necessary for transcription of the genome, and are later involved in egress from host cells. Recent years have seen an increase in our knowledge of the structure of these viruses coupled with substantial progress in unravelling the molecular details of these processes. Intriguingly, despite their diversity in hosts, structures and modes of transmission, striking parallels have emerged in the molecular interactions necessary for the essential processes of virus entry, assembly and release.

This book reviews our current understanding of Reoviridae entry, disassembly/assembly and egress in addition to updating high resolution structures of viral proteins and capsids from three different genera of the family.