High-resolution 3D structures reveal the biological functions of reoviruses
- 209 Downloads
Viruses in the family Reoviridae are non-enveloped particles comprising a segmented double-stranded RNA genome surrounded by a two-layered or multi-layered icosahedral protein capsid. These viruses are classified into two sub-families based on their particle structural organization. Recent studies have focused on high-resolution three-dimensional structures of reovirus particles by using cryo-electron microscopy (cryo-EM) to approach the resolutions seen in X-ray crystallographic structures. The results of cryo-EM image reconstructions allow tracing of most of the protein side chains, and thus permit integration of structural and functional information into a coherent mechanism for reovirus assembly and entry.
KeywordsNon-enveloped virus Reoviruses Structural basis Assembly Cell entry
Unable to display preview. Download preview PDF.
- Dryden K A, Wang G, Yeager M, Nibert M L, Coombs K M, Furlong D B, Fields B N, Baker T S. 1993. Early steps in reovirus infection are associated with dramatic changes in supramolecular structure and protein conformation: analysis of virions and subviral particles by cryoelectron microscopy and image reconstruction. J Cell Biol, 122: 1023–1041.PubMedCrossRefGoogle Scholar
- Estes M K, Kapikian A Z. 2007. Rotaviruses. In Fields Virology, Knipe DM, Howley PM (eds) 5th edn, pp 1918–1974. Philadelphia: Lippincott, Williams & Wilkins.Google Scholar
- Makkay A, Noordeloos A A, Mertens P P C, Attoui H, Duncan R, Dermody T S. 2011. Reoviridae. In: Virus Taxonomy (Andrew M.Q. King, Michael J. Adams, Eric B. Carstens, and Elliot J. Lefkowitz, eds.). Oxford: Elsevier, pp. 541–638.Google Scholar
- Odegard, A L, Chandran K, Zhang X, Parker J S, Baker T S, Nibert M L. 2004. Putative autocleavage of outer capsid protein micro1, allowing release of myristoylated peptide micro1N during particle uncoating, is critical for cell entry by reovirus. J Virol, 78: 8732–8745.PubMedCentralPubMedCrossRefGoogle Scholar