Rotavirus proteins: structure and assembly

Curr Top Microbiol Immunol. 2006:309:189-219. doi: 10.1007/3-540-30773-7_7.

Abstract

Rotavirus is a major pathogen of infantile gastroenteritis. It is a large and complex virus with a multilayered capsid organization that integrates the determinants of host specificity, cell entry, and the enzymatic functions necessary for endogenous transcription of the genome that consists of 11 dsRNA segments. These segments encode six structural and six nonstructural proteins. In the last few years, there has been substantial progress in our understanding of both the structural and functional aspects of a variety of molecular processes involved in the replication of this virus. Studies leading to this progress using of a variety of structural and biochemical techniques including the recent application of RNA interference technology have uncovered several unique and intriguing features related to viral morphogenesis. This review focuses on our current understanding of the structural basis of the molecular processes that govern the replication of rotavirus.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.
  • Review

MeSH terms

  • Antigens, Viral / chemistry
  • Capsid / chemistry
  • Capsid Proteins / chemistry
  • Genome, Viral
  • Hydrogen-Ion Concentration
  • RNA, Viral / biosynthesis
  • RNA-Binding Proteins / chemistry
  • Reassortant Viruses / chemistry
  • Rotavirus / physiology*
  • Viral Nonstructural Proteins / chemistry
  • Viral Proteins / chemistry*
  • Viral Proteins / physiology
  • Virus Assembly*
  • Virus Replication

Substances

  • Antigens, Viral
  • Capsid Proteins
  • RNA, Viral
  • RNA-Binding Proteins
  • VP4 protein, Rotavirus
  • VP6 protein, Rotavirus
  • VP7 protein, Rotavirus
  • Viral Nonstructural Proteins
  • Viral Proteins
  • NS35 protein, rotavirus