Molecular Architecture of the Retroviral Capsid

Trends Biochem Sci. 2016 May;41(5):410-420. doi: 10.1016/j.tibs.2016.02.009. Epub 2016 Mar 30.

Abstract

Retroviral capsid cores are proteinaceous containers that self-assemble to encase the viral genome and a handful of proteins that promote infection. Their function is to protect and aid in the delivery of viral genes to the nucleus of the host, and, in many cases, infection pathways are influenced by capsid-cellular interactions. From a mathematical perspective, capsid cores are polyhedral cages and, as such, follow well-defined geometric rules. However, marked morphological differences in shapes exist, depending on virus type. Given the specific roles of capsid in the viral life cycle, the availability of detailed molecular structures, particularly at assembly interfaces, opens novel avenues for targeted drug development against these pathogens. Here, we summarize recent advances in the structure and understanding of retroviral capsid, with particular emphasis on assemblies and the capsid cores.

Publication types

  • Review
  • Research Support, N.I.H., Extramural

MeSH terms

  • Binding Sites
  • Capsid / chemistry
  • Capsid / physiology
  • Capsid / ultrastructure*
  • Capsid Proteins / chemistry*
  • Capsid Proteins / metabolism
  • Crystallography, X-Ray
  • HIV-1 / chemistry
  • HIV-1 / physiology
  • HIV-1 / ultrastructure*
  • Leukemia Virus, Bovine / chemistry
  • Leukemia Virus, Bovine / physiology
  • Leukemia Virus, Bovine / ultrastructure*
  • Models, Molecular
  • Protein Binding
  • Protein Conformation, alpha-Helical
  • Protein Conformation, beta-Strand
  • Protein Interaction Domains and Motifs
  • Protein Multimerization
  • Protein Structure, Tertiary
  • Rous sarcoma virus / chemistry
  • Rous sarcoma virus / physiology
  • Rous sarcoma virus / ultrastructure*
  • Virion / chemistry
  • Virion / physiology
  • Virion / ultrastructure*
  • Virus Assembly

Substances

  • Capsid Proteins