Abstract
Retrovirus morphogenesis entails assembly of Gag proteins and the viral genome on the host plasma membrane, acquisition of the viral membrane and envelope proteins through budding, and formation of the core through the maturation process. Although in both immature and mature retroviruses, Gag and capsid proteins are organized as paracrystalline structures, the curvatures of these protein arrays are evidently not uniform within one or among all virus particles. The heterogeneity of retroviruses poses significant challenges to studying the protein contacts within the Gag and capsid lattices. This review focuses on current understanding of the molecular organization of retroviruses derived from the sub-nanometer structures of immature virus particles, helical capsid protein assemblies and soluble envelope protein complexes. These studies provide insight into the molecular elements that maintain the stability, flexibility and infectivity of virus particles. Also reviewed are morphological studies of retrovirus budding, maturation, infection and cell-cell transmission, which inform the structural transformation of the viruses and the cells during infection and viral transmission, and lead to better understanding of the interplay between the functioning viral proteins and the host cell.
Original language | English (US) |
---|---|
Pages (from-to) | 343-369 |
Number of pages | 27 |
Journal | AIMS Biophysics |
Volume | 2 |
Issue number | 3 |
DOIs | |
State | Published - 2015 |
Bibliographical note
Publisher Copyright:© 2015, Wei Zhang, et al.
Keywords
- Capsid protein shell
- Cryo-electron microscopy
- Cryo-electron tomography
- Envelop protein complex
- Gag lattice
- Retrovirus structure
- Sub-tomogram averaging