Assembly of the reovirus outer capsid requires μ1/σ3 interactions which are prevented by misfolded σ3 protein in temperature-sensitive mutant tsG453
| Autor: | Kevin M. Coombs, Molly Shing |
|---|---|
| Rok vydání: | 1996 |
| Předmět: |
Protein Folding
Cancer Research Genes Viral Protein Conformation medicine.drug_class viruses Mutant Biology Reoviridae Monoclonal antibody Viral Proteins Capsid Virology medicine Outer capsid Virus Assembly Capsomere Temperature RNA-Binding Proteins Temperature-sensitive mutant Molecular biology Infectious Diseases Mutation Biophysics Capsid Proteins |
| Zdroj: | Virus Research. 46:19-29 |
| ISSN: | 0168-1702 |
| DOI: | 10.1016/s0168-1702(96)01372-x |
| Popis: | A temperature-sensitive reovirus mutant, tsG453, whose defect was mapped to major outer capsid protein sigma 3, makes core particles but fails to assemble the outer capsid around the core at non-permissive temperature. Previous studies that made use of electron cryo-microscopy and image reconstructions showed that mu 1, the other major outer capsid protein, but not sigma 3, interact extensively with the core capsid. Although wild-type sigma 3 and mu 1 interact with each other, immunocoprecipitation studies showed that mutant sigma 3 protein was incapable of interacting with mu 1 at the non-permissive temperature. In addition, restrictively-grown mutant sigma 3 protein could not be precipitated by some sigma 3-specific monoclonal antibodies. These observations suggest that in a wild-type infection, specific sigma 3 and mu 1 interactions result in changes in mu 1 conformation which are required to allow mu 1/sigma 3 complexes to condense onto the core capsid shell during outer capsid assembly, and that sigma 3 in non-permissive tsG453 infections is misfolded such that it cannot interact with mu 1. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|
Full Text from ScienceDirect