» Articles » PMID: 7494347

Association of Reovirus Outer Capsid Proteins Sigma 3 and Mu 1 Causes a Conformational Change That Renders Sigma 3 Protease Sensitive

Overview
Journal J Virol
Date 1995 Dec 1
PMID 7494347
Citations 17
Authors
Affiliations
Soon will be listed here.
Abstract

Association of the reovirus proteins sigma 3 and mu 1 influences viral entry, initiation of outer capsid assembly, and modulation of the effect of sigma 3 on cellular translation. In this study, we have addressed whether structural changes occur in sigma 3 as a result of its interaction with mu 1. Using differences in protease sensitivity to detect conformationally distinct forms of sigma 3, we showed that association of sigma 3 with mu 1 caused a conformational change in sigma 3 that converted it from a protease-resistant to a protease-sensitive structure and occurred posttranslationally. The effect of mu 1 on the structure of sigma 3 was stoichiometric. Our results are consistent with a model in which sigma 3's association with mu 1 shifts its function from translational control to assembly of an outer capsid in which sigma 3 is folded into the protease-sensitive conformation that is required for its cleavage during the next round of infection.

Citing Articles

Strain-specific differences in reovirus infection of murine macrophages segregate with polymorphisms in viral outer-capsid protein σ3.

Fiske K, Brigleb P, Sanchez L, Hinterleitner R, Taylor G, Dermody T J Virol. 2024; 98(11):e0114724.

PMID: 39431846 PMC: 11575339. DOI: 10.1128/jvi.01147-24.


Reovirus uses temporospatial compartmentalization to orchestrate core versus outercapsid assembly.

Kniert J, Dos Santos T, Eaton H, Cho W, Plummer G, Shmulevitz M PLoS Pathog. 2022; 18(9):e1010641.

PMID: 36099325 PMC: 9514668. DOI: 10.1371/journal.ppat.1010641.


Reovirus σ3 Protein Limits Interferon Expression and Cell Death Induction.

Roebke K, Guo Y, Parker J, Danthi P J Virol. 2020; 94(22).

PMID: 32847863 PMC: 7592210. DOI: 10.1128/JVI.01485-20.


Cell Entry-Independent Role for the Reovirus μ1 Protein in Regulating Necroptosis and the Accumulation of Viral Gene Products.

Roebke K, Danthi P J Virol. 2019; 93(11).

PMID: 30894465 PMC: 6532083. DOI: 10.1128/JVI.00199-19.


Potential for Improving Potency and Specificity of Reovirus Oncolysis with Next-Generation Reovirus Variants.

Mohamed A, Johnston R, Shmulevitz M Viruses. 2015; 7(12):6251-78.

PMID: 26633466 PMC: 4690860. DOI: 10.3390/v7122936.


References
1.
Smith R, Zweerink H, Joklik W . Polypeptide components of virions, top component and cores of reovirus type 3. Virology. 1969; 39(4):791-810. DOI: 10.1016/0042-6822(69)90017-8. View

2.
Kedl R, Schmechel S, Schiff L . Comparative sequence analysis of the reovirus S4 genes from 13 serotype 1 and serotype 3 field isolates. J Virol. 1995; 69(1):552-9. PMC: 188609. DOI: 10.1128/JVI.69.1.552-559.1995. View

3.
Laemmli U . Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970; 227(5259):680-5. DOI: 10.1038/227680a0. View

4.
Fields B, Raine C, Baum S . Temperature-sensitive mutants of reovirus type 3: defects in viral maturation as studied by immunofluorescence and electron microscopy. Virology. 1971; 43(3):569-78. DOI: 10.1016/0042-6822(71)90282-0. View

5.
Chang C, Zweerink H . Fate of parental reovirus in infected cell. Virology. 1971; 46(3):544-55. DOI: 10.1016/0042-6822(71)90058-4. View