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Reovirus protein ?1: From cell attachment to protein oligomerization and folding mechanisms
- Source :
- BioEssays. 16:199-206
- Publication Year :
- 1994
- Publisher :
- Wiley, 1994.
-
Abstract
- The reovirus cell attachment protein sigma 1 is a lollipop-shaped structure with the fibrous tail anchored to the virion. Since it interacts with the cell receptor, sigma 1 is a major determinant of reovirus infectivity and tissue tropism. Studies on its structure-function relationships have been facilitated by the fact that protein sigma 1 produced in any expression system is capable of binding to cell receptors. The use of site-specific and deletion mutants has led to the identification and characterization of its virion anchorage and receptor binding domains. Studies on the oligomeric status of sigma 1 have revealed that sigma 1 is a homotrimer and that two independent trimerization events at different loci (the N- and C-terminal halves, respectively) of the protein, are involved in its generation. This also accounts for a clearly demonstrable dominant negative effect by a mutant subunit in a wild-type/mutant sigma 1 heterotrimer. Current efforts are focused on the involvement of chaperones in the generation of sigma 1 and on events that take place upon sigma 1 binding to the cell receptor. Protein sigma 1 has therefore become an excellent model system for the study of both virus attachment and protein oligomerization and folding mechanisms.
- Subjects :
- Protein Folding
Macromolecular Substances
Protein subunit
Mutant
Cell
Biology
Reoviridae
General Biochemistry, Genetics and Molecular Biology
Viral Proteins
medicine
Animals
Humans
Protein oligomerization
Receptor
Cell Membrane
fungi
Virion
Sigma
Molecular biology
Cell biology
Models, Structural
medicine.anatomical_structure
Tissue tropism
Receptors, Virus
Capsid Proteins
Protein folding
Subjects
Details
- ISSN :
- 15211878 and 02659247
- Volume :
- 16
- Database :
- OpenAIRE
- Journal :
- BioEssays
- Accession number :
- edsair.doi.dedup.....94a501ef42d5b0ed96142c1b96e912ff