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Evidence that the sigma 1 protein of reovirus serotype 3 is a multimer
Journal of Virology
|June 1, 1987
Abstract:
In this report, we study the reovirus serotype 3 (strain Dearing) sigma 1 protein obtained from various sources: from Escherichia coli expressing sigma 1 protein, from reovirus-infected mouse L cells, and from purified reovirions. We demonstrate that the sigma 1 protein is a multimer in its undisrupted form and present biochemical evidence suggesting that the multimer is made up of four sigma 1 subunits.
Insights
This study investigated the reovirus sigma 1 protein, finding it exists as a multimer. Biochemical evidence suggests this multimer is composed of four sigma 1 subunits.
Area of Science:
- Virology
- Molecular Biology
- Protein Chemistry
Background:
- Reovirus serotype 3 (strain Dearing) is a significant viral pathogen.
- The sigma 1 protein is a key viral surface protein involved in cell attachment and entry.
- Understanding the structure of sigma 1 protein is crucial for developing antiviral strategies.
Purpose of the Study:
- To characterize the oligomeric state of the reovirus sigma 1 protein.
- To determine the subunit composition of the sigma 1 protein multimer.
- To investigate the sigma 1 protein from different expression systems.
Main Methods:
- Purification of sigma 1 protein from Escherichia coli and reovirus-infected mouse L cells.
- Isolation of sigma 1 protein from purified reovirions.
- Biochemical assays to analyze protein structure and subunit composition.
Main Results:
- The sigma 1 protein exists as a multimer in its native, undisrupted form.
- Biochemical evidence indicates the multimer is composed of four sigma 1 subunits.
- Consistent multimeric structure observed across different sources of the protein.
Conclusions:
- The reovirus sigma 1 protein forms a stable tetrameric structure.
- This multimeric assembly is fundamental to the protein's function.
- Further studies can explore the functional implications of this tetrameric structure.