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Published on: May 29, 2012
Isolation of a receptor protein involved in attachment of human rhinoviruses
Abstract:
Human rhinoviruses can be classified into major and minor groups on the basis of receptor specificity. Recently, a mouse monoclonal antibody was isolated which selectively blocked the attachment of the major group of human rhinoviruses to cells. Using this monoclonal antibody, the cellular receptor for the major group of human rhinoviruses was isolated. A radioimmunoassay was developed by using the receptor antibody to specifically detect rhinovirus receptor during isolation. Solubilized receptor from detergent-treated HeLa cell membrane extracts eluted from gel filtration columns with an apparent molecular weight of 440,000. A cellular receptor protein, which had a molecular weight of 90,000 when analyzed on sodium dodecyl sulfate-polyacrylamide gels, was purified from solubilized extracts on an immunoaffinity column containing receptor antibody. Polyclonal rabbit antiserum, resulting from immunization with the isolated receptor protein, specifically blocked the attachment of the major group of human rhinoviruses and indicated that the 90-kilodalton protein plays a functional role in attachment. Prolonged exposure of HeLa cell monolayers with the receptor antibody showed no inhibition of cell growth and division.
Insights
Researchers identified the cellular receptor for major group human rhinoviruses using a specific monoclonal antibody. This 90-kilodalton protein is crucial for rhinovirus attachment to cells.
Area of Science:
- Virology
- Cell Biology
- Immunology
Background:
- Human rhinoviruses are classified into major and minor groups based on receptor usage.
- A specific monoclonal antibody was developed that blocks major group rhinovirus attachment.
Purpose of the Study:
- To isolate and characterize the cellular receptor for major group human rhinoviruses.
- To confirm the functional role of the isolated receptor in viral attachment.
Main Methods:
- Utilized a monoclonal antibody to isolate the cellular receptor.
- Developed a radioimmunoassay for receptor detection during purification.
- Purified the receptor protein using immunoaffinity chromatography.
- Analyzed protein molecular weight via SDS-PAGE and gel filtration.
Main Results:
- Isolated a solubilized receptor with an apparent molecular weight of 440,000 Da.
- Purified a 90,000 Da receptor protein.
- Antiserum against the purified protein blocked major group rhinovirus attachment.
- The 90 kDa protein plays a functional role in viral attachment.
Conclusions:
- The 90 kDa protein is the cellular receptor for major group human rhinoviruses.
- This receptor is essential for viral entry and can be targeted for therapeutic intervention.
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