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The structure of human rhinovirus 16
M A Oliveira1, R Zhao, W M Lee
1Department of Biological Sciences, Purdue University, West Lafayette, Indiana 47907.
Structure (London, England : 1993)
|September 15, 1993
Summary
The pocket factor in human rhinovirus (HRV)16 stabilizes the virus during transit. Receptor binding empties the pocket, destabilizing the virus for uncoating and infection.
Area of Science:
- Virology
- Structural Biology
- Drug Discovery
Background:
- Rhinoviruses and polioviruses possess hydrophobic pockets near receptor-binding sites, often containing unknown factors.
- Antiviral compounds can bind to these pockets, displacing factors and inhibiting viral uncoating.
- Human rhinovirus (HRV)14, using ICAM-1, has an empty pocket; antiviral binding deforms it, blocking receptor attachment.
Purpose of the Study:
- To investigate the role of the pocket factor in HRV infectivity.
- To determine the atomic structure of HRV16 and analyze its pocket factor.
- To understand how antiviral compounds interact with HRV pockets and affect receptor binding.
Main Methods:
- X-ray crystallography to determine the atomic resolution structure of HRV16.
- Analysis of electron density within the HRV16 pocket.
- Observation of antiviral compound (WIN 56291) binding to HRV16 and its effect on receptor attachment.
Main Results:
- The structure of HRV16 revealed a pocket containing electron density consistent with a fatty acid (≥8 carbons).
- Unlike HRV14, WIN 56291 binding to HRV16 did not deform the pocket.
- WIN 56291 binding still prevented receptor attachment in HRV16.
Conclusions:
- Receptor binding to HRV16 likely requires a temporarily empty pocket, allowing canyon floor deformation.
- The pocket factor may stabilize the virus during intercellular transit.
- ICAM-1 binding to HRV16 may trap the pocket in an empty state, promoting viral destabilization and uncoating.