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Structural analysis of the mechanism of adenovirus binding to its human cellular receptor, CAR
M C Bewley1, K Springer, Y B Zhang
1Biology Department, Brookhaven National Laboratory, Upton, NY 11973, USA.
Abstract:
Binding of virus particles to specific host cell surface receptors is known to be an obligatory step in infection even though the molecular basis for these interactions is not well characterized. The crystal structure of the adenovirus fiber knob domain in complex with domain I of its human cellular receptor, coxsackie and adenovirus receptor (CAR), is presented here. Surface-exposed loops on knob contact one face of CAR, forming a high-affinity complex. Topology mismatches between interacting surfaces create interfacial solvent-filled cavities and channels that may be targets for antiviral drug therapy. The structure identifies key determinants of binding specificity, which may suggest ways to modify the tropism of adenovirus-based gene therapy vectors.
Insights
The crystal structure reveals how adenovirus fiber knob binds to the coxsackie and adenovirus receptor (CAR), identifying potential targets for antiviral drugs and gene therapy vector modification.
Area of Science:
- Structural biology
- Virology
- Molecular interactions
Background:
- Virus-host cell binding is crucial for infection but poorly understood.
- Adenovirus uses its fiber knob domain to attach to host cells.
Purpose of the Study:
- To determine the molecular basis of adenovirus fiber knob binding to its human receptor, CAR.
- To identify potential targets for antiviral therapies and gene therapy vector development.
Main Methods:
- X-ray crystallography was used to obtain the structure of the adenovirus fiber knob domain in complex with CAR domain I.
Main Results:
- The crystal structure reveals high-affinity binding mediated by surface-exposed loops on the knob contacting CAR.
- Topology mismatches create cavities and channels at the interface, suggesting potential drug targets.
- Key determinants of binding specificity were identified.
Conclusions:
- The determined structure provides critical insights into adenovirus-CAR interactions.
- Findings may guide the development of novel antiviral strategies and the engineering of adenovirus gene therapy vectors with altered tropism.
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