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Use of Viral Entry Assays and Molecular Docking Analysis for the Identification of Antiviral Candidates against Coxsackievirus A16
Published on: July 15, 2019
Interaction of decay-accelerating factor with coxsackievirus B3
Susan Hafenstein1, Valorie D Bowman, Paul R Chipman
1Department of Biological Sciences, Purdue University, 915 W. State Street, West Lafayette, IN 47907-2054, USA.
Journal of Virology
|September 7, 2007
Summary
Many viruses use immunoglobulin (Ig)-like receptors to infect cells. This study reveals how decay-accelerating factor (DAF) binds to coxsackievirus B3, blocking other receptors and highlighting distinct viral evolutionary paths.
Area of Science:
- Virology
- Structural Biology
- Immunology
Background:
- Enteroviruses, rhinoviruses, and parechoviruses commonly utilize immunoglobulin (Ig)-like receptors that bind within viral canyons to initiate infection.
- Some viruses employ alternative receptors that bind outside the viral canyon.
- Coxsackievirus B3 (CVB3) is known to use both the coxsackievirus-adenovirus receptor (CAR) and decay-accelerating factor (DAF) as cellular receptors.
Purpose of the Study:
- To elucidate the structural basis of CVB3 interaction with DAF.
- To understand the competitive binding mechanism between DAF and CAR for CVB3.
- To investigate the evolutionary implications of DAF binding sites across different viruses.
Main Methods:
- Cryoelectron microscopy was used to determine the structure of CVB3 complexed with DAF.
- Analysis of receptor binding sites on the viral surface.
- Comparative analysis of DAF binding sites on CVB3 and echoviruses.
Main Results:
- A cryoelectron microscopy reconstruction revealed DAF binding to all 60 sites on the CVB3 variant.
- DAF binding bridges the viral canyon, sterically hindering the CAR binding site.
- The DAF binding site on CVB3 is distinct from that observed on echoviruses.
Conclusions:
- DAF acts as a receptor for CVB3, competing with CAR for viral binding.
- The distinct DAF binding site on CVB3 suggests independent evolutionary adaptation compared to echoviruses.
- Understanding these receptor interactions provides insights into viral entry mechanisms and evolution.
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