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Use of Viral Entry Assays and Molecular Docking Analysis for the Identification of Antiviral Candidates against Coxsackievirus A16
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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
PubMed

Insights

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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