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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 echovirus 7.

Pavel Plevka1, Susan Hafenstein, Katherine G Harris

  • 1Department of Biological Sciences, Purdue University, 915 W. State Street, West Lafayette, IN 47907-2054, USA.

Journal of Virology
|October 1, 2010
PubMed
Summary

Echovirus 7 uses Decay-accelerating factor (DAF) as a cellular receptor, binding outside the viral canyon. This binding site differs from other enteroviruses, suggesting unique evolutionary adaptations for Echovirus 7 infection.

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Dissecting Host-virus Interaction in Lytic Replication of a Model Herpesvirus
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Published on: October 7, 2011

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Dissecting Host-virus Interaction in Lytic Replication of a Model Herpesvirus
11:28

Dissecting Host-virus Interaction in Lytic Replication of a Model Herpesvirus

Published on: October 7, 2011

Area of Science:

  • Virology
  • Structural Biology
  • Molecular Biology

Background:

  • Echovirus 7 (EV7) is an enterovirus within the Picornaviridae family.
  • Many picornaviruses utilize IgG-like receptors binding in the viral canyon for uncoating.
  • Some enteroviruses employ alternative receptors binding outside the canyon.

Purpose of the Study:

  • To investigate the interaction between Echovirus 7 and its cellular receptor, Decay-accelerating factor (DAF).
  • To determine the structural basis of DAF binding to Echovirus 7.
  • To understand the evolutionary implications of DAF as an accessory receptor for enteroviruses.

Main Methods:

  • X-ray crystallography was used to determine the structure of Echovirus 7 at 3.1-Å resolution.
  • Cryo-electron microscopy was employed to visualize the Echovirus 7-DAF complex at 7.2-Å resolution.
  • Structural analysis was performed to identify the DAF binding site on Echovirus 7.

Main Results:

  • Decay-accelerating factor (DAF) was identified as a cellular receptor for Echovirus 7.
  • The DAF binding site on Echovirus 7 is located near a 2-fold icosahedral symmetry axis.
  • This binding site differs from that observed for DAF on coxsackievirus B3.

Conclusions:

  • Echovirus 7 utilizes DAF as an accessory receptor, binding outside the viral canyon.
  • The distinct DAF binding site suggests independent evolutionary selection for DAF recognition in enteroviruses.
  • Recognition of DAF likely confers an advantage during the initial stages of Echovirus 7 infection.