Echoviruses and coxsackie B viruses that use human decay-accelerating factor (DAF) as a receptor do not bind the

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Use of Viral Entry Assays and Molecular Docking Analysis for the Identification of Antiviral Candidates against Coxsackievirus A16
06:03

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

Published on: July 15, 2019

O B Spiller1, I G Goodfellow, D J Evans

  • 1Complement Biology Group, Dept. of Medical Biochemistry, University of Wales College of Medicine, Heath Park, Cardiff, CF4 4XX, United Kingdom. SpillerB@cardiff.ac.uk

The Journal of Infectious Diseases
|December 23, 1999
PubMed

Insights

Echoviruses and Coxsackie B viruses infect humans by binding to decay-accelerating factor (DAF). These viruses do not bind to rodent DAF, indicating species-specific viral entry mechanisms.

Area of Science:

  • Virology
  • Immunology
  • Molecular Biology

Background:

  • Many echovirus (EV) and Coxsackie B virus (CBV) serotypes utilize human decay-accelerating factor (DAF) as a cellular receptor for infection.
  • Rodent DAF analogues share approximately 60% amino acid identity with human DAF.

Purpose of the Study:

  • To investigate the species specificity of DAF as a receptor for EV and CBV infection.
  • To determine if rodent DAF analogues can serve as receptors for these viruses.

Main Methods:

  • Hemagglutination assays using human, rat, and mouse erythrocytes.
  • Binding assays with radiolabeled EVs and CBVs incubated with Chinese hamster ovary (CHO) cells expressing human or rodent DAF.

Main Results:

  • EV and CBV serotypes tested caused hemagglutination of human erythrocytes but not rodent erythrocytes.
  • Radiolabeled viruses specifically bound to CHO cells expressing human DAF, but not rodent DAF.
  • While binding was human DAF-specific, complement inhibition by expressed DAF was similar across species.

Conclusions:

  • EV and CBV binding and subsequent infection are specific to human DAF, not rodent analogues.
  • This species-specific interaction highlights distinct viral tropism mechanisms.
  • DAF's role in complement inhibition is conserved, despite species-specific viral binding differences.

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