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Early Viral Entry Assays for the Identification and Evaluation of Antiviral Compounds
Published on: October 29, 2015
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The conserved human astrovirus-receptor interface reveals a targetable vulnerability for antiviral development
Wei Wang1, Ying Xu1, Zehou Li1
1College of Life Sciences, Nanjing Agricultural University, Nanjing, China.
Nature Communications
|March 12, 2026
Summary
Human astrovirus uses the neonatal Fc receptor (FcRn) for cell entry. This study reveals a conserved binding mechanism and suggests repurposing FcRn inhibitors to treat astrovirus infections.
Area of Science:
- Virology
- Structural Biology
- Immunology
Background:
- Human astrovirus (HAstV) is a significant cause of viral enteritis globally, particularly in children and the elderly.
- Classical HAstVs (HAstV1-8) utilize the neonatal Fc receptor (FcRn) as their cellular entry receptor.
Purpose of the Study:
- To elucidate the receptor binding mechanism of HAstVs by determining the structural basis of HAstV-FcRn interaction.
- To investigate the potential of targeting this interaction for therapeutic intervention.
Main Methods:
- Crystal structure determination of the HAstV8 spike protein complexed with human FcRn.
- In vitro assessment of FcRn inhibitor efficacy against astrovirus infection in Caco2 cells.
Main Results:
- The crystal structure revealed that the HAstV8 spike protein binds to a conserved surface depression on human FcRn.
- This binding interface is conserved across classical HAstV serotypes.
- Clinically approved FcRn inhibitors effectively suppressed astrovirus infection and reduced viral RNA levels.
Conclusions:
- A conserved receptor recognition mechanism exists among human astroviruses, involving binding to a specific site on FcRn.
- Repurposing existing FcRn inhibitors presents a promising therapeutic strategy for treating human astrovirus infections.
