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Respiratory Syncytial Virus Disease01:29

Respiratory Syncytial Virus Disease

Human respiratory syncytial virus (RSV) is a widespread pathogen that primarily targets infants and young children but also poses a serious health risk to elderly and immunocompromised individuals. Belonging to the Pneumoviridae family, RSV is a negative-sense, single-stranded RNA virus within the Pneumovirus genus. Its global health burden is significant, with millions of cases annually resulting in hospitalizations and mortality, particularly in resource-limited settings. Although most...

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Mechanistic Insights into PRRSV Inhibition through CD163-SRCR5 Blockade by PRRSV/CD163-IN-1.

Prawit Thitayanuwat1, Kowit Hengphasatporn2, Surang Chankhamhaengdecha1

  • 1Department of Biology, Faculty of Science, Mahidol University, Rama VI Road, Rachadhavi, Bangkok 10400, Thailand.

The Journal of Physical Chemistry Letters
|June 13, 2025
PubMed
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This study reveals how a compound blocks the Porcine reproductive and respiratory syndrome virus (PRRSV) from infecting swine cells. Researchers identified baicalin as a potential antiviral lead compound for PRRSV entry inhibition.

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Area of Science:

  • Virology
  • Structural Biology
  • Computational Chemistry

Background:

  • Porcine reproductive and respiratory syndrome virus (PRRSV) causes significant economic losses in the swine industry.
  • PRRSV infects pulmonary alveolar macrophages by binding to the CD163 receptor, specifically its Scavenger Receptor Cysteine-Rich (SRCR) domain 5 (SRCR5).
  • The precise molecular mechanisms of small-molecule inhibition at the PRRSV-CD163 interface are not fully understood.

Purpose of the Study:

  • To elucidate the molecular mechanisms by which small molecules inhibit PRRSV entry via the CD163-SRCR5 interaction.
  • To identify potential PRRSV entry inhibitors through computational screening.

Main Methods:

  • Structural refinement and molecular dynamics (MD) simulations of the CD163-SRCR5 domain.
  • Ensemble docking and fragment molecular orbital (FMO) calculations to predict binding conformations.
  • Virtual screening of a small-molecule repurposing library against an MD-refined CD163-SRCR5 model.

Main Results:

  • A plausible binding conformation for the PRRSV/CD163-IN-1 (B7) compound at the CD163-SRCR5 interface was identified.
  • An MD-refined model of CD163-SRCR5 was developed to overcome crystal structure limitations in representing conformational flexibility.
  • Baicalin was identified as a top candidate inhibitor through in silico screening, aligning with prior experimental findings.

Conclusions:

  • The study provides the first mechanistic insights into PRRSV entry inhibition at the molecular level.
  • Baicalin's antiviral activity is supported, reinforcing its potential as a lead compound for PRRSV therapeutics.
  • A framework for designing novel PRRSV entry inhibitors targeting the CD163-SRCR5 interaction has been established.