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Transferrin receptor binds virus capsid with dynamic motion.

Hyunwook Lee1, Heather M Callaway2, Javier O Cifuente3

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Summary
This summary is machine-generated.

Canine parvovirus (CPV) uses mutations to bind dog transferrin receptor-1 (TfR), causing severe disease. New cryo-EM structures reveal dynamic CPV-TfR interactions, explaining viral species jumping and host range.

Keywords:
CPVTfRcryo-EM structuredynamichost jump

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Area of Science:

  • Virology
  • Structural Biology
  • Molecular Interactions

Background:

  • Canine parvovirus (CPV) causes severe diseases in dogs, including enteritis and myocarditis.
  • CPV cross-species transmission is linked to mutations altering binding to the canine transferrin receptor type-1 (TfR).
  • Previous studies suggested an asymmetric CPV-TfR complex, but molecular details remained unclear.

Purpose of the Study:

  • To elucidate the molecular mechanisms of CPV-TfR interaction.
  • To determine the high-resolution structures of the CPV-TfR complex.
  • To provide insights into CPV host range and species jumping.

Main Methods:

  • Cryo-electron microscopy (cryo-EM) was used to solve the structures of the CPV-TfR complex.
  • Icosahedral and asymmetric complex structures were determined at 3.0-Å and 5.0-Å resolution, respectively.
  • Detailed structural analyses identified the virus-receptor interface and interacting residues.

Main Results:

  • Conformational variations in TfR molecules were observed relative to the CPV binding site.
  • Dynamic molecular interactions between CPV and TfR were revealed.
  • The precise footprint of TfR on the CPV capsid and key amino acid residues at the interface were identified.

Conclusions:

  • A novel "rock-and-roll" model explains the dynamic CPV-TfR interaction.
  • The findings provide a molecular basis for CPV species jumping and host range variation.
  • Understanding these interactions is crucial for addressing new CPV pandemics in dogs.