Interaction of poliovirus with its purified receptor and conformational alteration in the virion

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Updated: Oct 30, 2026

Particle Agglutination Method for Poliovirus Identification
07:06

Particle Agglutination Method for Poliovirus Identification

Published on: April 20, 2011

M Arita1, S Koike, J Aoki

  • 1Institute of Medical Science, The University of Tokyo, Japan.

Journal of Virology
|April 29, 1998
PubMed

Insights

Human poliovirus receptor (hPVR) fragments PVR241 and PVR330 were produced and purified. PVR330 binds poliovirus virions, causing conformational changes and suggesting a specific interaction mechanism.

Area of Science:

  • Biochemistry
  • Virology
  • Molecular Biology

Background:

  • The human poliovirus receptor (hPVR) facilitates poliovirus entry into host cells.
  • Understanding hPVR-poliovirus interactions is crucial for antiviral strategies.
  • Extracellular domains of hPVR play a key role in virus binding.

Purpose of the Study:

  • To produce and characterize functional fragments of the human poliovirus receptor (hPVR).
  • To investigate the binding kinetics and conformational effects of hPVR-poliovirus interactions.
  • To elucidate the mechanism of poliovirus conformational changes upon receptor binding.

Main Methods:

  • Production of hPVR polypeptides (PVR241, PVR330) using a baculovirus expression system.
  • Purification of hPVR fragments via immunoaffinity chromatography with anti-hPVR monoclonal antibodies.
  • In vitro binding assays mixing purified PVR with poliovirus type 1 (Mahoney strain).
  • Analysis of virus conformational changes (160S to 135S and 80S particles) using sedimentation assays.

Main Results:

  • Purified PVR241 and PVR330 retained native conformation, confirmed by antibody reactivity.
  • PVR330 demonstrated binding to poliovirus virions, with at least 43 PVR330 molecules binding per virion.
  • The equilibrium dissociation constant (Kd) for PVR330-virion interaction was determined as 4.50 x 10(-8) M at 4°C.
  • Increased PVR330 concentration led to higher rates of poliovirus conformational changes (160S to 135S and 80S particles).
  • The ratio of 135S to 80S particles remained constant, and 80S particles did not form from 135S particles post-160S disappearance.

Conclusions:

  • Recombinant hPVR fragments, particularly PVR330, can be produced and retain functional conformation.
  • PVR330 binds poliovirus virions with high affinity, indicating specific molecular interactions.
  • PVR binding induces significant conformational changes in the poliovirus capsid, potentially related to uncoating or entry mechanisms.
  • The observed conformational transitions suggest distinct pathways or intermediates in the virus-receptor interaction process.

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