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Particle Agglutination Method for Poliovirus Identification
Published on: April 20, 2011
Distinct cellular receptor interactions in poliovirus and rhinoviruses
L Xing1, K Tjarnlund, B Lindqvist
1Karolinska Institute, Department of Biosciences at NOVUM, Center for Biotechnology, S-141 57 Huddinge, Sweden.
Abstract:
Receptor binding to human poliovirus type 1 (PV1/M) and the major group of human rhinoviruses (HRV) was studied comparatively to uncover the evolution of receptor recognition in picornaviruses. Surface plas- mon resonance showed receptor binding to PV1/M with faster association and dissociation rates than to HRV3 and HRV16, two serotypes that have similar binding kinetics. The faster rate for receptor association to PV1/M suggested a relatively more accessible binding site. Thermodynamics for receptor binding to the viruses and assays for receptor-mediated virus uncoating showed a more disruptive receptor interaction with PV1/M than with HRV3 or HRV16. Cryo-electron microscopy and image reconstruction of receptor-PV1/M complexes revealed receptor binding to the 'wall' of surface protrusions surrounding the 'canyon', a depressive surface in the capsid where the rhinovirus receptor binds. These data reveal more exposed receptor-binding sites in poliovirus than rhinoviruses, which are less protected from immune surveillance but more suited for receptor-mediated virus uncoating and entry at the cell surface.
Insights
Poliovirus (PV1/M) has more accessible receptor binding sites than rhinoviruses (HRV), facilitating faster cell entry. This difference in receptor interaction impacts viral evolution and immune evasion strategies.
Area of Science:
- Virology
- Structural Biology
- Evolutionary Biology
Background:
- Picornaviruses, including poliovirus and rhinoviruses, utilize specific cell surface receptors for entry.
- Understanding receptor recognition evolution is key to comprehending picornavirus diversity and pathogenesis.
Purpose of the Study:
- To comparatively analyze receptor binding kinetics and mechanisms between human poliovirus type 1 (PV1/M) and human rhinoviruses (HRV).
- To elucidate the evolutionary implications of differing receptor recognition strategies in picornaviruses.
Main Methods:
- Surface plasmon resonance (SPR) to measure virus-receptor binding kinetics (association and dissociation rates).
- Thermodynamic analysis of receptor-virus interactions.
- Assays for receptor-mediated virus uncoating.
- Cryo-electron microscopy (Cryo-EM) and image reconstruction to visualize receptor-PV1/M complexes.
Main Results:
- PV1/M exhibited faster association and dissociation rates with its receptor compared to HRV3 and HRV16.
- Receptor interaction with PV1/M was thermodynamically more disruptive than with HRV3 or HRV16.
- Cryo-EM revealed PV1/M receptor binding at the 'wall' of surface protrusions, distinct from the HRV receptor binding 'canyon'.
Conclusions:
- Poliovirus possesses more exposed receptor-binding sites than rhinoviruses.
- These exposed sites in poliovirus are less protected from immune surveillance but enhance receptor-mediated uncoating and cell entry.
- The findings provide insights into the distinct evolutionary paths of poliovirus and rhinovirus receptor engagement.
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