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J Virol. 2016 Apr 14;90(9):4849-53. doi: 10.1128/JVI.03204-15. Print 2016 May.

Single-Particle Tracking Shows that a Point Mutation in the Carnivore Parvovirus Capsid Switches Binding between Host-Specific Transferrin Receptors.

Author information

1
School of Chemical and Biomolecular Engineering, Cornell University, Ithaca, New York, USA.
2
Baker Institute for Animal Health, Department of Microbiology and Immunology, College of Veterinary Medicine, Cornell University, Ithaca, New York, USA.
3
Baker Institute for Animal Health, Department of Microbiology and Immunology, College of Veterinary Medicine, Cornell University, Ithaca, New York, USA crp3@cornell.edu sd386@cornell.edu.
4
School of Chemical and Biomolecular Engineering, Cornell University, Ithaca, New York, USA crp3@cornell.edu sd386@cornell.edu.

Abstract

Determining how viruses infect new hosts via receptor-binding mechanisms is important for understanding virus emergence. We studied the binding kinetics of canine parvovirus (CPV) variants isolated from raccoons-a newly recognized CPV host-to different carnivore transferrin receptors (TfRs) using single-particle tracking. Our data suggest that CPV may utilize adhesion-strengthening mechanisms during TfR binding and that a single mutation in the viral capsid at VP2 position 300 can profoundly alter receptor binding and infectivity.

PMID:
26889026
PMCID:
PMC4836364
DOI:
10.1128/JVI.03204-15
[Indexed for MEDLINE]
Free PMC Article

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