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

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 si...

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Bibliographic Details
Published in:Journal of virology 2016-05, Vol.90 (9), p.4849-4853
Main Authors: Lee, Donald W, Allison, Andrew B, Bacon, Kaitlyn B, Parrish, Colin R, Daniel, Susan
Format: Article
Language:English
Subjects:
Animals
Canine parvovirus
Capsid Proteins - chemistry
Capsid Proteins - genetics
Capsid Proteins - metabolism
Cell Line
Dogs
Kinetics
Microscopy, Fluorescence - methods
Molecular Imaging - methods
Parvovirus
Parvovirus, Canine - physiology
Point Mutation
Protein Binding
Raccoons
Receptors, Transferrin - metabolism
Spotlight
Staining and Labeling
Viral Tropism
Virus-Cell Interactions
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Summary: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.
ISSN:0022-538X
1098-5514
DOI:10.1128/JVI.03204-15