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 inJournal of virology Vol. 90; no. 9; pp. 4849 - 4853
Main Authors Lee, Donald W, Allison, Andrew B, Bacon, Kaitlyn B, Parrish, Colin R, Daniel, Susan
Format Journal Article
LanguageEnglish
Published United States American Society for Microbiology 01.05.2016
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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.
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D.W.L. and A.B.A. contributed equally to this work.
Citation Lee DW, Allison AB, Bacon KB, Parrish CR, Daniel S. 2016. Single-particle tracking shows that a point mutation in the carnivore parvovirus capsid switches binding between host-specific transferrin receptors. J Virol 90:4849–4853. doi:10.1128/JVI.03204-15.
ISSN:0022-538X
1098-5514
DOI:10.1128/JVI.03204-15