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

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

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.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Animals
  • Capsid Proteins / chemistry
  • Capsid Proteins / genetics*
  • Capsid Proteins / metabolism*
  • Cell Line
  • Dogs
  • Kinetics
  • Microscopy, Fluorescence / methods
  • Molecular Imaging / methods
  • Parvovirus, Canine / physiology*
  • Point Mutation*
  • Protein Binding
  • Raccoons
  • Receptors, Transferrin / metabolism*
  • Staining and Labeling
  • Viral Tropism*

Substances

  • Capsid Proteins
  • Receptors, Transferrin