This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Supplemental material
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Google Scholar
Right arrow Articles by Harbison, C. E.
Right arrow Articles by Parrish, C. R.
PubMed
Right arrow PubMed Citation
Right arrow Articles by Harbison, C. E.
Right arrow Articles by Parrish, C. R.

 Previous Article  |  Next Article 

Journal of Virology, October 2009, p. 10504-10514, Vol. 83, No. 20
0022-538X/09/$08.00+0     doi:10.1128/JVI.00295-09
Copyright © 2009, American Society for Microbiology. All Rights Reserved.

Early Steps in Cell Infection by Parvoviruses: Host-Specific Differences in Cell Receptor Binding but Similar Endosomal Trafficking {triangledown} ,{dagger}

Carole E. Harbison, Sangbom Michael Lyi, Wendy S. Weichert, and Colin R. Parrish*

Baker Institute for Animal Health, Department of Microbiology and Immunology, College of Veterinary Medicine, Cornell University, Ithaca, New York 14853

Received 11 February 2009/ Accepted 26 July 2009

Canine parvovirus (CPV) and feline panleukopenia virus (FPV) are closely related parvoviruses that differ in their host ranges for cats and dogs. Both viruses bind their host transferrin receptor (TfR), enter cells by clathrin-mediated endocytosis, and traffic with that receptor through endosomal pathways. Infection by these viruses appears to be inefficient and slow, with low numbers of virions infecting the cell after a number of hours. Species-specific binding to TfR controls viral host range, and in this study FPV and strains of CPV differed in the levels of cell attachment, uptake, and infection in canine and feline cells. During infection, CPV particles initially bound and trafficked passively on the filopodia of canine cells while they bound to the cell body of feline cells. That binding was associated with the TfR as it was disrupted by anti-TfR antibodies. Capsids were taken up from the cell surface with different kinetics in canine and feline cells but, unlike transferrin, most did not recycle. Capsids labeled with fluorescent markers were seen in Rab5-, Rab7-, or Rab11-positive endosomal compartments within minutes of uptake, but reached the nucleus. Constitutively active or dominant negative Rab mutants changed the intracellular distribution of capsids and affected the infectivity of virus in cells.


* Corresponding author. Mailing address: Baker Institute for Animal Health, Department of Microbiology and Immunology, College of Veterinary Medicine, Cornell University, Ithaca, NY 14853. Phone: (607) 256-5649. Fax: (607) 256-5608. E-mail: crp3{at}cornell.edu

{triangledown} Published ahead of print on 5 August 2009.

{dagger} Supplemental material for this article may be found at http://jvi.asm.org/.


Journal of Virology, October 2009, p. 10504-10514, Vol. 83, No. 20
0022-538X/09/$08.00+0     doi:10.1128/JVI.00295-09
Copyright © 2009, American Society for Microbiology. All Rights Reserved.