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Journal of Virology, August 1999, p. 6882-6891, Vol. 73, No. 8
0022-538X/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.

Three-Dimensional Structure of Aleutian Mink Disease Parvovirus: Implications for Disease Pathogenicity

Robert McKenna,1 Norman H. Olson,2 Paul R. Chipman,2,dagger Timothy S. Baker,2 Tim F. Booth,3,dagger Jesper Christensen,4 Bent Aasted,4 James M. Fox,5 Marshall E. Bloom,5 James B. Wolfinbarger,5 and Mavis Agbandje-McKenna1,*

Department of Biological Sciences, University of Warwick, Coventry CV4 7AL,1 and NERC Institute of Virology and Environmental Microbiology, Oxford OX1 3SR,3 United Kingdom; Department of Biological Sciences, Purdue University, West Lafayette, Indiana 47907-13922; Laboratory of Virology and Immunology, Department of Veterinary Microbiology, The Royal Veterinary and Agricultural University, Copenhagen, Denmark4; and Laboratory of Persistent Viral Diseases, National Institute of Allergy and Infectious Diseases, Hamilton, Montana 598405

Received 30 November 1998/Accepted 15 April 1999

The three-dimensional structure of expressed VP2 capsids of Aleutian mink disease parvovirus strain G (ADVG-VP2) has been determined to 22 Å resolution by cryo-electron microscopy and image reconstruction techniques. A structure-based sequence alignment of the VP2 capsid protein of canine parvovirus (CPV) provided a means to construct an atomic model of the ADVG-VP2 capsid. The ADVG-VP2 reconstruction reveals a capsid structure with a mean external radius of 128 Å and several surface features similar to those found in human parvovirus B19 (B19), CPV, feline panleukopenia virus (FPV), and minute virus of mice (MVM). Dimple-like depressions occur at the icosahedral twofold axes, canyon-like regions encircle the fivefold axes, and spike-like protrusions decorate the threefold axes. These spikes are not present in B19, and they are more prominent in ADV compared to the other parvoviruses owing to the presence of loop insertions which create mounds near the threefold axes. Cylindrical channels along the fivefold axes of CPV, FPV, and MVM, which are surrounded by five symmetry-related beta -ribbons, are closed in ADVG-VP2 and B19. Immunoreactive peptides made from segments of the ADVG-VP2 capsid protein map to residues in the mound structures. In vitro tissue tropism and in vivo pathogenic properties of ADV map to residues at the threefold axes and to the wall of the dimples.

* Corresponding author. Present address: Department of Biochemistry and Molecular Biology, Center for Structural Biology, The Brain Institute, College of Medicine, University of Florida, P.O. Box 100245, Gainesville, FL 32610-0245. Phone: (352)392-4304. Fax: (352) 392-3422. E-mail: mamckenna{at}ufl.edu.

dagger Present address: Canadian Food Inspection Agency, National Centre for Foreign Animal Disease, Winnipeg, Mannitoba R3E 3M4, Canada.

Journal of Virology, August 1999, p. 6882-6891, Vol. 73, No. 8
0022-538X/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.


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