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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,
Timothy S.
Baker,2
Tim F.
Booth,3,
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
-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.
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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