Three-dimensional structure of Aleutian mink disease parvovirus: implications for disease pathogenicity.

TY - JOUR

T1 - Three-dimensional structure of Aleutian mink disease parvovirus: implications for disease pathogenicity.

AU - McKenna, R

AU - Olson, N H

AU - Chipman, P R

AU - Baker, T S

AU - Booth, T F

AU - Christensen, Jesper Aagaard

AU - Aasted, B

AU - Fox, J M

AU - Bloom, M E

AU - Wolfinbarger, J B

AU - Agbandje-McKenna, M

N1 - Keywords: Aleutian Mink Disease; Aleutian Mink Disease Virus; Amino Acid Sequence; Animals; Capsid; Capsid Proteins; Cats; Cell Line; Cryoelectron Microscopy; Dogs; Humans; Mice; Models, Molecular; Molecular Sequence Data; Protein Structure, Secondary; Recombinant Fusion Proteins; Sequence Homology, Amino Acid; Spodoptera

PY - 1999

Y1 - 1999

N2 - The three-dimensional structure of expressed VP2 capsids of Aleutian mink disease parvovirus strain G (ADVG-VP2) has been determined to 22 A 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 A 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.

AB - The three-dimensional structure of expressed VP2 capsids of Aleutian mink disease parvovirus strain G (ADVG-VP2) has been determined to 22 A 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 A 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.

M3 - Journal article

C2 - 10400786

SN - 0022-538X

VL - 73

SP - 6882

EP - 6891

JO - Journal of Virology

JF - Journal of Virology

IS - 8

ER -