 |
PDBsum entry 1z1c
|
|
|
|
References listed in PDB file
|
 |
|
Key reference
|
|
|
Title
|
|
Structural determinants of tissue tropism and in vivo pathogenicity for the parvovirus minute virus of mice.
|
|
|
Authors
|
|
M.Kontou,
L.Govindasamy,
H.J.Nam,
N.Bryant,
A.L.Llamas-Saiz,
C.Foces-Foces,
E.Hernando,
M.P.Rubio,
R.Mckenna,
J.M.Almendral,
M.Agbandje-Mckenna.
|
|
|
Ref.
|
|
J Virol, 2005,
79,
10931-10943.
|
|
|
PubMed id
|
|
|
|
|
|
Abstract
|
|
|
Two strains of the parvovirus minute virus of mice (MVM), the immunosuppressive
(MVMi) and the prototype (MVMp) strains, display disparate in vitro tropism and
in vivo pathogenicity. We report the crystal structures of MVMp virus-like
particles (MVMp(b)) and native wild-type (wt) empty capsids (MVMp(e)),
determined and refined to 3.25 and 3.75 A resolution, respectively, and their
comparison to the structure of MVMi, also refined to 3.5 A resolution in this
study. A comparison of the MVMp(b) and MVMp(e) capsids showed their structures
to be the same, providing structural verification that some heterologously
expressed parvovirus capsids are indistinguishable from wt capsids produced in
host cells. The structures of MVMi and MVMp capsids were almost identical, but
local surface conformational differences clustered from symmetry-related capsid
proteins at three specific domains: (i) the icosahedral fivefold axis, (ii) the
"shoulder" of the protrusion at the icosahedral threefold axis, and (iii) the
area surrounding the depression at the icosahedral twofold axis. The latter two
domains contain important determinants of MVM in vitro tropism (residues 317 and
321) and forward mutation residues (residues 399, 460, 553, and 558) conferring
fibrotropism on MVMi. Furthermore, these structural differences between the MVM
strains colocalize with tropism and pathogenicity determinants mapped for other
autonomous parvovirus capsids, highlighting the importance of common parvovirus
capsid regions in the control of virus-host interactions.
|
|
|
Secondary reference #1
|
|
|
Title
|
|
Structure determination of minute virus of mice.
|
|
|
Authors
|
|
A.L.Llamas-Saiz,
M.Agbandje-Mckenna,
W.R.Wikoff,
J.Bratton,
P.Tattersall,
M.G.Rossmann.
|
|
|
Ref.
|
|
Acta Crystallogr D Biol Crystallogr, 1997,
53,
93.
[DOI no: ]
|
|
|
PubMed id
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
Figure 1.
Fig. 1. (a) Selfrotation functions for x = 180 ° sing data between 10
and 6 A resolution in the C2 space group. Axial directions for he
rhombohedral system's hexagonl setting ar shown as aN*, b/4,
and c/4. The axial directions for the monoclinic system a M, b v and
c M are also hown. The orientation is chosen to correspond o he
rhobohedral spacegroup setting looking down the threefold axis.
Great circles are shon connecting adjacent twofold axes. Contours
and grid circles for the two independent particles are differentiated
by using red and blue. Insets show details of selecte peaks using
data between 4.0 and 3.0 A resolution. The black contours show he
rotation function calculated with the data processed in space group
R32, whereas the green contours show he rotation function
calculated for space group C2. (b) The relatioship between he
pseudo higher order space group R32 and the actual space group
C2. Axes are labeled as indicated above.
|
|
Figure 3.
Fig. 3. Stereoviews of the
MVMi electron density (blue)
superimposed on the origi
nal CPV density (red). (a)
Insertion of six residues
(554559) in MVMi, relative
to CPV. (b) Deleton of
three residues in MVMi
after residue 303, relative to
CPV. (c) Substitution of CPV
residue Val106 with Trp108
in MVMi. (d) Substitution
of CPV residue Phel21 with
Leu]23 in MVMi.
|
|
Figure 4.
Fig. 4. Comparison of averaged radial difference between MVMi and
CPV Co positions as a function of radial distance from the viral
center.
|
|
|
|
|
|
The above figures are
reproduced from the cited reference
with permission from the IUCr
|
|
|
|
|
|
|
