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Cover photograph
(Copyright © 2006, Wiley):
legend: Hepatitis B virus,
rdially depth cued, as solved by X-ray crystallography (Image © 2004
Jean-Yves Sgro, University of Wisconsin Institute for Molecular Virology)
Atom rendering from atomic coordinates (PDB ID 1QGT) is radially
depth cued by color and was created with the program RASMOL.
Wynne, S.A., Crowther, R.A., Leslie, A.G. (1999)
The crystal structure of the human hepatitis B virus capsid.
Mol. Cell 3: 771-780
Virus Image created by JY Sgro
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HEPATOLOGY, VOLUME 44, NUMBER 2, AUGUST 2006 .
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Cover photograph
(Copyright © 2001, US Geological Survey):
legend:Molecular surface of Poliovirus Type 1 Mahoney,
rdially depth cued, as solved by X-ray crystallography (Image © 1999
Jean-Yves Sgro, University of Wisconsin Institute for Molecular
Virology)
Surface rendering from atomic coordinates (PDB ID 2PLV) is radially
depth cued by color and was created with the program GRASP.
Filman, D. J., Syed, R., Chow, M., Macadam, A. J., Minor, P. D.,
Hogle, J. M.: Structural factors that control conformational
transitions and serotype specificity in type 3 poliovirus. EMBO J 8 pp.
1567 (1989)
Virus Image created by JY Sgro
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Occurrence and Distribution of Enteric Viruses in SHallow Ground Water
and Factors Affecting Well Vulnerability to Microbiological
Contamination in Worcester and Wicomico Counties, Maryland .
Banks, W.S.L. and Klohe C.A.
(US Geological Survey)
and Batigelli D.A.
(Wisconsin State Laboratory of Hygiene)
Water-Resources Investigations Report 01-4147
In cooperation with the Maryland Department of the Environment.
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Cover photograph
(Copyright © 2001, American Society for Microbiology. All rights reserved.):
Structure of the cucumber necrosis virus (CNV) particle (T=3 icosahedron),
showing areas of the capsid important in fungal vector recognition.
Areas in yellow correspond to amino acid residues in the particle
quasi-threefold axis that are mutated in naturally occurring CNV
transmission mutants. The mutations also affect attachment to the outer
membrane of the fungal zoospore, suggesting a role for these sites in
receptor recognition. Three-dimensional coordinates for the CNV structure
were obtained by homology modeling, using tomato bushy stunt virus
coordinates and the program MODELLER. Surface rendering from atomic
coordinates is radially depth cued by color and was created with the
program GRASP.
Virus Image created by JY Sgro
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Journal of Virology
volume 75 June 2001 Issue 12
The American Society for Microbiology
Related article: Kishore Kakani,Jean-Yves Sgro, and D'Ann Rochon (2001)
Identification of Specific Cucumber Necrosis Virus Coat Protein Amino
Acids Affecting Fungus Transmission and Zoospore Attachment
J. Virol. 75(12): 5576-5583
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legend: Principios de virología
FRONT COVER: Many virus images. Sizes are not to relative scale.
The larger image is that of foot-and-mouth disease virus (FMDV), shown as
radially depth cued. In reality this virus is not larger than the other
viruses represented here. The red surface represents the location of the
highly antigenic loop (residues 134 - 157 on protein VP1) which was disordered
in previous crystallographic attempts.
FMDV, PDB-ID: 1FOD:
D.LOGAN, R.ABU-GHAZALEH, W.BLAKEMORE, S.CURRY,
T.JACKSON, A.KING, S.LEA, R.LEWIS, J.NEWMAN, N.PARRY,
D.ROWLANDS, D.STUART, E.FRY
Structure of a major immunogenic site on foot-and-mouth disease virus.
Nature 362 566, 1993.
BACK COVER: 2 stereo pairs, top pair depicts FMDV (virus de la fiebre aftosa),
bottom pair depicts poliovirus structure. Both viruses have a similar diameter
of about 30 nm.
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Principios de virología
© 2000
ISBN:958-655-449-X
Jorge Ossa Londoño Editor,
Medellín, Colombia.
Language: Spanish
Links:
Aspectos de la Universidad Colombiana
Alumni Profile, (UW-Madison)
e-mail: jeossa@catios.udea.edu.co
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legend: Largest and smallest complete viral particles solved by X-Ray
crystallography. Both structures are reprented here to scale.
The larger structure is simian virus 40 (PDB entry 1SVA, Stehle et. al.
1996), a Polyomavirus from the Papovaviridae family. The non-enveloped
icosahedral particles, ~45 nm in diameter contains the circular dsDNA
genome. 72 pentameric capsomers are arrange on a T=7d icosahedral
lattice, 12 strict pentamers at the icosahedral vertices have only 5
neighbouring capsomers while the other and 60 pentameric capsomers are
arranged in hexamers. View is along an icosahedral 2-fold axis of
symmetry.
The small structure is that of satellite tobacco necrosis virus
(PDB entry 2STV, Unge et. al. 1980). The non-enveloped
icosahedral particles, ~17 nm in diameter contains the linear ssRNA
genome. 60 proteins are arranges on a T=1 icosahedral lattice. View
is along an icosahedral 5-fold axis of symmetry.
T.STEHLE,S.J.GAMBLIN,Y.YAN,S.C.HARRISON
The structure of simian virus 40 refined at 3.1 A
resolution STRUCTURE (LONDON) 4, 165 1996
T.UNGE,L.LILJAS,B.STRANDBERG,I.VAARA,K.K.KANNAN,
K.FRIDBORG,C.E.NORDMAN,P.J.LENTZ *JUNIOR
Satellite tobaco necrosis virus structure at 4.0 A
resolution NATURE 285,373 1980
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Archives of Virology
All 1999 volumes.
ISSN 0304-8608
Springer-Verlag Wien
|
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legend: Coxscakievirus B3 image is a computer representation
derived fromx-ray coordinates (Mucklebauer et al. Structure 3:653,
1995). The PDB ENTRY for the virus is 1COV. The GRASP protein
molecular surface is radially depth-cued to visually highlight surface
features. The canyon is clearly evident. Note that the canyons are not
continuous around the 5-fold icosahedral axes. (Courtesy of Dr.
Jean-Yves Sgro, University of Wisconsin-Madison;
sgro@rhino.bocklabs.wisc.edu).
Photomicrographs of 0.6 micron thick hemotoxylin and eosin
stained sections of heart (above) and pancreas (below) taken
from a C3H/HeJ male mouse, 10 days post-inoculation with the
cardiovirulent wild-type strain of CVB3, CVB3/DO. Note significant and
widespread regions of necrosis and calcification in heart section
typical of results induced by infection with a
cardiovirulent CVB3. Pancreas has sustained severe damage to acinar cells.
Original magnification x100.
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The Coxsackie B Viruses
S. Tracy, N.M. Chapman and B.W.J. Mahy (Eds)
Springer
1997
ISSN 0070-217X
ISBN 3-540-62390-6
Library of Congress Catalog Card Number 15-12910
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legend: Computer-generated image of poliovirus type 1 Mahoney
strain derived from X-ray coordinates (PDB entry 2PLV, Hogle et
al.) showing a virion oriented along one of twelve icosahedral
50fold symmetry axes. Image generated by J.-Y. Sgro with the program
GRASP on Silicon Graphics. There are three articles about poliovirus
in this issue: M.-M. Georgescu et al. (pages 1819-1828),
B. Rombaut and J.P. M. Jore (pages 1829-1832) and F. J. M. Kuppeveld
et al. (pages 1833-1840).
Image represents poliovirus type 1 Mahoney (X-ray data Hogle et al., 1985,
Science 229: 1358) seen along one icosahedral 5-fold axis. Down in the
depression around the 5-fold axis the small yellow sticks represent a visible
portion of the "pocket factor". In most rhinoviruses this pocket entry
would be blocked by the C-terminal end of the VP3 protein "hanging" above
the pore entrance.
The image in radially depth cued to enhance toppographical perception of the
surface. Lighter colors are more prominents, darker colors represents areas
closer to the virion center.
Created with Grasp (A.Nicholls)
on Silicon Graphics from PDB published coordinates
(PDB entries 2PLV).
Image created by JY Sgro.
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Journal of General Virology
Volume 78 Part 8
August 1997
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No legend.
Image represents halved virion particles of
Theiler's virus BeAn (green) and DA (orange) strains,
showns side by side for comparison, created with Grasp
on Silicon Graphics from PDB published coordinates
(PDB entries 1TME (DA) and 1TMF (BeAn)).
Image created by JY Sgro
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Journal of General Virology
Off-Print promotional cover
1997
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| Computer graphics of the
three-dimensional structure of bean pod mottle virus. The surface of
virions has been radially depth-cued to enhance depiction of surface
topography. Virions on the left appear in various orientations;
prominent structures protrude at axes of 5-fold symmetry (yellow); deep
depressions occur at axes of 2-fold symmetry; and small surface ridges
are visible at axes of 3-fold symmetry. The virion at the right has
been sliced through is center to reveal interior features. Capsid
protein atoms are delineated as blue spheres to show the capsid
thickness (<10 Å at 2-fold axes, > 40 Å at 5-fold
axes). About 20% of the virion RNA was detected; it appears as trefoils
(pink) at axes of 3-fold symmetry. In the foreground an edge of a
virion appeats at close range. The structure of this virus was solved
in the laboratory of J.E. Johnson, then at Purdue University
[Chen et al., Science 245:154-159 (1989)]. The illustration
was created on a Silicon Graphics Workstation, using the program
GRASP as developped by Anthony Nicholls of Columbia University.
The image was composed and produced by Jean-Yves Sgro of the
Institute for Molecular Virology, University of Wisconsin, 1525
Linden Drive, Madison, Wisconsin, 53706-1596 USA.
|
Archives of Virology
All 1996 volumes.
ISSN 0304-8608
Springer-Verlag Wien
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Artistic rendering of a Mengo virion releasing its single stranded
RNA genome after infecting a cell.
Four kinds of viral coat proteins assemble following icosahedral
symmetry o form a shell around the genome. The icosahedral
5-fold axis of symmetry is easily recognized at the center of the
pentamers, star shaped raised surfaces. See "Using Viral Genes
to Fight Disease," p. 1050.
Image created by JY Sgro
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BIOTECHNOLOGY
volume 13 October 1995 Number 10
ISSN 0733-222X
Nature Publishing Co., owned
by Nature America, Inc., a
subsidiary of Macmillan Magazines
of London.
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Computer graphics representation of the virion of
human rhinovirus 14 along the icosahedral 3-fold axis
of symmetry, highlighting the topographic details
of the surface. Lighter colored structures are situated
further away from the virion center, showing
that the 5-fold axis region is the most prominent
feature. The "canyon" is clearly seen as a dark blue
depression around the 5-fold axis and is the binding site
for the cellular receptor ICAM-1. A depression is visible
at the icosahedral 2-fold axis of symmetry
(equidistant between two 5-fold vertices), but has no known
role.
Antibody binding sites determined by escape mutations are shown
in magenta and clearly appear in more exposed (white or light
blue) areas on "domes" and "ridges", suggesting that the dark
and blue areas are not within the reach of antibodies.
Image created by JY Sgro
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Medical Virology
David O. White
Frank J. Fenner
Academic Press, Inc.
ISBN 0-12-746642-8
1994
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No legend.
Image created by JY Sgro from VSurf Data (VSurfProgram from
Michael Rossamnn) and visualized with FRODO on an Evans & Sutherland
PS390 series workstation.
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NIAID
Report of the Task Force on Microbiology and Infectious Diseases
U.S. Department of Health and Human Services
Public Health Service
National Institute of Health
1992
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