Other search tools

About this data

The publication data currently available has been vetted by Vanderbilt faculty, staff, administrators and trainees. The data itself is retrieved directly from NCBI's PubMed and is automatically updated on a weekly basis to ensure accuracy and completeness.

If you have any questions or comments, please contact us.

Results: 1 to 5 of 5

Publication Record

Connections

A common structure for the potexviruses.
Kendall A, Bian W, Maris A, Azzo C, Groom J, Williams D, Shi J, Stewart PL, Wall JS, Stubbs G
(2013) Virology 436: 173-8
MeSH Terms: Amino Acid Sequence, Binding Sites, Capsid, Capsid Proteins, Cryoelectron Microscopy, Microscopy, Electron, Scanning Transmission, Potexvirus, Protein Structure, Secondary, RNA, Viral, X-Ray Diffraction
Show Abstract · Added February 15, 2016
We have used fiber diffraction, cryo-electron microscopy, and scanning transmission electron microscopy to confirm the symmetry of three potexviruses, potato virus X, papaya mosaic virus, and narcissus mosaic virus, and to determine their low-resolution structures. All three viruses have slightly less than nine subunits per turn of the viral helix. Our data strongly support the view that all potexviruses have approximately the same symmetry. The structures are dominated by a large domain at high radius in the virion, with a smaller domain, which includes the putative RNA-binding site, extending to low radius.
Copyright © 2012 Elsevier Inc. All rights reserved.
0 Communities
1 Members
0 Resources
10 MeSH Terms
Structure of flexible filamentous plant viruses.
Kendall A, McDonald M, Bian W, Bowles T, Baumgarten SC, Shi J, Stewart PL, Bullitt E, Gore D, Irving TC, Havens WM, Ghabrial SA, Wall JS, Stubbs G
(2008) J Virol 82: 9546-54
MeSH Terms: Capsid, Capsid Proteins, Cryoelectron Microscopy, Flexiviridae, Image Processing, Computer-Assisted, Microscopy, Electron, Scanning, Microscopy, Electron, Transmission, Molecular Conformation, Plant Viruses, Potexvirus, Potyvirus, RNA, Viral, Virion
Show Abstract · Added March 13, 2012
Flexible filamentous viruses make up a large fraction of the known plant viruses, but in comparison with those of other viruses, very little is known about their structures. We have used fiber diffraction, cryo-electron microscopy, and scanning transmission electron microscopy to determine the symmetry of a potyvirus, soybean mosaic virus; to confirm the symmetry of a potexvirus, potato virus X; and to determine the low-resolution structures of both viruses. We conclude that these viruses and, by implication, most or all flexible filamentous plant viruses share a common coat protein fold and helical symmetry, with slightly less than 9 subunits per helical turn.
0 Communities
2 Members
0 Resources
13 MeSH Terms
Radial density distribution and symmetry of a Potexvirus, narcissus mosaic virus.
Kendall A, Bian W, Junn J, McCullough I, Gore D, Stubbs G
(2007) Virology 357: 158-64
MeSH Terms: Narcissus, Potexvirus, RNA, Viral, Virion
Show Abstract · Added March 13, 2012
Narcissus mosaic virus is a Potexvirus, a member of the Flexiviridae family of filamentous plant viruses. Fiber diffraction patterns from oriented sols of narcissus mosaic virus have been used to determine the symmetry and structural parameters of the viral helix. The virions have a radius of 55+/-5 A. The viral helix has a pitch of 34.45+/-0.5 A, with 7.8 subunits per turn of the helix. We conclude that all members of the Potexvirus genus have close to 8 subunits per helical turn.
0 Communities
2 Members
0 Resources
4 MeSH Terms
Surface features of potato virus X from fiber diffraction.
Parker L, Kendall A, Stubbs G
(2002) Virology 300: 291-5
MeSH Terms: Potexvirus, X-Ray Diffraction
Show Abstract · Added March 13, 2012
Fiber diffraction patterns have been obtained from oriented sols of potato virus X. Orientation in the sols was greatly improved by a combination of centrifugation and exposure to very high magnetic fields. Diffraction patterns were also improved by using a very finely collimated synchrotron X-ray beam. The diffraction patterns show that there are 8.9 subunits in each turn of the viral helix and that intersecting sets of deep grooves mark the viral surface, with one set running almost longitudinally and the other following the simple viral helix.
0 Communities
2 Members
0 Resources
2 MeSH Terms
Coat protein interactions involved in tobacco mosaic tobamovirus cross-protection.
Lu B, Stubbs G, Culver JN
(1998) Virology 248: 188-98
MeSH Terms: Capsid Proteins, Models, Molecular, Mutagenesis, Site-Directed, Plants, Toxic, Potexvirus, RNA, Viral, Tobacco, Tobacco Mosaic Virus, Viral Interference, Viral Proteins, Virus Assembly
Show Abstract · Added February 15, 2016
To investigate the molecular role of the tobacco mosaic tobamovirus (TMV) coat protein (CP) in conferring cross-protection, a potato X potexvirus (PVX) vector (S. Chapman, Plant J. 2, 549-557, 1992) was used to systemically express a set of TMV mutant CPs in Nicotiana benthamiana prior to challenge inoculation with TMV. PVX-expressed wild-type TMV CP delayed TMV accumulation for up to 2 weeks compared to unprotected plants or plants preinfected with the unmodified PVX vector. Similar delays in TMV accumulation were obtained using TMV CPs that were deficient in virion formation but competent to assemble into helical aggregates. In contrast, TMV CPs that were incapable of helical aggregation or unable to bind viral RNA did not delay the accumulation of TMV. Furthermore, TMV CPs with enhanced intersubunit interactions that favor helical aggregation produced significantly greater delays in the accumulation of challenge TMV than obtained from the wild-type CP. Thus the capabilities of TMV CP to interact with viral RNA and self-associate in a helical fashion appear to be essential to its ability to confer protection. Taken together, these findings support a model for CP-mediated resistance in which the protecting CP recoats the challenge virus RNA as it disassembles.
Copyright 1998 Academic Press.
0 Communities
1 Members
0 Resources
11 MeSH Terms