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Cylindrical inclusion protein of potato virus A is associated with a subpopulation of particles isolated from infected plants.
- Source :
-
The Journal of general virology [J Gen Virol] 2008 Mar; Vol. 89 (Pt 3), pp. 829-838. - Publication Year :
- 2008
-
Abstract
- Potato virus A (PVA) particles were purified by centrifugation through a 30 % sucrose cushion and the pellet (P1) was resuspended and sedimented through a 5-40 % sucrose gradient. The gradient separation resulted in two different virus particle populations: a virus fraction (F) that formed a band in the gradient and one that formed a pellet (P2) at the bottom of the gradient. All three preparations contained infectious particles that retained their integrity when visualized by electron microscopy (EM). Western blotting of the P1 particles revealed that the viral RNA helicase, cylindrical inclusion protein (CI), co-purified with virus particles. This result was confirmed with co-immunoprecipitation experiments. CI was detected in P2 particle preparations, whereas F particles were devoid of detectable amounts of CI. ATPase activity was detected in all three preparations with the greatest amount in P2. Results from immunogold-labelling EM experiments suggested that a fraction of the CI present in the preparations was localized to one end of the virion. Atomic force microscopy (AFM) studies showed that P1 and P2 contained intact particles, some of which had a protruding tip structure at one end, whilst F virions were less stable and mostly appeared as beaded structures under the conditions of AFM. The RNA of the particles in F was translated five to ten times more efficiently than RNA from P2 particles when these preparations were subjected to translation in wheat-germ extracts. The results are discussed in the context of a model for CI-mediated functions.
- Subjects :
- Amino Acid Sequence
Centrifugation, Density Gradient
Immunoprecipitation
Microscopy, Atomic Force
Molecular Sequence Data
Peptide Mapping
Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
Viral Proteins chemistry
Virion pathogenicity
Plant Diseases virology
Potyvirus metabolism
Solanum tuberosum virology
Viral Proteins metabolism
Virion isolation & purification
Virion metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 0022-1317
- Volume :
- 89
- Issue :
- Pt 3
- Database :
- MEDLINE
- Journal :
- The Journal of general virology
- Publication Type :
- Academic Journal
- Accession number :
- 18272775
- Full Text :
- https://doi.org/10.1099/vir.0.83406-0