Subcellular targeting of the coat protein of African cassava mosaic geminivirus.
@article{Unseld2001SubcellularTO, title={Subcellular targeting of the coat protein of African cassava mosaic geminivirus.}, author={Sigrid D. Unseld and M. K. H{\"o}hnle and M. Ringel and Thomas Frischmuth}, journal={Virology}, year={2001}, volume={286 2}, pages={ 373-83 }, url={https://api.semanticscholar.org/CorpusID:22923154} }
Results indicate that domains of the CP facilitate several aspects of geminivirus movement, including nuclear import and export and transport of the viral genome to the cell periphery.
73 Citations
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To map the functional domains of NSP, the intra-cellular localization of its full-length protein and deletion derivatives was studied in the epidermal cells of detached leaves of the laboratory host plant, Nicotiana benthamiana, where the target proteins were transiently expressed as GFP fusions.
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In DNA binding assays, supernatant CP accelerated the migration of ssDNA in agarose gels, which is a first hint for particle formation, and size-exclusion chromatography of the supernatan CP indicated high order complexes.
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Biology, Environmental Science
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46 References
Host and viral factors determine the dispensability of coat protein for bipartite geminivirus systemic movement.
- 1996
Biology, Environmental Science
B bipartite geminivirus movement in planta can be resolved genetically into three components: (i) local, cell-to-cell movement, which does not require CP; (ii) CP-dependent systemicmovement, which occurs in all hosts tested; and (iii)CP-independent systemic movement,Which occurs in hosts to which a given virus is well adapted.
Maize streak virus coat protein is karyophyllic and facilitates nuclear transport of viral DNA.
- 1999
Biology
Results suggest that, in addition to entering the nucleus where it is required for encapsidation of the viral ss DNA, the MSV CP facilitates the rapid transport of viral DNA into the nucleus.
Nuclear import of the capsid protein of tomato yellow leaf curl virus (TYLCV) in plant and insect cells.
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Biology, Environmental Science
It is demonstrated that TYLCV CP is transported into plant- and insect-cell nuclei by an active process of nuclear import via a nuclear localization signal (NLS)-specific pathway.
Whitefly transmission and efficient ssDNA accumulation of bean golden mosaic geminivirus require functional coat protein.
- 1994
Biology, Environmental Science
Two deletions and a restriction fragment inversion were introduced into the BGMV coat protein gene and all three coat protein mutants produced systemic infections when coinoculated with DNA-B onto Phaseolus vulgaris using electric discharge particle acceleration "particle gun" but none of the mutants were transmitted by whiteflies.
Nucleotide sequence of cassava latent virus DNA
- 1983
Biology
Results show that CLV DNA comprises two similar-sized molecular species with a common region encompassing almost 200 nucleotides, and is a fundamental step towards the investigation of the mode of replication of this group of viruses.
The Bipartite Geminivirus Coat Protein Aids BR1 Function in Viral Movement by Affecting the Accumulation of Viral Single-Stranded DNA
- 1998
Biology
The model for SqLCV movement is extended, demonstrating that coat protein affects viral movement through its ability to induce the accumulation of replicated viral ssDNA genomes.
Genetic analysis of tomato golden mosaic virus: the coat protein is not required for systemic spread or symptom development
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Biology
Investigating the role of the coat protein in TGMV replication reports here that its coding sequence may be interrupted or substantially deleted without loss of infectivity, however, certain coat‐protein mutants showed reproducible delays in time of symptom appearance as well as reduced symptom development, when inoculated onto transgenic Nicotiana benthamiana plants containing the T GMV B component.
The geminivirus BR1 movement protein binds single-stranded DNA and localizes to the cell nucleus.
- 1994
Biology, Environmental Science
The biochemical properties and cellular locations of BR1 andBL1 suggest a model for SqLCV movement whereby BR1 is involved in the shuttling of the genome in and/or out of the nucleus and BL1 acts at the plasma membrane/cell wall to facilitate viral movement across cell boundaries.
A Viral Movement Protein as a Nuclear Shuttle (The Geminivirus BR1 Movement Protein Contains Domains Essential for Interaction with BL1 and Nuclear Localization)
- 1996
Biology
It is proposed that BR1 functions as a nuclear shuttle protein, transporting the viral single-stranded DNA to and from the nucleus as a complex that is recognized by BL1 for movement to adjacent cells and demonstrated that the C-terminal 86 amino acids of BR1 contains a domain(s) essential for its interaction with BL1.