ArticleVirus genes2001
The product of ORF III in cauliflower mosaic virus interacts with the viral coat protein through its C-terminal proline rich domain.
Article in Virus genes, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed.
- Complete genome sequence of pueraria virus A, a new member of the genus Caulimovirus.Archives of virology · 2022Article
- Efficient immunodiagnosis of3 Biotech · 2018Article
- Article
- Association of the P6 protein of Cauliflower mosaic virus with plasmodesmata and plasmodesmal proteins.Plant physiology · 2014Article
- Cauliflower mosaic virus major inclusion body protein interacts with the aphid transmission factor, the virion-associated protein, and gene VII product.Virus research · 2012Article
- Intracellular transport of plant viruses: finding the door out of the cell.Molecular plant · 2011Review
- Structural insights into the molecular mechanisms of cauliflower mosaic virus transmission by its insect vector.Journal of virology · 2010Article
- Plant virus transmission from the insect point of view.Proceedings of the National Academy of Sciences of the United States of America · 2007Article
- A coiled-coil interaction mediates cauliflower mosaic virus cell-to-cell movement.Proceedings of the National Academy of Sciences of the United States of America · 2005Article
- The cauliflower mosaic virus virion-associated protein is dispensable for viral replication in single cells.Journal of virology · 2002Article
- Tetramerization is a conserved feature of the virion-associated protein in plant pararetroviruses.Journal of virology · 2001Article
Corrections and comments
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Authors and funding
6 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Using the yeast two-hybrid system, we show that the ORF III product of cauliflower mosaic virus (pIII) interacts through its C-terminus with the viral coat protein. The last five amino acids of pIII were essential for the interaction and virus infectivity. Deletion of the last three amino acids or the mutation F129A decreased the strength of the interaction by 90%. We further show that pIII is closely associated with virus particles found in the inclusion bodies of infected plants but not in viral particles released from the inclusion bodies by urea treatment.
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