Cauliflower Mosaic Virus: A Plant Gene Vector

Author(s):  
B. Gronenborn
2005 ◽  
Vol 18 (3) ◽  
pp. 212-219 ◽  
Author(s):  
John Cawly ◽  
Anthony B. Cole ◽  
Lóránt Király ◽  
Wenping Qiu ◽  
James E. Schoelz

The P6 protein of Cauliflower mosaic virus (CaMV) W260 elicits a hypersensitive response (HR) on inoculated leaves of Nicotiana edwardsonii. This defense response, common to many plant pathogens, has two key characteristics, cell death within the initially infected tissues and restriction of the pathogen to this area. We present evidence that a plant gene designated CCD1, originally identified in N. bigelovii, can selectively block the cell death pathway during HR, whereas the resistance pathway against W260 remains intact. Suppression of cell death was evident not only macroscopically but also microscopically. The suppression of HR-mediated cell death was specific to CaMV, as Tobacco mosaic virus was able to elicit HR in the plants that contained CCD1. CCD1 also blocks the development of a systemic cell death symptom induced specifically by the P6 protein of W260 in N. clevelandii. Introgression of CCD1 from N. bigelovii into N. clevelandii blocked the development of systemic cell death in response to W260 infection but could not prevent systemic cell death induced by Tomato bushy stunt virus. Thus, CCD1 blocks both local and systemic cell death induced by P6 of W260 but does not act as a general suppressor of cell death induced by other plant viruses. Furthermore, experiments with CCD1 provide further evidence that cell death could be uncoupled from resistance in the HR of Nicotiana edwardsonii to CaMV W260.


Author(s):  
Roberto Alers-Velazquez ◽  
Sushant Khandekar ◽  
Clare Muller ◽  
Jennifer Boldt ◽  
Scott Leisner

AbstractLower temperatures delayed development of systemic symptoms by Cauliflower mosaic virus (CaMV) in two different plant hosts. However, lower temperature exposure increased CaMV nucleic acid levels in leaves of systemically-infected turnips. Furthermore, lower temperature altered the formation of aggregates formed by the CaMV major inclusion body (IB) protein, P6. Finally, lower temperature altered the architecture of the actin cytoskeleton. These data may suggest that lower temperatures alter the actin cytoskeleton, facilitating the formation of larger IBs that hold on to their internal virions more strongly than small ones, impairing virus particle release and causing a delay in systemic infection.


2002 ◽  
Vol 15 (10) ◽  
pp. 1050-1057 ◽  
Author(s):  
Yongzhong Li ◽  
Scott M. Leisner

The Cauliflower mosaic virus (CaMV) gene VI product (P6) is a multifunctional protein essential for viral propagation. It is likely that at least some of these functions require P6 self-association. The work described here was performed to confirm that P6 self-associates and to identify domains involved in this interaction. Yeast two-hybrid analyses indicated that full-length P6 self-associates and that this interaction is specific. Additional analyses indicated that at least four independent domains bind to full-length P6. When a central domain (termed domain D3) was removed, these interactions were abolished. However, this deleted P6 was able to bind to the full-length wild-type protein and to isolated domain D3. Viruses lacking domain D3 were incapable of producing a systemic infection. Isolated domain D3 was capable of binding to at least two of the other domains but was unable to self-associate. This suggests that domain D3 facilitates P6 self-association by binding to the other domains but not itself. The presence of multiple domains involved in P6 self-association may help explain the ability of this protein to form the intracellular inclusions characteristic of caulimoviruses.


Virology ◽  
1972 ◽  
Vol 47 (3) ◽  
pp. 694-700 ◽  
Author(s):  
G.G. Conti ◽  
G. Vegetti ◽  
Maria Bassi ◽  
M.Augusta Favali

Virology ◽  
1989 ◽  
Vol 172 (2) ◽  
pp. 451-459 ◽  
Author(s):  
Rebecca Stratford ◽  
Simon N. Covey

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