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The p20 gene product of Citrus tristeza virus accumulates in the amorphous inclusion bodies
Year:
2000
Source of publication :
Virology
Authors :
Bar-Joseph, Moshe
;
.
Mawassi, Munir
;
.
Volume :
274
Co-Authors:

Gowda, S.
Satyanarayana, T.
Davis, C.L.
Navas-Castillo, J.
Albiach-Marti, M.R.
Mawassi, M.
Valkov, N.
Bar-Joseph, M.
Moreno, P.
Dawson, W.O.

Facilitators :
From page:
246
To page:
254
(
Total pages:
9
)
Abstract:
Citrus tristeza virus (CTV) has 10 3' open reading frames (ORFs) of unknown function except for the two coat proteins. The highest produced subgenomic RNAs are those of the major coat protein gene (p25) and the 3' most genes, p20 and p23. The proteins from three ORFs, p25, p27, and p20, were examined in the yeast two-hybrid assay for the interactions between themselves and to one another. The p20 protein exhibited a high affinity for itself, suggesting that it might aggregate in infected cells. The cytopathotogy of CTV infections includes characteristic paracrystalline and amorphous inclusions in the phloem elements of infected citrus. Polyclonal antiserum raised against the bacterial expressed p20 gene product detected a protein of ~22-23 kDa, which accumulated to relatively high levels in CTV-infected citrus, but not in healthy citrus. Immunogold localization using antibodies to p20 protein showed strong and specific labeling of the amorphous inclusion bodies present in CTV-infected cells. Mesophyll protoplasts of Nicotiana benthamiana transfected with a CTV mutant containing the green fluorescent protein (GFP) ORF fused in-frame to the 3' end of p20 protein ORF expressed high levels of GFP. The fusion protein was concentrated in one specific area in the cytoplasm and lacked an organized shape. Accumulation of high levels of p20 protein in infected tissue, specific localization of the p20-GFP fusion protein, immunolocalization of p20 protein into amorphous inclusions, and strong homologous p20 protein-p20 protein interactions in the yeast-two-hybrid assay suggest that the p20 protein of CTV is a major component of the amorphous inclusion bodies present in CTV-infected celts. (C) 2000 Academic Press.
Note:
Related Files :
cytopathology
mutation
Plant Diseases
protein localization
protein p25
Protoplasts
unclassified drug
virus RNA
Show More
Related Content
More details
DOI :
10.1006/viro.2000.0413
Article number:
0
Affiliations:
Database:
Scopus
Publication Type:
article
;
.
Language:
English
Editors' remarks:
ID:
30488
Last updated date:
02/03/2022 17:27
Creation date:
17/04/2018 00:55
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Scientific Publication
The p20 gene product of Citrus tristeza virus accumulates in the amorphous inclusion bodies
274

Gowda, S.
Satyanarayana, T.
Davis, C.L.
Navas-Castillo, J.
Albiach-Marti, M.R.
Mawassi, M.
Valkov, N.
Bar-Joseph, M.
Moreno, P.
Dawson, W.O.

The p20 gene product of Citrus tristeza virus accumulates in the amorphous inclusion bodies
Citrus tristeza virus (CTV) has 10 3' open reading frames (ORFs) of unknown function except for the two coat proteins. The highest produced subgenomic RNAs are those of the major coat protein gene (p25) and the 3' most genes, p20 and p23. The proteins from three ORFs, p25, p27, and p20, were examined in the yeast two-hybrid assay for the interactions between themselves and to one another. The p20 protein exhibited a high affinity for itself, suggesting that it might aggregate in infected cells. The cytopathotogy of CTV infections includes characteristic paracrystalline and amorphous inclusions in the phloem elements of infected citrus. Polyclonal antiserum raised against the bacterial expressed p20 gene product detected a protein of ~22-23 kDa, which accumulated to relatively high levels in CTV-infected citrus, but not in healthy citrus. Immunogold localization using antibodies to p20 protein showed strong and specific labeling of the amorphous inclusion bodies present in CTV-infected cells. Mesophyll protoplasts of Nicotiana benthamiana transfected with a CTV mutant containing the green fluorescent protein (GFP) ORF fused in-frame to the 3' end of p20 protein ORF expressed high levels of GFP. The fusion protein was concentrated in one specific area in the cytoplasm and lacked an organized shape. Accumulation of high levels of p20 protein in infected tissue, specific localization of the p20-GFP fusion protein, immunolocalization of p20 protein into amorphous inclusions, and strong homologous p20 protein-p20 protein interactions in the yeast-two-hybrid assay suggest that the p20 protein of CTV is a major component of the amorphous inclusion bodies present in CTV-infected celts. (C) 2000 Academic Press.
Scientific Publication
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