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The p27 protein is present at one end of citrus tristeza virus particles
Year:
1996
Source of publication :
Phytopathology
Authors :
Ashoulin, Lilach
;
.
Bar-Joseph, Moshe
;
.
Franck, Andre
;
.
Mawassi, Munir
;
.
Volume :
86
Co-Authors:
Febres, V.J., Plant Pathology Department, University of Florida, Gainesville, FL 32611-0680, United States
Ashoulin, L., S. Tolkowsky Laboratory, Department of Virology, Volcani Center, Bet Dagan 50250, Israel
Mawassi, M., S. Tolkowsky Laboratory, Department of Virology, Volcani Center, Bet Dagan 50250, Israel
Frank, A., S. Tolkowsky Laboratory, Department of Virology, Volcani Center, Bet Dagan 50250, Israel
Bar-Joseph, M., S. Tolkowsky Laboratory, Department of Virology, Volcani Center, Bet Dagan 50250, Israel
Manjunath, K.L., Citrus Research and Education Center, University of Florida, Lake Alfred, FL 33850, United States
Lee, R.F., Citrus Research and Education Center, University of Florida, Lake Alfred, FL 33850, United States
Niblett, C.L., Plant Pathology Department, University of Florida, Gainesville, FL 32611-0680, United States
Facilitators :
From page:
1331
To page:
1335
(
Total pages:
5
)
Abstract:
Sequence analysis of the citrus tristeza closterovirus (CTV) genome indicated the presence of an open reading frame upstream of the capsid protein (CP) gene that codes for a protein of 27 kDa (p27). p27 is a diverged CP, showing 41% deduced amino acid sequence similarity with the CP. Previous reports indicated that CTV particles were composed of a single protein, the CP. However, adsorption of extracts of CTV-infected tissue to enzyme-linked immunosorbent assay (ELISA) plates with p27-specific antibodies and their detection with antibodies to the CP suggested that the p27 and CP were associated. The association of p27 with the virion was indicated by positive reverse transcription and polymerase chain reaction results using the p27- adsorbed material and two sets of primer pairs corresponding to the 5' and 3' ends of the CTV genome. Immunoelectron microscopy demonstrated that p27 antibodies decorated a 75- to 85-nm-long segment at one end of the virus particle, but not the main portion of the particle, for both a Florida and an Israeli strain of CTV. Conversely, the CP antibodies decorated the majority of the virus particle, but not a terminal 75- to 85-nm-long segment. Both normal length (about 2,000 nm) and shorter particles contained the p27 segment.
Note:
Related Files :
Citrus
Citrus tristeza
Citrus tristeza virus
Closterovirus
electron microscopy
Miridae
Show More
Related Content
More details
DOI :
Article number:
0
Affiliations:
Database:
Scopus
Publication Type:
article
;
.
Language:
English
Editors' remarks:
ID:
21908
Last updated date:
02/03/2022 17:27
Creation date:
16/04/2018 23:47
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Scientific Publication
The p27 protein is present at one end of citrus tristeza virus particles
86
Febres, V.J., Plant Pathology Department, University of Florida, Gainesville, FL 32611-0680, United States
Ashoulin, L., S. Tolkowsky Laboratory, Department of Virology, Volcani Center, Bet Dagan 50250, Israel
Mawassi, M., S. Tolkowsky Laboratory, Department of Virology, Volcani Center, Bet Dagan 50250, Israel
Frank, A., S. Tolkowsky Laboratory, Department of Virology, Volcani Center, Bet Dagan 50250, Israel
Bar-Joseph, M., S. Tolkowsky Laboratory, Department of Virology, Volcani Center, Bet Dagan 50250, Israel
Manjunath, K.L., Citrus Research and Education Center, University of Florida, Lake Alfred, FL 33850, United States
Lee, R.F., Citrus Research and Education Center, University of Florida, Lake Alfred, FL 33850, United States
Niblett, C.L., Plant Pathology Department, University of Florida, Gainesville, FL 32611-0680, United States
The p27 protein is present at one end of citrus tristeza virus particles
Sequence analysis of the citrus tristeza closterovirus (CTV) genome indicated the presence of an open reading frame upstream of the capsid protein (CP) gene that codes for a protein of 27 kDa (p27). p27 is a diverged CP, showing 41% deduced amino acid sequence similarity with the CP. Previous reports indicated that CTV particles were composed of a single protein, the CP. However, adsorption of extracts of CTV-infected tissue to enzyme-linked immunosorbent assay (ELISA) plates with p27-specific antibodies and their detection with antibodies to the CP suggested that the p27 and CP were associated. The association of p27 with the virion was indicated by positive reverse transcription and polymerase chain reaction results using the p27- adsorbed material and two sets of primer pairs corresponding to the 5' and 3' ends of the CTV genome. Immunoelectron microscopy demonstrated that p27 antibodies decorated a 75- to 85-nm-long segment at one end of the virus particle, but not the main portion of the particle, for both a Florida and an Israeli strain of CTV. Conversely, the CP antibodies decorated the majority of the virus particle, but not a terminal 75- to 85-nm-long segment. Both normal length (about 2,000 nm) and shorter particles contained the p27 segment.
Scientific Publication
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