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Biological and molecular characterization of a new carlavirus isolated from an Aconitum sp.
Year:
2000
Source of publication :
Phytopathology
Authors :
Gera, Abdullah
;
.
Rosner, Arie
;
.
Volume :
90
Co-Authors:
Cohen, J., Department of Virology, Agricultural Research Organization, Volcani Center, P.O. Box 6, Bet Dagan 50250, Israel
Zeidan, M., Plant Protect. and Inspection Serv., Ministry of Agriculture, Bet Dagan 50250, Israel
Rosner, A., Department of Virology, Agricultural Research Organization, Volcani Center, P.O. Box 6, Bet Dagan 50250, Israel
Gera, A., Department of Virology, Agricultural Research Organization, Volcani Center, P.O. Box 6, Bet Dagan 50250, Israel
Facilitators :
From page:
340
To page:
344
(
Total pages:
5
)
Abstract:
A new virus was isolated from symptomless Aconitum napellus plants. The virus, for which the name Aconitum latent virus (AcLV) is proposed, has flexuous particles 640 nm in length. The experimental host range was limited to Nicotiana clevelandii. Electron microscopy studies of ultrathin sections of infected A. napellus tissues revealed the presence of elongated virus particles. No inclusion bodies characteristic of potyvirus infection were observed. AcLV was purified from naturally infected A. napellus by cesium chloride step gradient centrifugation. In sodium dodecyl sulfate-polyacrylamide gel electrophoresis of dissociated purified virus preparations, a major protein component with a molecular mass of 35 kDa was observed. Diagnostic antibodies that could specifically bind to virus particles were produced. The 5' terminus (620 nucleotides) of the viral RNA was cloned and sequenced. It comprised 71 nucleotides from the untranslated 5' terminus and 549 nucleotides of an open reading frame encoding 183 amino acids. Comparison of the predicted amino acid sequence with those of other plant viruses revealed 40 to 60% identity with several carlaviruses. Based on particle morphology, absence of inclusion bodies in ultrathin sections, the relative molecular weight of the coat protein, the nucleotide sequence, and predicted amino acid homology, it is suggested that this virus belongs to the carlavirus group.
Note:
Related Files :
host range
Open reading frame
SDS polyacrylamide gel electrophoresis
sequence homology
virus infection
virus RNA
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DOI :
Article number:
Affiliations:
Database:
Scopus
Publication Type:
article
;
.
Language:
English
Editors' remarks:
ID:
28712
Last updated date:
02/03/2022 17:27
Creation date:
17/04/2018 00:41
Scientific Publication
Biological and molecular characterization of a new carlavirus isolated from an Aconitum sp.
90
Cohen, J., Department of Virology, Agricultural Research Organization, Volcani Center, P.O. Box 6, Bet Dagan 50250, Israel
Zeidan, M., Plant Protect. and Inspection Serv., Ministry of Agriculture, Bet Dagan 50250, Israel
Rosner, A., Department of Virology, Agricultural Research Organization, Volcani Center, P.O. Box 6, Bet Dagan 50250, Israel
Gera, A., Department of Virology, Agricultural Research Organization, Volcani Center, P.O. Box 6, Bet Dagan 50250, Israel
Biological and molecular characterization of a new carlavirus isolated from an Aconitum sp.
A new virus was isolated from symptomless Aconitum napellus plants. The virus, for which the name Aconitum latent virus (AcLV) is proposed, has flexuous particles 640 nm in length. The experimental host range was limited to Nicotiana clevelandii. Electron microscopy studies of ultrathin sections of infected A. napellus tissues revealed the presence of elongated virus particles. No inclusion bodies characteristic of potyvirus infection were observed. AcLV was purified from naturally infected A. napellus by cesium chloride step gradient centrifugation. In sodium dodecyl sulfate-polyacrylamide gel electrophoresis of dissociated purified virus preparations, a major protein component with a molecular mass of 35 kDa was observed. Diagnostic antibodies that could specifically bind to virus particles were produced. The 5' terminus (620 nucleotides) of the viral RNA was cloned and sequenced. It comprised 71 nucleotides from the untranslated 5' terminus and 549 nucleotides of an open reading frame encoding 183 amino acids. Comparison of the predicted amino acid sequence with those of other plant viruses revealed 40 to 60% identity with several carlaviruses. Based on particle morphology, absence of inclusion bodies in ultrathin sections, the relative molecular weight of the coat protein, the nucleotide sequence, and predicted amino acid homology, it is suggested that this virus belongs to the carlavirus group.
Scientific Publication
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