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Particle properties of blackcurrant reversion associated virus - A new mite-transmitted nepovirus
Tekijät: Susi P, Latvala S, Lehto K, Lemmetty A
Julkaisuvuosi: 1998
Lehti:: Acta Horticulturae
Tietokannassa oleva lehden nimi: 8TH INTERNATIONAL SYMPOSIUM ON SMALL FRUIT VIRUS DISEASES
Lehden akronyymi: ACTA HORTIC
Numero: 471
Aloitussivu: 99
Lopetussivu: 103
Sivujen määrä: 5
ISBN: 90-6605-910-9
ISSN: 0567-7572
DOI: https://doi.org/10.17660/ActaHortic.1998.471.16
Tiivistelmä
Blackcurrant reversion associated virus is the first known mite-transmitted nepovirus. The virus particle is spherical, 27 nm in diameter, and the viral genome is composed of bipartite, single-stranded RNA. The coat protein gene of the virus is located on RNA2, and the coat protein is released from a polyprotein using a unique proteolytic cleavage site (asparagine/serine). The amino acid sequence of the coat protein was analysed and shown to contain three putative asparagine-linked glycosylation sites at the C-terminus of the CP sequence: Asn-X-Thr (where X is any amino acid, amino acids 1 to 3 from the C terminus of GP sequence), Asn-X-Ser (83-85), and Asn-X-Ser (126-128). When secondary structure of CP was created by using the PLOTSTRUCTURE program of Genetics Computer Program (GCG) sequence analysis package program to predict the probable amino acids on the surface of CP, it indicated that two of these glycosylation sites were located on the surface of CP. The possible glycosylation of the CP was analyzed by Alcian blue staining and antibody-based method specific for oxidized hydroxyl groups in glycoconjugates, but no signal for glycosylation of CP was obtained. The surface properties and the possible role of glycosylation sites in mite-transmission of blackcurrant reversion associated nepovirus remain to be determined.
Blackcurrant reversion associated virus is the first known mite-transmitted nepovirus. The virus particle is spherical, 27 nm in diameter, and the viral genome is composed of bipartite, single-stranded RNA. The coat protein gene of the virus is located on RNA2, and the coat protein is released from a polyprotein using a unique proteolytic cleavage site (asparagine/serine). The amino acid sequence of the coat protein was analysed and shown to contain three putative asparagine-linked glycosylation sites at the C-terminus of the CP sequence: Asn-X-Thr (where X is any amino acid, amino acids 1 to 3 from the C terminus of GP sequence), Asn-X-Ser (83-85), and Asn-X-Ser (126-128). When secondary structure of CP was created by using the PLOTSTRUCTURE program of Genetics Computer Program (GCG) sequence analysis package program to predict the probable amino acids on the surface of CP, it indicated that two of these glycosylation sites were located on the surface of CP. The possible glycosylation of the CP was analyzed by Alcian blue staining and antibody-based method specific for oxidized hydroxyl groups in glycoconjugates, but no signal for glycosylation of CP was obtained. The surface properties and the possible role of glycosylation sites in mite-transmission of blackcurrant reversion associated nepovirus remain to be determined.
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