A New Host Record: Strawberry Latent Ringspot Virus Isolated From Flowering Cherry.

Everett, K.R.; Milne, K. S.; Forster, R. L. S.

doi:10.1071/app9940011

Cited by 7 publications

(4 citation statements)

References 19 publications

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“…The larger coat protein of SLRV has 388 amino acids and an Mr of 43K, and the smaller 235 amino acid protein has an M r of 27K. These values are similar to the reported sizes of the coat proteins of SLRV of M r 44K and 29K (Murant, 1974) and 45K and 30K (Everett et al, 1994) determined from purified virus particles on 6 to 10 % and 12.5 % polyacrylamide gels respectively.…”

Section: Tnca(c/t)ga(a/g)ga(c/t)(c/t)tngtnccsupporting

confidence: 74%

“…Some isolates of SLRV also have a 'middle' component of 95S to 99S (Gallitelli et al, 1982). The genome of SLRV consists of two RNA species of 9.0 and 5-15 kb (Everett et al, 1994) that are translated as polyproteins (Hellen et al, 1991). The RNAs are polyadenylated at their 3' termini (Mayo et al, 1979), and contain a protein covalently bound to their 5' termini (Mayo et al, 1982).…”

mentioning

confidence: 99%

“…The SLRV strain was obtained from flowering cherry (Everett et aL, 1993) and was maintained in cucumber and purified as described (Everett et al, 1994). SLRV from flowering cherry reacted homologously with antiserum to SLRV obtained from the Scottish Crop Research Institute, Dundee, U.K. RNA was extracted from purified virus according to Everett et al (1994).…”

mentioning

confidence: 99%

“…SLRV from flowering cherry reacted homologously with antiserum to SLRV obtained from the Scottish Crop Research Institute, Dundee, U.K. RNA was extracted from purified virus according to Everett et al (1994).…”

mentioning

confidence: 99%

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Nucleotide sequence of the coat protein genes of strawberry latent ringspot virus: lack of homology to the nepoviruses and comoviruses

Everett

Milne

Forster

1994

Journal of General Virology

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The sequence of the 3'-terminal 2424 nucleotides of RNA-2 of the flowering cherry strain of strawberry latent ringspot virus (SLRV) was determined from eDNA clones. The sequence contains a reading frame in the virus-sense strand of 2070 nucleotides, a 3' untranslated region of 552 nucleotides and a T-terminal poly(A) tract. The positions of the two coat proteins of SLRV within the reading frame were determined from sequence data obtained by N-terminal sequencing using Edman degradation. The larger coat protein with an M r of 43K is located 5' of the smaller coat protein of 27K, and the two proteins are apparently cleaved at a Ser-Gly bond. Although there are numerous similarities between SLRV and the nepoviruses and comoviruses, there is no significant homology between the SLRV coat proteins and the coat proteins of either group. Furthermore, the hydropathy profiles of the SLRV coat proteins are unlike those of either group. No comparisons could be made with the fabaviruses owing to lack of sequencing information. This lack of homology suggests that SLRV is more distantly related to the nepoviruses and comoviruses than has been considered previously.

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Section: Tnca(c/t)ga(a/g)ga(c/t)(c/t)tngtnccsupporting

confidence: 74%

mentioning

confidence: 99%

mentioning

confidence: 99%

mentioning

confidence: 99%

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Nucleotide sequence of the coat protein genes of strawberry latent ringspot virus: lack of homology to the nepoviruses and comoviruses

Everett

Milne

Forster

1994

Journal of General Virology

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Prunus serrulata (Oriental flowering cherry)

Sastry¹,

Mandal²,

Scott³

et al. 2019

Encyclopedia of Plant Viruses and Viroids

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Some coat protein constituents from strawberry latent ringspot virus expressed in transgenic tobacco protect plants against systematic invasion following root inoculation by nematode vectors

et al. 1996

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The coding sequences in RNA2 for the coat proteins (CP) of strawberry latent ringspot virus (SLRSV) were modified and amplified using polymerase chain amplification reactions (PCR) to facilitate their expression in Agrobacterium tumefaciens-transformed Nicotiana tabacum Xanthi-nc. The coding sequences for the smaller capsid protein (S, 29kDa) and that for the theoretical precursor of L and S (P, 73kDa) had ATG 'initiation' codon sequences added at the 5'-proximal Ser/Gly (S/G) cleavage site in the unmodified sequence. The sequence coding for the larger of the two proteins of mature SLRSV capsids (L, 44kDa) had an ATG codon added at its 5' S/G site and a TAG 'stop' codon sequence added at the 3~-proximal S/G site. The P, L and S proteins were expressed in planta to a maximum concentration of 0.01% of total extractable proteins but did not assemble into virus-like particles. When challenged by mechanical inoculation with virus particles or viral RNA, and compared with control plants, tobacco plants (primary transgenic clones or S 1 and $2, kanamycin-resistant seedlings) expressing the virus capsid subunits separately, or their precursor, decreased the accumulation of SLRSV particles in inoculated leaves and fewer plants became invaded systemically. In experiments in which the roots of seedlings were exposed to SLRSV-carrying vector nematodes (Xiphinema diversicaudatum), SLRSV was detected in the roots of non-transformed control tobacco plants (6/20) and in transgenic tobacco expressing the L protein (7/40), but not in any of 25 tobacco plants expressing the S protein or in 35 expressing the P protein. This is the second example of CP-mediated resistance to virus inoculation by nematode vectors.

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A New Host Record: Strawberry Latent Ringspot Virus Isolated From Flowering Cherry.

Cited by 7 publications

References 19 publications

Nucleotide sequence of the coat protein genes of strawberry latent ringspot virus: lack of homology to the nepoviruses and comoviruses

Nucleotide sequence of the coat protein genes of strawberry latent ringspot virus: lack of homology to the nepoviruses and comoviruses

Prunus serrulata (Oriental flowering cherry)

Some coat protein constituents from strawberry latent ringspot virus expressed in transgenic tobacco protect plants against systematic invasion following root inoculation by nematode vectors

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