Serological Analysis of Barley Stripe Mosaic Virus-Encoded Proteins in Infected Barley

Donald, Robert G. K.; Zhou, Huan; Jackson, A.O.

doi:10.1006/viro.1993.1417

Cited by 59 publications

(59 citation statements)

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“…This procedure was previously used to (Donald et al, 1993). A control experiment with the ND18 wild-type strain ( Figure 5) verified our previous conclusion that the yb protein in plants infected with the wild-type virus is partitioned to the soluble (S30) fraction.…”

Section: Mutations Within Yb Alter the Cytoplasmic Localization Of Thsupporting

confidence: 75%

“…Aliquots were fractionated on 15% SDS-polyacrylamide gels and transferred to nitrocellulose (Hybond C-super; Amersham Corp.) as described by Towbin et al (1979). Blots were blocked with TBS (50 mM Tris-HCI, pH 7.4, 200 mM sodium chloride) containing 12.5% (wlv) powdered skimmed milk and 5% (vh) newborn calf serum (Gibco BRL Life Technologies Inc., Gaithersburg, MD) and incubated with diluted mouse anti-BSMV ascites fluid as described by Donald et al (1993). The filters were subsequently washed with TBS and reacted with either goat anti-mouse IgG horseradish peroxidase conjugate or anti-mouse IgG alkaline phosphatase conjugate.…”

Section: Analysis Of Plantsmentioning

confidence: 99%

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The barley stripe mosaic virus gamma b gene encodes a multifunctional cysteine-rich protein that affects pathogenesis.

Donald

Jackson

1994

Plant Cell

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Barley stripe mosaic virus contains seven genes, one of which specifies a 17-kD cysteine-rich protein, yb, that is known to affect virulence. To further characterize the role of yb in pathogenesis, we mutagenized sequences encoding amino acids within two clusters of cysteine and histidine residues in the cysteine-rich domain and a group of basic amino acids located between the clusters and determined the effects of these mutations on the symptom phenotype in barley. Three single amino acid substitutions in cluster 1 and two amino acid exchanges in the basic region caused bleached symptoms associated with pronounced elevations in accumulation of yb pmtein. In contrast, three single amino acid substitutions in cluster 2 and a mutation in the basic motif resulted in attenuated (Ynull") symptoms typical of those produced when the yb gene is deleted. Tissue infected with these "null" mutants accumulated slightly elevated amounts of the yb protein but significantly lower levels of coat protein and the putative movement protein pb. Genetic complementation tests revealed that cluster 1 mutations are dominant over the wild-type yb gene, whereas those in cluster 2 are recessive. These results highlight the pivotal role of yb in pathogenesis and suggest that the two cysteine-rich clusters are functionally distinct and that they affect different aspects of disease development.

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Section: Mutations Within Yb Alter the Cytoplasmic Localization Of Thsupporting

confidence: 75%

Section: Analysis Of Plantsmentioning

confidence: 99%

The barley stripe mosaic virus gamma b gene encodes a multifunctional cysteine-rich protein that affects pathogenesis.

Donald

Jackson

1994

Plant Cell

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“…In the hordeivirus barley stripe mosaic virus (BSMV), TGB3 is produced in approximately one-tenth of the amount of TGB2 (Donald et al, 1993). However, whilst excessive amounts of BSMV or other hordeivirus-like TGB3s interfere with virus replication (Lauber et al, 2005;Lim et al, 2008), there seems to be no such limitation with potexvirus-like TGB3s (Lin et al, 2006; this study).…”

Section: Discussionmentioning

confidence: 72%

Mutation of a chloroplast-targeting signal in Alternanthera mosaic virus TGB3 impairs cell-to-cell movement and eliminates long-distance virus movement

Lim¹,

Vaira²,

Bae

et al. 2010

Journal of General Virology

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Cell-to-cell movement of potexviruses requires coordinated action of the coat protein and triple gene block (TGB) proteins. The structural properties of Alternanthera mosaic virus (AltMV) TGB3 were examined by methods differentiating between signal peptides and transmembrane domains, and its subcellular localization was studied by Agrobacterium-mediated transient expression and confocal microscopy. Unlike potato virus X (PVX) TGB3, AltMV TGB3 was not associated with the endoplasmic reticulum, and accumulated preferentially in mesophyll cells. Deletion and sitespecific mutagenesis revealed an internal signal VL(17,18) of TGB3 essential for chloroplast localization, and either deletion of the TGB3 start codon or alteration of the chloroplastlocalization signal limited cell-to-cell movement to the epidermis, yielding a virus that was unable to move into the mesophyll layer. Overexpression of AltMV TGB3 from either AltMV or PVX infectious clones resulted in veinal necrosis and vesiculation at the chloroplast membrane, a cytopathology not observed in wild-type infections. The distinctive mesophyll and chloroplast localization of AltMV TGB3 highlights the critical role played by mesophyll targeting in virus longdistance movement within plants.

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“…Initial attempts to detect R N A binding were conducted with a BSMV 17 k D a ~b protein derived from pET3a, a T7 R N A polymerase expression vector (Donald et al, 1993). However, we were unable to obtain biochemically active protein from the purified unfused ~b preparations, which tended to form insoluble precipitates.…”

Section: Recombinant B S M V ?B Protein Exhibits Cooperative R N a Bimentioning

confidence: 98%

RNA-binding activities of barley stripe mosaic virus b fusion proteins

Donald

Jackson

1996

Journal of General Virology

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Serological Analysis of Barley Stripe Mosaic Virus-Encoded Proteins in Infected Barley

Cited by 59 publications

References 0 publications

The barley stripe mosaic virus gamma b gene encodes a multifunctional cysteine-rich protein that affects pathogenesis.

The barley stripe mosaic virus gamma b gene encodes a multifunctional cysteine-rich protein that affects pathogenesis.

Mutation of a chloroplast-targeting signal in Alternanthera mosaic virus TGB3 impairs cell-to-cell movement and eliminates long-distance virus movement

RNA-binding activities of barley stripe mosaic virus b fusion proteins

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