The 30-Kilodalton Gene Product of Tobacco Mosaic Virus Potentiates Virus Movement

Deom, C. M.; Oliver, Melvin J.; Beachy, Roger N.

doi:10.1126/science.237.4813.389

Cited by 413 publications

(242 citation statements)

References 43 publications

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“…With respect to the 58K and 48K proteins, this result was not unexpected. These proteins show a limited homology with the 30K transport protein of tobamoviruses (Meyer et al, 1986;Deom et al, 1987;Meshi et al, 1987). Furthermore the 48K protein is found in the membrane fraction of infected leaves (Wellink et al, 1987) and recent results with immunogold labelling of sections of infected leaves with anti-48K serum have revealed an association of this protein with tubular structures protruding from the cell wall (J. van Lent, unpublished results).…”

Section: Discussionmentioning

confidence: 94%

Cell-to-cell Transport of Cowpea Mosaic Virus Requires Both the 58K/48K Proteins and the Capsid Proteins

Wellink

Kammen

1989

Journal of General Virology

119

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SUMMARYInsertions and deletions have been introduced into an infectious cDNA clone of M RNA of cowpea mosaic virus (CPMV), in the coding regions of the 58K/48K and capsid proteins. Transcripts derived from these mutant clones appeared to be replicated in cowpea protoplasts as detected by immunofluorescent staining and Northern blotting. However in cowpea plants, mutations in either region restricted the replication of the viral RNAs to the inoculated cells and thus prevented a successful systemic infection of the plant. These results indicate that the M RNA-encoded 58K/48K proteins are involved in cell-to-cell transport of CPMV, and that the virus can spread only if the RNA is encapsidated in particles.

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Section: Discussionmentioning

confidence: 94%

Cell-to-cell Transport of Cowpea Mosaic Virus Requires Both the 58K/48K Proteins and the Capsid Proteins

Wellink

Kammen

1989

Journal of General Virology

119

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“…Transgenic plants that accumulate the MP of TMV can complement mutants of TMV that do not produce functional MP (Deom et al, 1987;Holt and Beachy, 1991). The coat protein (CP) is not required for cell-to-cell movement (Dawson et al, 1988), although it is required for systemic spread in most hosts (Dawson, 1992).…”

Section: Introductionmentioning

confidence: 99%

Domains of the TMV movement protein involved in subcellular localization

et al. 1998

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SummaryTo identify and map functionally important regions of the tobacco mosaic virus movement protein, deletions of three amino acids were introduced at intervals of 10 amino acids throughout the protein. Mutations located between amino acids 1 and 160 abolished the capacity of the protein to transport virus from cell to cell, while some of the mutations in the C-terminal third of the protein permitted function. Despite extensive tests, no examples were found of intermolecular complementation between mutants, suggesting that function requires each movement protein molecule to be fully competent. Many of the mutants were fused to green fluorescent protein, and their subcellular localizations were determined by fluorescence microscopy in infected plants and protoplasts. Most mutants lost the ability to accumulate in one or more of the multiple subcellular sites targeted by wild-type movement protein, suggesting that specific functional domains were disrupted. The order in which accumulation at subcellular sites occurs during infection does not represent a targeting pathway. Association of the movement protein with microtubules or with plasmodesmata can occur in the absence of other associations. The region of the protein around amino acids 9-11 may be involved in targeting the protein to cortical bodies (probably associated with the endoplasmic reticulum) and to plasmodesmata. The region around residues 49-51 may be involved in co-alignment of the protein with microtubules. The region around residues 88-101 appears to play a role in targeting to both the cortical bodies and microtubules. Thus, the movement protein contains independently functional domains.

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“…A part of the putative 34.3K protein of PPV-NAT was found to be slightly homologous to the 30K protein of tobacco mosaic virus (TMV; Meshi et aL, 1982). Deom et al (1987) demonstrated that expression of the 30K protein of TMV in transgenic tobacco plants could play a role in cell-to-cell spread during virus infection. This suggests that the 34-3K protein could have a similar function.…”

Section: Coding Regionsmentioning

confidence: 99%

The Complete Nucleotide Sequence of Plum Pox Virus RNA

Maiß¹,

Timpe²,

Brisske³

et al. 1989

Journal of General Virology

208

143

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SUMMARYThe complete nucleotide sequence of the RNA of an aphid non-transmissible plum pox virus (PPV-NAT) isolate has been determined from five overlapping cDNA clones, cDNA prepared by primer extension was used to determine the 5' terminus. The assembled RNA is 9741 nucleotides in length, excluding a 3' terminal poly(A) sequence. One large open reading frame starts at nucleotide positions 36 to 38 and is terminated with an UAG codon at positions 9522 to 9524. The putative start codon is located at positions 147 to 149. The encoded polyprotein has a predicted Mr of 353"8K. Comparison of cistrons from tobacco vein mottling virus and tobacco etch virus with those predicted for PPV-NAT indicated a similar genome organization. A highly conserved sequence of 12 nucleotides was found in the 5' non-coding region of these three potyviruses. The potential polyadenylation signal from yeast (UAUGU) was found in the 3' non-coding region of PPV-NAT and several other members of the potyvirus group.

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The 30-Kilodalton Gene Product of Tobacco Mosaic Virus Potentiates Virus Movement

Cited by 413 publications

References 43 publications

Cell-to-cell Transport of Cowpea Mosaic Virus Requires Both the 58K/48K Proteins and the Capsid Proteins

Cell-to-cell Transport of Cowpea Mosaic Virus Requires Both the 58K/48K Proteins and the Capsid Proteins

Domains of the TMV movement protein involved in subcellular localization

The Complete Nucleotide Sequence of Plum Pox Virus RNA

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