An analysis of the complete sequence of a sugarcane bacilliform virus genome infectious to banana and rice

Bouhida, M; Lockhart, B. E. L.; Olszewski, Neil E.

doi:10.1099/0022-1317-74-1-15

Cited by 127 publications

(89 citation statements)

References 27 publications

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“…The strongest area of homology lies between amino acids 120 and 190. This region has been shown by deletion analysis to comprise the P1 RNA binding domain (Thomas and Maule, 1995) and is also strongly conserved in wider comparisons between caulimoviruses and badnaviruses (Bouhida et al, 1993). Whereas there was generally less conservation around the C terminus, the last 20 amino acids comprised a structure with significantly higher conservation than the region (amino acids 278 to 306) immediately before it.…”

Section: Amino Acid Sequence Comparison With Other Caulimovirus Mpsmentioning

confidence: 91%

Identification of structural domains within the cauliflower mosaic virus movement protein by scanning deletion mutagenesis and epitope tagging.

Thomas

Maule

1995

Plant Cell

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Plant viruses encode proteins that mediate their movement from cell to cell through plasmodesmata. Currently, the mechanisms of action of these movement proteins (MPs) can be divided broadly into two types, requiring or not requiring the presence of viral capsid protein. Cauliflower mosaic virus encodes a multifunctional MP (Pl) that modifies plasmodesmata through the formation of tubules that contain virus particles. To investigate the structure of P1,26 small deletions (scanning deletions) were used to characterize regions of P1 essential for full biological activity. These deletions identified an N-terminal region and a region close to but not at the C terminus as domains that could tolerate manipulation, although gross deletions of either domain abolished infection. In sequence comparisons with other caulimovirus MPs, these regions coincided with the areas of least amino acid homology. Epitope tags inserted into either of these regions were stably maintained in systemic infections, and in extracts from infected plants, tagged P1 was detected on immunoblots. We predicted that, from the hypenrariability of these regions, they would be located on the surface of the native P1 structure. lmmunofluorescence of P1-specific tubules formed on the surface of infected protoplasts confirmed that the N-terminal and C terminus-proximal regions were exposed on the surface of the P1 tubule subunit. These findings establish a structure for P1 that is likely to be applicable to other tubule-forming MPs.

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Section: Amino Acid Sequence Comparison With Other Caulimovirus Mpsmentioning

confidence: 91%

Identification of structural domains within the cauliflower mosaic virus movement protein by scanning deletion mutagenesis and epitope tagging.

Thomas

Maule

1995

Plant Cell

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“…BSV presents a high degree of heterogeneity among isolates . It is a member of the badnavirus group (Lockhart, 1990) together with Rice tungro bacilliform virus (Hay et al, 1991), Commelina yellow mottle virus (Medberry et al, 1990), Sugarcane bacilliform virus (Bouhida et al, 1993) and Cacao swollen shoot virus (Hagen et al, 1993). This non-enveloped virus contains a circular dsDNA genome of 7.4 kb (Harper and Hull, 1998).…”

Section: Introductionmentioning

confidence: 99%

The acyclic nucleoside phosphonate analogues, adefovir, tenofovir and PMEDAP, efficiently eliminate banana streak virus from banana (Musa spp.)

Helliot

Panis

Frison³

et al. 2003

Antiviral Research

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We report that the anti-retroviral and anti-hepadnavirus molecules, adefovir, tenofovir and 9-(2-phosphonomethoxyethyl)-2,6-diaminopurine (PMEDAP), efficiently eradicate the episomal form of Banana streak virus (BSV) from banana plants. Up to 90% of plants regenerated from BSV-infected highly proliferating meristems were virus free following a 6-month treatment period with 10 g/ml (a non-phytotoxic concentration) of either compounds.

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“…The largest of these proteins is a polyprotein that yields several proteins including the virus coat, an aspartic protease involved in processing the polyprotein, and enzymes with reverse transcriptase and ribonuclease H activities that are involved in virus replication. Although little is known about the mechanism of badnavirus cell-to-cell movement, there is limited sequence similarity between the N terminus of the polyprotein and known movement proteins (Bouhida et al, 1993), and mutations affecting this region block cell-to-cell spread of the virus but do not affect its replication (Tzafrir et al, 1997), suggesting that this portion of the polyprotein gives rise to the CoYMV movement protein. Here we report the observation of CoYMV-containing tubules both in fractionated cell-free extracts of infected leaves and in situ.…”

mentioning

confidence: 99%

Tubules containing virions are present in plant tissues infected with Commelina yellow mottle badnavirus.

Cheng

Tzafrir

Lockhart

et al. 1998

Journal of General Virology

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In establishing a systemic infection, plant viruses must overcome the barrier to cell-to-cell movement that the plant cell wall presents. Two mechanisms of cell-to-cell movement that take advantage of plasmodesmatal connections between cells have been recognized (for reviews see Maule, 1991 ;Lucas & Gilbertson, 1994). One mechanism involves a specific virus movement protein that increases the gating limit of plasmodesmata and is thought to participate in the formation of an RNA-movement protein-nucleoprotein complex that is capable of passing through the modified plasmodesmata. The second mechanism involves the formation of virus-conducting tubular structures that extend between the cytoplasms of adjacent cells. These tubules are composed, at least partly, of virus-encoded movement proteins and their formation is not dependent on the presence of the cell wall, plasmodesmata or other virus gene products (Perbal et al., 1993 ; Kasteel et al., 1996Kasteel et al., , 1997.Badnaviruses are plant pararetroviruses that encapsidate 7n5-8 kb circular double-stranded DNA in non-enveloped bacilliform virions. Commelina yellow mottle badnavirus (CoYMV) is the type member for the genus (Lockhart & Olszewski, 1994). Generally, badnaviruses encode three proteins. The largest of these proteins is a polyprotein that yields several proteins including the virus coat, an aspartic protease involved in processing the polyprotein, and enzymes with reverse transcriptase and ribonuclease H activities that are involved in virus replication. Although little is known about the mechanism of badnavirus cell-to-cell movement, there is limited sequence similarity between the N terminus of the polyprotein and known movement proteins (Bouhida et al., 1993), and mutations affecting this region block cell-to-cell spread of the virus but do not affect its replication (Tzafrir et al., 1997), suggesting that this portion of the polyprotein gives rise to the CoYMV movement protein. Here we report the observation of CoYMV-containing tubules both in fractionated cell-free extracts of infected leaves and in situ. In addition, immunogold labelling demonstrates that the tubules are composed, at least partly, of CoYMV movement protein. This report describes a likely mechanism of cell-to-cell movement of badnaviruses, and provides additional evidence that this mechanism, which has been reported primarily for viruses with isometric particles, may also operate in the case of viruses with elongated particles (Kasteel et al., 1997).Cell-free extracts of CoYMV-infected Commelina diffusa leaf tissues were prepared in phosphate buffer (200 mM phosphate buffer pH 6n0, 4 % PEG 8000, 0n5 % 2-mercaptoethanol, 0n5 % sodium sulfite, 10 mM EDTA). The extracts were layered over a 5 ml cushion of 30 % sucrose in 20 mM phosphate buffer pH 6n0 containing 250 mM NaCl (PN buffer) and the virions and tubules were pelleted by centrifugation in a Beckman 50.2 Ti rotor at 35 000 r.p.m. for 70 min. The resulting pellet was resuspended in 0n5-1 ml PN buffer and layered onto a prefor...

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An analysis of the complete sequence of a sugarcane bacilliform virus genome infectious to banana and rice

Cited by 127 publications

References 27 publications

Identification of structural domains within the cauliflower mosaic virus movement protein by scanning deletion mutagenesis and epitope tagging.

Identification of structural domains within the cauliflower mosaic virus movement protein by scanning deletion mutagenesis and epitope tagging.

The acyclic nucleoside phosphonate analogues, adefovir, tenofovir and PMEDAP, efficiently eliminate banana streak virus from banana (Musa spp.)

Tubules containing virions are present in plant tissues infected with Commelina yellow mottle badnavirus.

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