Failure of long-distance movement of southern bean mosaic virus in a resistant host is correlated with lack of normal virion formation

Fuentes, Ana Lucía; Hamilton, R. I.

doi:10.1099/0022-1317-74-9-1903

Cited by 33 publications

(12 citation statements)

References 16 publications

(24 reference statements)

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“…In contrast, the presence of virions in systemically infected leaves indicates that encapsidation may be required for long-distance transport. The failure of systemic spread of another sobemovirus, southern bean mosaic virus C, in a resistant host was related to the absence of virion formation (36). Similar observations also have been reported for other plant viruses, including tobacco mosaic virus and red clover necrotic mosaic virus (3,13,14).…”

Section: Discussionsupporting

confidence: 75%

Movement of rice yellow mottle virus between xylem cells through pit membranes

Opalka

Brugidou

Bonneau

et al. 1998

Proc. Natl. Acad. Sci. U.S.A.

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The translocation of rice yellow mottle virus (RYMV) within tissues of inoculated and systemically infected Oryza sativa L. leaves was characterized by Western immunoblotting, Northern blotting, and electron microscopy of thin sections. In inoculated leaves, RYMV RNA and coat protein first were detected at 3 and 5 days postinoculation, respectively. By 6 days postinoculation, RYMV had spread systemically to leaves, and virus particles were observed in most cell types, including epidermal, mesophyll, bundle sheath, and vascular parenchyma cells. Most of the virions accumulated in large crystalline patches in xylem parenchyma cells and sieve elements. Colocalization of a cell wall marker for cellulosic ␤-(1-4)-D-glucans and anti-RYMV antibodies over vessel pit membranes suggests a pathway for virus migration between vessels. We propose that the partial digestion of pit membranes resulting from programmed cell death may permit virus migration through them, concomitant with autolysis. In addition, displacement of the Ca 2؉ from pit membranes to virus particles may contribute to the disruption of the pit membranes and facilitate systemic virus transport.

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Section: Discussionsupporting

confidence: 75%

Movement of rice yellow mottle virus between xylem cells through pit membranes

Opalka

Brugidou

Bonneau

et al. 1998

Proc. Natl. Acad. Sci. U.S.A.

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“…This SCPMV movement limitation was not due to the inability of the bean cells to support virus replication, since SCPMV replicated efficiently in bean protoplasts. It was proposed that the failure of SCPMV to move systemically in bean plants was due to a lack of normal SCPMV virion formation (27). Examination of thin sections of primary bean leaves doubly infected with SHMV and SCPMV revealed the presence of SCPMV virions having a Tϭ1 structure and coat protein clumps in the vacuoles of mesophyll cells.…”

Section: Gene Products and Their Functionsmentioning

confidence: 99%

Sobemoviruses

Tamm

Truve

2000

J Virol

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“…The N-terminus of CfMV and all other sobemovirus CPs are rich in basic amino acid residues and it has been suggested that all sobemoviruses might have a putative NLS in the N-terminal region of CP [19]. Furthermore, sobemovirus particles have been found in the nucleus [16,17,18]. The current study is the first report that provides direct evidence about the nuclear localization of CP and the importance of the N-terminal region regarding the subcellular localization.…”

Section: Discussionmentioning

confidence: 52%

“…It has been demonstrated that the CP is needed for virus cell-to-cell movement but not for virus replication [21,22]. Long distance movement of SCPMV [18] and RYMV [23] has been observed to be dependent on particle formation.…”

Section: Introductionmentioning

confidence: 97%

“…It has also been demonstrated that the N-terminal part of SCPMV CP could interact with membranes [15], however, the biological relevance of that feature is unknown. Sobemovirus particles have been found in the nucleus [16,17,18]. Based on sequence similarity it has been supposed that the N-terminal region of sobemovirus CPs contains a nuclear localization signal (NLS) [19,20].…”

Section: Introductionmentioning

confidence: 99%

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Cocksfoot mottle sobemovirus coat protein contains two nuclear localization signals

et al. 2010

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Cocksfoot mottle virus (CfMV) coat protein (CP) localization was studied in plant and mammalian cells. Fusion of the full-length CP with enhanced green fluorescent protein (EGFP) localized to the cell nucleus whereas similar constructs lacking the first 33 N-terminal amino acids of CP localized to the cytoplasm. CP and EGFP fusions containing mutations in the arginine-rich motif of CP localized to the cytoplasm and to the nucleus in plant cells indicating the involvement of the motif in nuclear localization. In mammalian cells, mutations in the arginine-rich region were sufficient to completely abolish nuclear transport. The analysis of deletions of amino acid residues 1-11, 1-22, and 22-33 of CP demonstrated that there were two separate nuclear localization signals (NLS) within the N-terminus--a strong NLS1 in the arginine-rich region (residues 22-33) and a weaker NLS2 within residues 1-22. Analysis of point mutants revealed that the basic amino acid residues in the region of the two NLSs were individually not sufficient to direct CP to the nucleus. Additional microinjection studies with fluorescently labeled RNA and CP purified from CfMV particles demonstrated that the wild-type CP was capable of transporting the RNA to the nucleus. This feature was not sequence-specific in transient assays since both CfMV and GFP mRNA were transported to the cell nucleus by CfMV CP. Together the results suggest that the nucleus may be involved in CfMV infection.

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Failure of long-distance movement of southern bean mosaic virus in a resistant host is correlated with lack of normal virion formation

Cited by 33 publications

References 16 publications

Movement of rice yellow mottle virus between xylem cells through pit membranes

Movement of rice yellow mottle virus between xylem cells through pit membranes

Sobemoviruses

Cocksfoot mottle sobemovirus coat protein contains two nuclear localization signals

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