Literature DB >> 9601503

The movement protein and coat protein of alfalfa mosaic virus accumulate in structurally modified plasmodesmata.

N N van der Wel1, R W Goldbach, J W van Lent.   

Abstract

In systemically infected tissues of Nicotiana benthamiana, alfalfa mosaic virus (AMV) coat protein (CP) and movement protein (MP) are detected in plasmodesmata in a layer of three to four cells at the progressing front of infection. Besides the presence of these viral proteins, the plasmodesmata are structurally modified in that the desmotubule is absent and the diameter has increased drastically (almost twofold) when compared to plasmodesmata in uninfected cells or cells in which AMV infection had been fully established. Previously reported observations on virion-containing tubule formation at the surface of AMV-infected protoplasts suggest that AMV employs a tubule-guided mechanism for intercellular movement. Although CP and MP localization to plasmodesmata is consistent with such a mechanism, no tubules were found in plasmodesmata of AMV-infected tissues. The significance of these observations is discussed.

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Year:  1998        PMID: 9601503     DOI: 10.1006/viro.1998.9117

Source DB:  PubMed          Journal:  Virology        ISSN: 0042-6822            Impact factor:   3.616


  7 in total

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2.  Tomato spotted wilt virus particle morphogenesis in plant cells.

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Authors:  Edmund Kozieł; Józef J Bujarski; Katarzyna Otulak
Journal:  Int J Mol Sci       Date:  2017-12-16       Impact factor: 5.923

5.  Ultrastructural Analysis of Prune DwarfVirus Intercellular Transport and Pathogenesis.

Authors:  Edmund Kozieł; Katarzyna Otulak-Kozieł; Józef J Bujarski
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6.  The development of a hairless phenotype in barley roots treated with gold nanoparticles is accompanied by changes in the symplasmic communication.

Authors:  Anna Milewska-Hendel; Weronika Witek; Aleksandra Rypień; Maciej Zubko; Rafal Baranski; Danuta Stróż; Ewa U Kurczyńska
Journal:  Sci Rep       Date:  2019-03-18       Impact factor: 4.379

7.  Groundnut bud necrosis virus encoded NSm associates with membranes via its C-terminal domain.

Authors:  Pratibha Singh; Shantinath S Indi; Handanahal S Savithri
Journal:  PLoS One       Date:  2014-06-11       Impact factor: 3.240

  7 in total

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