Literature DB >> 9267012

Tubule-forming capacity of the movement proteins of alfalfa mosaic virus and brome mosaic virus.

D T Kasteel1, N N van der Wel, K A Jansen, R W Goldbach, J W van Lent.   

Abstract

The structural phenotype of the movement proteins (MPs) of two representatives of the Bromoviridae, alfalfa mosaic virus (AMV) and brome mosaic virus (BMV), was studied in protoplasts. Immunofluorescence microscopy showed that the MPs of these viruses, for which there has been no evidence of a tubule-guided mechanism, assemble into long tubular structures at the surface of the infected protoplast. Electron microscopy and immunogold analysis confirmed the presence of both MP and virus particles in the tubules induced by AMV and BMV. The significance of the tubule-forming properties of these viral MPs is discussed.

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Year:  1997        PMID: 9267012     DOI: 10.1099/0022-1317-78-8-2089

Source DB:  PubMed          Journal:  J Gen Virol        ISSN: 0022-1317            Impact factor:   3.891


  21 in total

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Authors:  T Soellick; J F Uhrig; G L Bucher; J W Kellmann; P H Schreier
Journal:  Proc Natl Acad Sci U S A       Date:  2000-02-29       Impact factor: 11.205

6.  Citrus Psorosis Virus Movement Protein Contains an Aspartic Protease Required for Autocleavage and the Formation of Tubule-Like Structures at Plasmodesmata.

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8.  Reverse genetic analysis of Ourmiaviruses reveals the nucleolar localization of the coat protein in Nicotiana benthamiana and unusual requirements for virion formation.

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9.  Mutations in the capsid protein of Brome mosaic virus affecting encapsidation eliminate vesicle induction in planta: implications for virus cell-to-cell spread.

Authors:  Devinka Bamunusinghe; Sonali Chaturvedi; Jang-Kyun Seo; A L N Rao
Journal:  J Virol       Date:  2013-06-05       Impact factor: 5.103

10.  The C terminus of brome mosaic virus coat protein controls viral cell-to-cell and long-distance movement.

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Journal:  J Virol       Date:  2001-06       Impact factor: 5.103

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