Detection of the movement protein of red clover necrotic mosaic virus in a cell wall fraction from infected Nicotiana clevelandii plants

Osman, T. A. M.; Buck, K. W.

doi:10.1099/0022-1317-72-11-2853

Cited by 28 publications

(14 citation statements)

References 36 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…As reported in the present paper, ACLSV ORF2 protein was mainly detected in CW and CM fractions extracted from infected tissues, in agreement with the subcellular locations of other plant virus movement proteins (Albrecht et al, 1988;Godefroy-Colburn et al, 1986;Kormelink et al, 1994;Moser et al, 1988;Osman & Buck, 1991). The transient accumulation of movement proteins has been reported for several plant viruses.…”

supporting

confidence: 91%

Expression, subcellular location and modification of the 50 kDa protein encoded by ORF2 of the apple chlorotic leaf spot trichovirus genome

Sato

Yoshikawa

Takahashi

et al. 1995

Journal of General Virology

View full text Add to dashboard Cite

A putative movement protein of molecular mass 50 kDa encoded by the ORF2 of the apple chlorotic leaf spot virus (ACLSV) genome was expressed in Escherichia coli using an expression vector and was then used to produce an antiserum. Immunoblot analysis using an antiserum raised against this protein showed that the ORF2 protein of ACLSV was detected in both cell wall and cell membrane fractions prepared from infected Chenopodium quinoa tissues. The ORF2 protein from infected tissues had a molecular mass of 52 kDa, larger than that of the full-length ORF2 protein (50kDa protein) expressed in E. coli. Incubation of the 52 kDa protein with alkaline phosphatase resulted in a decrease in its apparent molecular mass from 52kDa to 50kDa, strongly suggesting that the ORF2 protein of ACLSV is phosphorylated in infected plant tissues.

show abstract

supporting

confidence: 91%

Expression, subcellular location and modification of the 50 kDa protein encoded by ORF2 of the apple chlorotic leaf spot trichovirus genome

Sato

Yoshikawa

Takahashi

et al. 1995

Journal of General Virology

View full text Add to dashboard Cite

show abstract

“…MP might instead work intercellularly to disrupt the RNA silencing cascade by disrupting the spread of the silencing signal. MP is known to target to the cell wall of plant cells, presumably the plasmodesmata, a logical location for the interception of the spreading signal adding support for this argument (Osman and Buck, 1991; Tremblay et al, 2005). Indeed, earlier work in characterizing the MP alanine-scanning mutants used in these studies suggests that the intracellular location of MP directly correlates with the ability of MP to suppress RNA silencing.…”

Section: Discussionmentioning

confidence: 91%

“…The RCNMV genome consists of 2 RNAs, with RNA-1 containing the genes encoding the two polymerase proteins p27 and p88 as well as the capsid protein (CP) while RNA-2 encodes the movement protein (MP; Fig 1A; Lommel et al, 1988; Osman and Buck, 1991; Xiong et al, 1993a; Xiong et al, 1993b; Xiong and Lommel, 1989). An earlier study investigating the suppression of RNA silencing by RCNMV identified not a single protein, but instead the viral replication complex as the source of RNA silencing suppression (Takeda et al, 2005).…”

Section: Introductionmentioning

confidence: 99%

The Red clover necrotic mosaic virus RNA-2 encoded movement protein is a second suppressor of RNA silencing

et al. 2008

View full text Add to dashboard Cite

The replication complex of Red clover necrotic mosaic virus (RCNMV) has been shown to possess silencing suppression activity. Here a newly developed viral-based assay for the identification of silencing suppression activity was used to provide evidence for a second, mechanistically distinct method of silencing suppression provided for by the RCNMV movement protein (MP). This new assay relies on Turnip crinkle virus with its capsid protein replaced with green fluorescent protein to act as a reporter (TCV-sGFP). In the presence of a protein with silencing suppression activity TCV-sGFP readily moves from cell-to-cell, but in the absence of such a protein TCV-sGFP is confined to small foci of infection. This TCV-sGFP assay was used to identify MP as a suppressor of RNA silencing, to delimit essential amino acids for this activity and uncouple silencing and movement functions.

show abstract

“…Thus, whereas some properties of BL1, namely its cell wall and plasma membrane localization, basic charge, and phosphorylation, resemble those of the single MP encoded byTMV (Deom et ai., 1990;Atkins et al, 1991;Moore et al, 1992;Watanabe et al, 1992) and red clover necrotic mosaic virus (RCNMV) (Osman and Buck, 1991), BL1 is quite distinct in its inability to bind nucleic acids. Recently, based on microinjection of individual mesophyll cells, Noueiry et al (1994) have concluded that an E. coli-synthesized BL1 fusion protein can increase the size exclusion limits of plasmodesmata and facilitate the transport of dsDNA.…”

Section: Discussionmentioning

confidence: 99%

The geminivirus BR1 movement protein binds single-stranded DNA and localizes to the cell nucleus.

et al. 1994

View full text Add to dashboard Cite

Plant viruses encode movement proteins that are essential for infection of the host but are not required for viral replication or encapsidation. Squash leaf curl virus (SqLCV), a bipartite geminivirus with a single-stranded DNA genome, encodes two movement proteins, BR1 and BL1, that have been implicated in separate functions in viral movement. To further elucidate these functions, we have investigated the nucleic acid binding properties and cellular localization of BR1 and BL1. In this study, we showed that BR1 binds strongly to single-stranded nucleic acids, with a higher affinity for single-stranded DNA than RNA, and is localized to the nucleus of SqLCV-infected plant cells. In contrast, BL1 binds only weakly to single-stranded nucleic acids and not at all to double-stranded DNA. The nuclear localization of BR1 and the previously demonstrated plasma membrane localization of BL1 were also observed when these proteins were expressed from baculovirus vectors in Spodoptera frugiperda insect cells. The biochemical properties and cellular locations of BR1 and BL1 suggest a model for SqLCV movement whereby BR1 is involved in the shuttling of the genome in and/or out of the nucleus and BL1 acts at the plasma membrane/cell wall to facilitate viral movement across cell boundaries.

show abstract

Detection of the movement protein of red clover necrotic mosaic virus in a cell wall fraction from infected Nicotiana clevelandii plants

Cited by 28 publications

References 36 publications

Expression, subcellular location and modification of the 50 kDa protein encoded by ORF2 of the apple chlorotic leaf spot trichovirus genome

Expression, subcellular location and modification of the 50 kDa protein encoded by ORF2 of the apple chlorotic leaf spot trichovirus genome

The Red clover necrotic mosaic virus RNA-2 encoded movement protein is a second suppressor of RNA silencing

The geminivirus BR1 movement protein binds single-stranded DNA and localizes to the cell nucleus.

Contact Info

Product

Resources

About