Interaction between the tobacco mosaic virus movement protein and host cell pectin methylesterases is required for viral cell-to-cell movement

Chen, Min-Huei; Sheng, Jinsong; Hínd, Geoffrey; Handa, Avtar K.; Citovsky, Vitaly

doi:10.1093/emboj/19.5.913

Cited by 291 publications

(204 citation statements)

References 50 publications

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“…The binding properties of MP and DC48MP were further explored using blot overlay assays essentially as described by Chen et al (2000). Ten mg of purified MP or DC48MP and different virus suspensions (CPMV, RCMV, CPSMV and TMV) were resolved on a 12 % SDS-PAGE gel and electroblotted onto a PVDF Immobilon P membrane.…”

Section: Methodsmentioning

confidence: 99%

The C-terminal region of the movement protein of Cowpea mosaic virus is involved in binding to the large but not to the small coat protein

Carvalho

Wellink²,

Ribeiro

et al. 2003

Journal of General Virology

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Cowpea mosaic virus (CPMV) moves from cell to cell as virus particles which are translocated through a plasmodesmata-penetrating transport tubule made up of viral movement protein (MP) copies. To gain further insight into the roles of the viral MP and capsid proteins (CP) in virus movement, full-length and truncated forms of the MP were expressed in insect cells using the baculovirus expression system. Using ELISA and blot overlay assays, affinity purified MP was shown to bind specifically to intact CPMV virions and to the large CP, but not to the small CP. This binding was not observed with a C-terminal deletion mutant of the MP, although this mutant retained the capacity to bind to other MP molecules and to form tubules. These results suggest that the C-terminal 48 amino acids constitute the virion-binding domain of the MP.

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Section: Methodsmentioning

confidence: 99%

The C-terminal region of the movement protein of Cowpea mosaic virus is involved in binding to the large but not to the small coat protein

Carvalho

Wellink²,

Ribeiro

et al. 2003

Journal of General Virology

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“…The extraction of the expressed protein from E. coli BL21-DE3-pLysS cells demonstrated that the MP was present only in the insoluble fraction, probably as the result of inclusion bodies formation (Martínez-Alonso et al, 2009). Similar cases of insolubility of proteins expressed in E. coli system were reported with the replicases of Tobacco mosaic virus (TMV) and Citrus tristeza virus (CTV) (Hills et al, 1987;Çevik et al, 2008) and with TMV MP (Chen et al, 2000). The formation of inclusion bodies is not correlated with the size of the synthesized polypeptide, the use of a fusion construct, the subunit structure, or the relative hydrophobicity of the recombinant protein.…”

mentioning

confidence: 54%

“…No significant labeling by anti-MP antibody was observed in CiLV-C infected tissues. A possible explanation for these failures is that MP has high hydrophobicity and is associated with membranes of the host cell (Chen et al, 2000). Such circumstances make its solubilization difficult, even after boiling the samples.…”

mentioning

confidence: 99%

In vitro expression and antiserum production against the movement protein of Citrus leprosis virus C (CiLV-C)

Calegario¹,

Labate²,

Peroni³

et al. 2012

Trop. plant pathol.

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Citrus leprosis, caused by Citrus leprosis virus C (CiLV-C), is currently considered the most important viral disease in the Brazilian citrus industry due to the high costs required for the chemical control of its vector, the mite Brevipalpus phoenicis. The pathogen induces a non-systemic infection and the disease is characterized by the appearance of localized lesions on citrus leaves, stems and fruits, premature fruit and leaf drop and dieback of stems. Attempts were made to promote in vitro expression of the putative cell-to-cell movement protein of CiLV-C in Escherichia coli and to produce a specific polyclonal antibody against this protein as a tool to investigate the virus-plantvector relationship. The antibody reacted strongly with the homologous protein expressed in vitro by ELISA, but poorly with the native protein present in leaf lesion extracts from sweet orange caused by CiLV-C. Reactions from old lesions were more intense than those from young lesions. Western blot and in situ immunolocalization assays failed to detect the native protein. These results suggest low expression of the movement protein (MP) in host tissues. Moreover, it is possible that the conformation of the protein expressed in vitro and used to produce the antibody differs from that of the native MP, hindering a full recognition of the latter.

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“…Numerous host factors involved have also been identified. For example, the targeting and anchorage of MPs to plasmodesmata require the action of a cell wallassociated pectin-methylesterase (PME) protein (Chen et al, 2000;Lionetti et al, 2014). An MP-binding protein 2C (MPB2C) was shown to co-localize with MP on microtubules (Kragler et al, 2003).…”

Section: Effects Of Tmv Movement Proteinmentioning

confidence: 99%

Modulation of host plant immunity by Tobamovirus proteins

Conti

Rodríguez

Venturuzzi

et al. 2016

Ann Bot

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Background To establish successful infection, plant viruses produce profound alterations of host physiology, disturbing unrelated endogenous processes and contributing to the development of disease. In tobamoviruses, emerging evidence suggests that viral-encoded proteins display a great variety of functions beyond the canonical roles required for virus structure and replication. Among these, their modulation of host immunity appears to be relevant in infection progression.Scope In this review, some recently described effects on host plant physiology of Tobacco mosaic virus (TMV)-encoded proteins, namely replicase, movement protein (MP) and coat protein (CP), are summarized. The discussion is focused on the effects of each viral component on the modulation of host defense responses, through mechanisms involving hormonal imbalance, innate immunity modulation and antiviral RNA silencing. These effects are described taking into consideration the differential spatial distribution and temporality of viral proteins during the dynamic process of replication and spread of the virus.Conclusion In discussion of these mechanisms, it is shown that both individual and combined effects of viralencoded proteins contribute to the development of the pathogenesis process, with the host plant's ability to control infection to some extent potentially advantageous to the invading virus.

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Interaction between the tobacco mosaic virus movement protein and host cell pectin methylesterases is required for viral cell-to-cell movement

Cited by 291 publications

References 50 publications

The C-terminal region of the movement protein of Cowpea mosaic virus is involved in binding to the large but not to the small coat protein

The C-terminal region of the movement protein of Cowpea mosaic virus is involved in binding to the large but not to the small coat protein

In vitro expression and antiserum production against the movement protein of Citrus leprosis virus C (CiLV-C)

Modulation of host plant immunity by Tobamovirus proteins

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