RNA-Directed Assembly of Tobacco Mosaic Virus (TMV)-Like Carriers with Tunable Fractions of Differently Addressable Coat Proteins

Replication of Potato virus X (PVX) was reduced in transgenic protoplasts that accumulated wild-type coat protein (CPWT) of Tobacco mosaic virus (TMV) or a mutant CP, CPT42W, that produced highly ordered states of aggregation, including pseudovirions. This reaction is referred to as heterologous CP-mediated resistance. However, protoplasts expressing a CP mutant that abolished aggregation and did not produce pseudovirions, CPT28W, did not reduce PVX replication. Similarly, in transgenic tobacco plants producing TMV CPWT or CPT42W, there was a delay in local cell-to-cell spread of PVX infection that was not observed in CPT28W plants or in non-transgenic plants. The results suggest that the quaternary structure of the TMV CP regulates the mechanism(s) of heterologous CP-mediated resistance. Similarly, transgenic protoplasts that produced PVX CP conferred transient protection against infection by TMV RNA. Transgenic plants that accumulated PVX CP reduced the cell-to-cell spread of infection and resulted in a delay in systemic infection following inoculation with TMV or TMV RNA. Heterologous CP-mediated resistance was characterized by a brief delay in systemic infection, whilst homologous CP-mediated resistance conferred reduced or no systemic infection.

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Dual Functional Modification of Alkaline Amino Acids Induces the Self-Assembly of Cylinder-Like Tobacco Mosaic Virus Coat Proteins into Gear-Like Architectures

Small ◽

10.1002/smll.201805543 ◽

2019 ◽

Vol 15 (10) ◽

pp. 1805543 ◽

Cited By ~ 2

Author(s):

Jian-Ting Zhang ◽

Ranjith Kumar Kankala ◽

Yi-Hao Zhou ◽

Jin-Chen Dong ◽

Ai-Zheng Chen ◽

...

Keyword(s):

Amino Acids ◽

Tobacco Mosaic Virus ◽

Mosaic Virus ◽

Self Assembly ◽

The Self ◽

Coat Proteins ◽

Dual Functional ◽

Functional Modification ◽

Virus Coat

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DEMONSTRATION OF THE UNIVERSALITY OF THE GENETIC CODE in vivo BY COMPARISON OF THE COAT PROTEINS SYNTHESIZED IN DIFFERENT PLANTS BY TOBACCO MOSAIC VIRUS RNA

Proceedings of the National Academy of Sciences ◽

10.1073/pnas.63.4.1189 ◽

1969 ◽

Vol 63 (4) ◽

pp. 1189-1195 ◽

Cited By ~ 1

Author(s):

Y. Okada ◽

Y. Nozu ◽

T. Ohno

Keyword(s):

Tobacco Mosaic Virus ◽

Genetic Code ◽

Mosaic Virus ◽

Coat Proteins ◽

Virus Rna

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Self-Assembling Light-Harvesting Systems from Synthetically Modified Tobacco Mosaic Virus Coat Proteins

Journal of the American Chemical Society ◽

10.1021/ja063887t ◽

2007 ◽

Vol 129 (11) ◽

pp. 3104-3109 ◽

Cited By ~ 289

Author(s):

Rebekah A. Miller ◽

Andrew D. Presley ◽

Matthew B. Francis

Keyword(s):

Tobacco Mosaic Virus ◽

Mosaic Virus ◽

Light Harvesting ◽

Coat Proteins ◽

Self Assembling ◽

Harvesting Systems ◽

Virus Coat

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Mutants of Tobacco mosaic virus with Temperature-Sensitive Coat Proteins Induce Heat Shock Response in Tobacco Leaves

Molecular Plant-Microbe Interactions ◽

10.1094/mpmi.2001.14.7.914 ◽

2001 ◽

Vol 14 (7) ◽

pp. 914-917 ◽

Cited By ~ 39

Author(s):

Harald Jockusch ◽

Christiane Wiegand ◽

Birgit Mersch ◽

Daniela Rajes

Keyword(s):

Heat Shock ◽

Tobacco Mosaic Virus ◽

Mosaic Virus ◽

Heat Shock Response ◽

Temperature Sensitive ◽

Coat Proteins ◽

Leaf Extracts ◽

Tobacco Leaves ◽

Shock Response ◽

Shock Proteins

We analyzed, with respect to heat shock proteins (HSPs), systemically reacting tobacco leaves inoculated with Tobacco mosaic virus (TMV), wild-type vulgare, and temperature-sensitive coat protein (CP) mutants Ni 118 (P20L) and flavum (D19A), kept at 23 or 30°C. HSP18 and HSP70 mRNAs and proteins were induced with temperature-sensitive CP mutants after 1 to 2 days at 30°C. After 4 to 6 days, HSP70 was also induced at 23°C. The induction of HSPs paralleled the amount of insoluble TMV CP in leaf extracts, indicating that denatured TMV CP by itself induces a heat-shock response.

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