scholarly journals Two amino acid substitutions in the tomato mosaic virus 30-kilodalton movement protein confer the ability to overcome the Tm-2(2) resistance gene in the tomato.

1993 ◽  
Vol 67 (11) ◽  
pp. 6432-6438 ◽  
Author(s):  
H Weber ◽  
S Schultze ◽  
A J Pfitzner
Keyword(s):  
Amino Acid ◽  
Mosaic Virus ◽  
Resistance Gene ◽  
Movement Protein ◽  
Tomato Mosaic Virus ◽  
Amino Acid Substitutions

scholarly journals Tm-22 Resistance in Tomato Requires Recognition of the Carboxy Terminus of the Movement Protein of Tomato Mosaic Virus

1998 ◽  
Vol 11 (6) ◽  
pp. 498-503 ◽  
Author(s):  
Hans Weber ◽  
Artur J. P. Pfitzner
Keyword(s):  
Mosaic Virus ◽  
Resistance Gene ◽  
Movement Protein ◽  
Cell Movement ◽  
Tomato Mosaic Virus ◽  
Wild Type ◽  
Virus Transport ◽  
Tomato Plants ◽  
Movement Proteins ◽  
Carboxy Terminal

The Tm-22 resistance gene is used in most commercial tomato cultivars for protection against infection with tomato mosaic virus (ToMV). It has been suggested that Tm-22 resistance interferes with viral cell-to-cell movement in plants; ToMV strain ToMV-22 requires two amino acid (aa) exchanges in the carboxy-terminal region of the viral 30-kDa movement protein (at positions 238 and 244) to overcome Tm-22 resistance. For further analysis of this region of the 30-kDa protein, two stop codons were introduced into ToMV movement proteins at aa positions 235 and 237, leading to deletion of the terminal 30 aa. The mutant virus strains were able to infect wild-type tomato plants systemically, suggesting the carboxy-terminal portion of the ToMV 30-kDa protein is dispensable for virus transport in tomato. Even more important, the deletion mutants overcame the Tm-22 resistance gene. These data indicate the carboxy-terminal domain of the ToMV movement protein serves as a recognition target in the context of the Tm-22 resistance gene. Furthermore, expression of the 30-kDa movement protein from wild-type ToMV, but not from ToMV-22, in transgenic tomato plants with the Tm-22 resistance gene led to elicitation of a necrotic reaction in tomato seedlings, showing that the 30-kDa protein on its own is able to induce the plant's defense reaction.

scholarly journals RNA Helicase Domain of Tobamovirus Replicase Executes Cell-to-Cell Movement Possibly through Collaboration with Its Nonconserved Region

2003 ◽  
Vol 77 (22) ◽  
pp. 12357-12362 ◽  
Author(s):  
Kyotaro Hirashima ◽  
Yuichiro Watanabe
Keyword(s):  
Amino Acid ◽  
Tobacco Mosaic Virus ◽  
Mosaic Virus ◽  
Movement Protein ◽  
Cell Movement ◽  
Rna Helicase ◽  
Chimeric Virus ◽  
Amino Acid Substitutions ◽  
Helicase Domain ◽  
Phenotypic Reversion

ABSTRACT UR-hel, a chimeric virus obtained by replacement of the RNA helicase domain of tobacco mosaic virus (TMV)-U1 replicase with that from the TMV-R strain, could replicate similarly to TMV-U1 in protoplasts but could not move from cell to cell (K. Hirashima and Y. Watanabe, J. Virol. 75:8831-8836, 2001). It was suggested that TMV recruited both the movement protein (MP) and replicase for cell-to-cell movement by unknown mechanisms. Here, we found that a recombinant, UR-hel/V, in which the nonconserved region was derived from TMV-R in addition to the RNA helicase domain of replicase, could move from cell to cell. We also analyzed revertants isolated from UR-hel, which recovered cell-to-cell movement by their own abilities. We found amino acid substitutions responsible for phenotypic reversion only in the nonconserved region and/or RNA helicase domain but never in MP. Together, these data show that both the nonconserved region and the RNA helicase domain of replicase are involved in cell-to-cell movement. The RNA helicase domain of tobamovirus replicase possibly does not interact directly with MP but interacts with its nonconserved region to execute cell-to-cell movement.

scholarly journals The catalytic subunit of protein kinase CK2 phosphorylates in vitro the movement protein of Tomato mosaic virus

2003 ◽  
Vol 84 (2) ◽  
pp. 497-505 ◽  
Author(s):  
Yasuhiko Matsushita ◽  
Mayumi Ohshima ◽  
Kuniaki Yoshioka ◽  
Masamichi Nishiguchi ◽  
Hiroshi Nyunoya
Keyword(s):  
Protein Kinase ◽  
Mosaic Virus ◽  
Protein Kinase Ck2 ◽  
Movement Protein ◽  
Catalytic Subunit ◽  
Tomato Mosaic Virus ◽  
Kinase Ck2

scholarly journals Structural basis for the recognition-evasion arms race between Tomato mosaic virus and the resistance gene Tm-1

2014 ◽  
Vol 111 (33) ◽  
pp. E3486-E3495 ◽  
Author(s):  
K. Ishibashi ◽  
Y. Kezuka ◽  
C. Kobayashi ◽  
M. Kato ◽  
T. Inoue ◽  
...  
Keyword(s):  
Mosaic Virus ◽  
Resistance Gene ◽  
Arms Race ◽  
Tomato Mosaic Virus ◽  
Structural Basis

Kazakh strains of tobacco mosaic virus: two strains with potentially destabilizing amino acid substitutions in the coat protein

2000 ◽  
Vol 56 (2) ◽  
pp. 71-77 ◽  
Author(s):  
VICTOR K. NOVIKOV ◽  
EKATERINA V. BELENOVICH ◽  
EVGENY N. DOBROV ◽  
SERGEI K. ZAVRIEV
Keyword(s):  
Amino Acid ◽  
Coat Protein ◽  
Tobacco Mosaic Virus ◽  
Mosaic Virus ◽  
Amino Acid Substitutions

scholarly journals The Tomato brown rugose fruit virus movement protein overcomes Tm-22 resistance in tomato while attenuating viral transport

2021 ◽  
Author(s):  
Hagit Hak ◽  
Ziv Spiegelman
Keyword(s):  
Mosaic Virus ◽  
Movement Protein ◽  
Cell Movement ◽  
Systemic Infection ◽  
Movement Analysis ◽  
Tomato Mosaic Virus ◽  
Resistance Response ◽  
Global Epidemic ◽  
High Durability ◽  
C Terminus

Tomato brown rugose fruit virus (ToBRFV) is a new virus of the Tobamovirus genus, causing substantial damage to tomato crops. Reports of recent ToBRFV outbreaks from around the world indicate an emerging global epidemic. ToBRFV overcomes all tobamovirus resistances in tomato, including the durable Tm-22 resistance gene, which had been effective against multiple tobamoviruses. Here, we show that the ToBRFV movement protein (MPToBRFV) enables the virus to evade Tm-22 resistance. Transient expression of MPToBRFV failed to activate the Tm-22 resistance response. Replacement of the original MP sequence of Tomato mosaic virus (ToMV) with MPToBRFV enabled this recombinant virus to infect Tm-22 resistant plants. Using hybrid protein analysis, we show that the elements required to evade Tm-22 are located between MPToBRFV amino acids 1 and 216, and not the C terminus as previously assumed. Analysis of ToBRFV systemic infection in tomato revealed that ToBRFV spreads slower compared to ToMV. Interestingly, replacement of Tobacco mosaic virus (TMV) and ToMV MPs with MPToBRFV caused an attenuation of systemic infection of both viruses. Cell-to-cell movement analysis showed that MPToBRFV moves less effectively compared to the TMV MP (MPTMV). These findings suggest that overcoming Tm-22 is associated with attenuated MP function. This may explain the high durability of Tm-22 resistance, which had remained unbroken for over 60 years.

scholarly journals Tobamovirus Replicase Coding Region Is Involved in Cell-to-Cell Movement

2001 ◽  
Vol 75 (18) ◽  
pp. 8831-8836 ◽  
Author(s):  
Kyotaro Hirashima ◽  
Yuichiro Watanabe
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Tobacco Mosaic Virus ◽  
Host Range ◽  
Mosaic Virus ◽  
Movement Protein ◽  
Cell Movement ◽  
Coding Region ◽  
Replicase Proteins ◽  
Viral Movement

ABSTRACT Tobacco mosaic virus (TMV) encodes a 30-kDa movement protein (MP) which enables viral movement from cell to cell. It is, however, unclear whether the 126- and 183-kDa replicase proteins are involved in the cell-to-cell movement of TMV. In the course of our studies into TMV-R, a strain with a host range different from that of TMV-U1, we have obtained an interesting chimeric virus, UR-hel. The amino acid sequence differences between UR-hel and TMV-U1 are located only in the helicase-like domain of the replicase. Interestingly, UR-hel has a defect in its cell-to-cell movement. The replication of UR-hel showed a level of replication of the genome, synthesis, and accumulation of MP similar to that observed in TMV-U1-inoculated protoplasts. Such observations support the hypothesis that the replicase coding region may in some fashion be involved in cell-to-cell movement of TMV.

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