Salicylic Acid Interferes with Tobacco Mosaic Virus Replication via a Novel Salicylhydroxamic Acid-Sensitive Mechanism

1997 ◽  
Vol 9 (4) ◽  
pp. 547 ◽  
Author(s):  
Stephen Chivasa ◽  
Alex M. Murphy ◽  
Martin Naylor ◽  
John P. Carr
Keyword(s):  
Salicylic Acid ◽  
Tobacco Mosaic Virus ◽  
Mosaic Virus ◽  
Virus Replication ◽  
Salicylhydroxamic Acid

scholarly journals Oligomerization and Activity of the Helicase Domain of the Tobacco Mosaic Virus 126- and 183-Kilodalton Replicase Proteins

2003 ◽  
Vol 77 (6) ◽  
pp. 3549-3556 ◽  
Author(s):  
Sameer P. Goregaoker ◽  
James N. Culver
Keyword(s):  
Electron Microscopy ◽  
Molecular Weight ◽  
Tobacco Mosaic Virus ◽  
Mosaic Virus ◽  
Virus Replication ◽  
Protein Interaction ◽  
Gel Filtration ◽  
Helicase Domain ◽  
Protein Protein Interaction ◽  
Replicase Proteins

ABSTRACT A protein-protein interaction within the helicase domain of the Tobacco mosaic virus (TMV) 126- and 183-kDa replicase proteins was previously implicated in virus replication (S. Goregaoker, D. Lewandowski, and J. Culver, Virology 282:320-328, 2001). To further characterize the interaction, polypeptides covering the interacting portions of the TMV helicase domain were expressed and purified. Biochemical characterizations demonstrated that the helicase domain polypeptides hydrolyzed ATP and bound both single-stranded and duplexed RNA in an ATP-controlled fashion. A TMV helicase polypeptide also was capable of unwinding duplexed RNA, confirming the predicted helicase function of the domain. Biochemically active helicase polypeptides were shown by gel filtration to form high-molecular-weight complexes. Electron microscopy studies revealed the presence of ring-like oligomers that displayed six-sided symmetry. Taken together, these data demonstrate that the TMV helicase domain interacts with itself to produce hexamer-like oligomers. Within the context of the full-length 126- and 183-kDa proteins, these findings suggest that the TMV replicase may form a similar oligomer.

scholarly journals A Vicilin-Like Seed Storage Protein, PAP85, Is Involved in Tobacco Mosaic Virus Replication

2013 ◽  
Vol 87 (12) ◽  
pp. 6888-6900 ◽  
Author(s):  
C.-E. Chen ◽  
K.-C. Yeh ◽  
S.-H. Wu ◽  
H.-I. Wang ◽  
H.-H. Yeh
Keyword(s):  
Tobacco Mosaic Virus ◽  
Mosaic Virus ◽  
Virus Replication ◽  
Storage Protein ◽  
Seed Storage Protein ◽  
Seed Storage

scholarly journals Salicylic Acid and Jasmonic Acid Are Essential for Systemic Resistance Against Tobacco mosaic virus in Nicotiana benthamiana

2014 ◽  
Vol 27 (6) ◽  
pp. 567-577 ◽  
Author(s):  
Feng Zhu ◽  
De-Hui Xi ◽  
Shu Yuan ◽  
Fei Xu ◽  
Da-Wei Zhang ◽  
...  
Keyword(s):  
Salicylic Acid ◽  
Jasmonic Acid ◽  
Tobacco Mosaic Virus ◽  
Mosaic Virus ◽  
Nicotiana Benthamiana ◽  
Foliar Application ◽  
Mass Spectrometry Analysis ◽  
Systemic Resistance ◽  
Long Distance ◽  
Resistance Response

Systemic resistance is induced by pathogens and confers protection against a broad range of pathogens. Recent studies have indicated that salicylic acid (SA) derivative methyl salicylate (MeSA) serves as a long-distance phloem-mobile systemic resistance signal in tobacco, Arabidopsis, and potato. However, other experiments indicate that jasmonic acid (JA) is a critical mobile signal. Here, we present evidence suggesting both MeSA and methyl jasmonate (MeJA) are essential for systemic resistance against Tobacco mosaic virus (TMV), possibly acting as the initiating signals for systemic resistance. Foliar application of JA followed by SA triggered the strongest systemic resistance against TMV. Furthermore, we use a virus-induced gene-silencing–based genetics approach to investigate the function of JA and SA biosynthesis or signaling genes in systemic response against TMV infection. Silencing of SA or JA biosynthetic and signaling genes in Nicotiana benthamiana plants increased susceptibility to TMV. Genetic experiments also proved the irreplaceable roles of MeSA and MeJA in systemic resistance response. Systemic resistance was compromised when SA methyl transferase or JA carboxyl methyltransferase, which are required for MeSA and MeJA formation, respectively, were silenced. Moreover, high-performance liquid chromatography–mass spectrometry analysis indicated that JA and MeJA accumulated in phloem exudates of leaves at early stages and SA and MeSA accumulated at later stages, after TMV infection. Our data also indicated that JA and MeJA could regulate MeSA and SA production. Taken together, our results demonstrate that (Me)JA and (Me)SA are required for systemic resistance response against TMV.

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