Search PubMed⌕ Search

SEARCH · Search PubMed

Results for “TMV”

Search indexed PubMed citations on genomics, clinical trials, systematic reviews and public health. Explore titles, authors and supplied subject terms, then open the PubMed record.

Quote a phrase for an exact phrase match. Source license links do not imply unrestricted reuse.

At least 361 records · Page 20Linked to original sources

Mechanism of RNA-protein interactions in tobacco mosaic virus: analysis of the pH stability of virus protein complexes with synthetic polynucleotides.

TMV-like RNP complexes were reconstituted from TMV protein and synthetic polynucleotides. Analysis of the pH stability of RNP with polynucleotides containing U, G, or their analogues reveals a correlation between the stability of their structure and the pK values of the bases, and indicates that the -NH-CO-groups of U and G are involved in hydrogen bonding with protein. It is suggested that TMV protein has two U- and one G-specific binding sites which, according to the phase position of the protein subunits relative to the origin of TMV assembly (D. Zimmern (1977), Cell 11, 463) are likely to be organized as UGU. The binding of the A and C residues of RNA with TMV protein is nonspecific. TMV protein groups with pK 6.3, 7.5 and 9.7 were found to be essential in the protein-protein interactions in RNP. A group of the protein with pK 8.2 is also involved in RNP stabilization. Both protein-protein interactions and interactions of protein with RNA phosphate groups were shown to be mediated by a conformational change in the protein induced by base binding. The effect of bases on both types of interactions changes in the order G approximately equal to much greater than A, and incorporation of C in RNP proceeds in a compulsory way at the expense of interaction of the neighbouring nucleotide residues in polynucleotides with protein. The data obtained are used to discuss the principles of the cooperativity of the interactions between TMV components and the mechanism of initiation and elongation in TMV self-assembly.

Binding Sites↗

Tracheal mucus velocity remains normal in healthy sheep intubated with a new endotracheal tube with a novel laryngeal seal.

BACKGROUND: Tracheal mucus velocity (TMV), an index of mucociliary clearance, is reduced markedly in patients intubated with standard endotracheal tubes (ETTs) with high-compliance low-pressure (hi-lo) cuffs. The authors developed a new ultra-thin walled ETT in which the inflatable cuff is replaced with a no-pressure seal, positioned at the level of the larynx. The seal consists of 12 to 20 toroidal layers of thin polyurethane film ("gills") at the level of the vocal cords and prevents both air leak and fluid aspiration. The authors hypothesized that ETTs with the new laryngeal seal may impair TMV less than ETTs with inflated hi-lo cuffs do. METHODS: The TMV was measured in seven healthy female sheep by radiographically tracking the motion of small discs of tantalum inserted into the trachea through a bronchoscope. The TMV was measured in spontaneously breathing sheep before intubation (baseline) and after intubation with either a hi-lo ETT (control group) or after intubation with a new ETT with gills (study group). Four to six weeks later, the studies were repeated, but the sheep that were previously in the control group served as the study group, and those in the study group served as controls. RESULTS: Baseline TMV did not differ in the two groups. In the control group, TMV decreased significantly (by 67%) from baseline. In the study group, TMV did not differ significantly from baseline and remained steady during 3 h of intubation. CONCLUSIONS: The TMV does not change in sheep intubated with new ETTs with gills. The new ETT's may help promote a normal mucociliary clearance in patients who require ventilation.

Animals↗

Response of Membrane-bound Mg-activated ATPase of Tobacco Leaves to Tobacco Mosaic Virus.

Infectious material was formed at an early stage, and migrated into the mesophyll from the epidermis of tobacco leaves (Nicotiana tabacum cv. Samsun NN) during the period of 1 to 3 hours after inoculation with tobacco mosaic virus (TMV). The activity of membrane-bound Mg(2+)-activated ATPase from the mesophyll was stimulated two to four times within 30 minutes after inoculation with 1.0 microgram per milliliter of TMV. Maximum TMV stimulation of membrane-bound Mg(2+)-activated ATPase activity in epidermis and mesophyll was observed at 0.5 and 3.0 hours after inoculation, respectively. This stimulation was also observed with ultraviolet irradiated TMV (only RNA was destroyed), whereas, the stimulation was not observed with heat-irradiated TMV (both coat and RNA were destroyed). Stimulation equal to that of TMV was observed by inoculation with cucumber green mottle mosaic virus and to a lesser extent with cucumber mosaic virus.These results illustrate that the stimulus resulting from inoculation with TMV transfers to underlying cells faster than the migration of TMV particles. This stimulus might be closely correlated to the structure of virus, but not to the infectivity of virus.

Journal Article↗

Reduced Photosystem II Activity and Accumulation of Viral Coat Protein in Chloroplasts of Leaves Infected with Tobacco Mosaic Virus.

We previously reported (A Reinero, RN Beachy 1986 Plant Mol Biol 6:291-301) that coat protein (CP) of tobacco mosaic virus (TMV) accumulates in chloroplasts of systemically infected leaves. To determine the significance of such interaction we examined electron transport rates in chloroplasts containing different levels of TMV-CP. Tobacco (Nicotiana tabacum L.) plants were infected with either a TMV strain inducing chlorosis or with a strain inducing mild symptoms, and both the accumulation pattern of TMV-CP inside chloroplasts as well as the rates of photosynthetic electron transport were followed. The CP of the TMV strain inducing chlorosis was detected inside chloroplasts 3 days after infection, and thereafter accumulated at a rapid rate, first in the stroma and then in the thylakoid membranes. On the other hand, the CP of the TMV strain that caused only mild symptoms accumulated in chloroplasts to lower levels and little CP was associated with the thylakoids. In vivo and in vitro measurements of electron transport revealed that photosystem II activity was inhibited in plants infected with the aggressive TMV strain while no reduction was observed in plants infected with the mild strain. The capacity of chloroplasts to synthesize proteins was equivalent in organelles isolated from healthy and virus-infected leaves. The possibility that a large accumulation of TMV-CP inside chloroplasts may affect photosynthesis in virus-infected plants by inhibiting photosystem II activity is discussed.

Journal Article↗

Salicylic acid is a systemic signal and an inducer of pathogenesis-related proteins in virus-infected tobacco.

Systemic induction of pathogenesis-related (PR) proteins in tobacco, which occurs during the hypersensitive response to tobacco mosaic virus (TMV), may be caused by a minimum 10-fold systemic increase in endogenous levels of salicylic acid (SA). This rise in SA parallels PR-1 protein induction and occurs in TMV-resistant Xanthi-nc tobacco carrying the N gene, but not in TMV-susceptible (nn) tobacco. By feeding SA to excised leaves of Xanthi-nc (NN) tobacco, we have shown that the observed increase in endogenous SA levels is sufficient for the systemic induction of PR-1 proteins. TMV infection became systemic and Xanthi-nc plants failed to accumulate PR-1 proteins at 32 degrees C. This loss of hypersensitive response at high temperature was associated with an inability to accumulate SA. However, spraying leaves with SA induced PR-1 proteins at both 24 and 32 degrees C. SA is most likely exported from the primary site of infection to the uninfected tissues. A computer model predicts that SA should move rapidly in phloem. When leaves of Xanthi-nc tobacco were excised 24 hr after TMV inoculation and exudates from the cut petioles were collected, the increase in endogenous SA in TMV-inoculated leaves paralleled SA levels in exudates. Exudation and leaf accumulation of SA were proportional to TMV concentration and were higher in light than in darkness. Different components of TMV were compared for their ability to induce SA accumulation and exudation: three different aggregation states of coat protein failed to induce SA, but unencapsidated viral RNA elicited SA accumulation in leaves and phloem. These results further support the hypothesis that SA acts as an endogenous signal that triggers local and systemic induction of PR-1 proteins and, possibly, some components of systemic acquired resistance in NN tobacco.

Immunity, Innate↗

Infectivity suppressing and virus-binding activities of a membrane material isolated from tobacco leaves.

TMV binding substance (R) was isolated from a tobacco leaf membrane fraction and was purified by extraction with organic solvents and by column chromatography. Experimental results suggest that the binding of R with TMV results in inactivation of TMV. When tobacco leaves were inoculated with the R-TMV complex, it was found that the formation of polysome containing infecting viral RNA was inhibited. Model experiments showed that the mode of R-TMV adsorption to the membrane is different from that of TMV adsorption and that stripping of coat protein from TMV by SDS was inhibited by R. A possible explanation for the mechanism of this inhibition by R is that the R-TMV complex follows a pathway which does not lead to establishment of infection. Although less efficient, R was still active when it was applied after virus inoculation. Due to its affinity to coat protein, R might also interfere with a later process of viral multiplication.

Adsorption↗

Tissue Doppler echocardiography reveals insufficient contractile reserve recruitment during effort in subjects with mitral valve prolapse and those with thick mitral valve.

OBJECTIVE: To assess by tissue Doppler echocardiography (TDE), the tissue velocities, both at rest and after exercise stress testing, in subjects with mitral valve prolapse (MVP) and those with thick mitral valve (TMV). METHODS: Twenty individuals with typical MVP, 30 with TMV, and 30 healthy controls were enrolled. TDE was performed at the basal-inferior wall and the parameters evaluated were the S, Em, and Am velocities, as well as the Em/Am ratio. RESULTS: The mean S-wave at rest was higher in subjects with MVP compared to that of the TMV (P < 0.01) and the control groups (P = 0.00005), whereas after exercise it was higher in the control group compared to either MVP (P = 0.013) or TMV group (P = 0.00002). The mean Em wave at rest was higher in the control individuals both at rest (P = 0.007 compared with MVP group and P = 0.013 compared with TMV group), and after exercise (P = 0.0002 and 0.0009, respectively). The Am wave in the MVP group was higher compared with TMV and control subjects at rest (P = 0.022 and 0.00001, respectively) but it was not after exercise (P = ns for both comparisons). The Em/Am ratio of the control group at rest was higher than that of the MVP (P = 0.0000) and TMV (P = 0.00028) groups. However, after exercise, it was higher only when compared with the MVP group (P = 0.016). CONCLUSIONS: Subjects with MVP and those with TMV exhibit a less effective contractile response to exercise compared to healthy individuals. Some degree of diastolic dysfunction, particularly after exercise, was also detected in the individuals with MVP.

Adult↗

Deposition of platinum clusters on surface-modified Tobacco mosaic virus.

Nanoscaled Pt conductors were prepared from genetically engineered Tobacco mosaic virus (TMV) templates through Pt cluster deposition on the outer surface of the TMV. Pt clusters were synthesized and deposited on the engineered TMV with surface-exposed cysteine via the in situ mineralization of hexachloroplatinate anions. This deposition was driven by the specific binding between thiols and the solid metal clusters. In addition, Pt-thiolate adducts are suggested to form on the engineered TMV in aqueous solutions that work as nucleation sites for the formation of the Pt clusters. The specific binding between Pt clusters and the engineered TMV template was investigated using UV/vis spectrophotometry and quartz crystal microbalance (QCM) analysis. The electric conductance of Pt-deposited TMV was greater than that of the uncoated TMV virion particles. This result suggests the application of metal cluster-deposited engineered TMV in future electrical devices such as rapid response sensors.

Adsorption↗

5'-dephosphorylated 2',5'-adenylate trimer and its analogs. Inhibition of tobacco mosaic virus replication in tobacco mosaic virus-infected leaf discs, protoplasts, and intact tobacco plants.

The effect of the 5'-dephosphorylated 2',5'-adenylate trimer and its 2',5'-trimer core analogs on the inhibition of tobacco mosaic virus (TMV) replication was determined in tobacco leaf discs, protoplasts, and whole tobacco plants, using infectivity tests and enzyme-linked immunosorbent assays. A structure-activity-metabolic stability-toxicity analysis of the 2',5'-adenylate trimer core molecule in TMV-infected Nicotiana glutinosa was determined. Modification at either the 6-amino position of the adenylate residues (i.e. inosinate trimer core) or at the 2' terminus (i.e. A-A-ara-A or A-A-Tu) inhibited replication of TMV. Modification of the 3'-hydroxyl group of the adenylate residues to 3-deoxyribose (i.e. the 2',5'-cordycepin trimer core) inhibited TMV replication better than the 2',5'-adenylate trimer core molecule. With enzyme-linked immunosorbent assays, there was complete inhibition of TMV replication by 200 nM 2',5'-adenylate trimer core for 60 h and by 200 nM 2',5'-cordycepin trimer core for 96 h. The amount of 2',5'-oligonucleotides associated with the leaves was determined using 2',5'-[3H]cordycepin trimer core; 1 X 10(-12) mol/cm2 of plant leaves inhibited TMV replication by 99%. No 2',5'-phosphodiesterase activity was detected in TMV-infected and noninfected leaf extracts. Therefore, the 2',5'-trimer cores were potent inhibitors of TMV replication at nanomolar concentrations, i.e. at 1000-fold lower concentration than that required in mammalian systems.

Adenosine↗

Proteomic analysis of tobacco mosaic virus-infected tomato (Lycopersicon esculentum M.) fruits and detection of viral coat protein.

Tobacco mosaic virus (TMV) is a widespread plant virus from the genus Tobamovirus that affects tobacco and tomato plants causing a pathology characterised by cell breakage and disorganisation in plant leaves and fruits. In this study we undertook a proteomic approach to investigate the molecular and biochemical mechanisms potentially involved in tomato fruit defence against the viral infection. The comparison of 2-D gels from control and TMV-infected but asymptomatic tomato fruits revealed changes in several proteins. The differential expression of peptidases, endoglucanase, chitinase and proteins participating in the ascorbate-glutathione cycle in infected fruits suggests that pathogenesis-related proteins and antioxidant enzymes may play a role in the protection against TMV infection. TMV coat protein appeared as a prominent spot in 2-D gels from TMV-infected asymptomatic fruits. A Triton X-114 phase-partitioning step of tomato protein extracts favoured the solubilisation of TMV coat protein and the enrichment of two aminopeptidases not present in control fruits. PMF and MS/MS data of the 2-D gel-isolated TMV coat protein is proposed as a powerful analysis method for the simultaneous tobamovirus detection, species determination and strain differentiation in virus-infected fruit commodities.

Capsid Proteins↗

Isolation of a mutant of Arabidopsis thaliana carrying two simultaneous mutations affecting tobacco mosaic virus multiplication within a single cell.

Tobacco mosaic virus strain Cg (TMV-Cg) infects A. thaliana systemically. In order to identify host factors involved in the multiplication of TMV-Cg, we isolated mutant of A. thaliana from an M2 population mutagenized by fast neutron irradiation, in which the accumulation of the coat protein in upper systemic leaves was reduced to low levels. The phenotype of the mutant, YS241, was controlled primarily by a single nuclear recessive mutation named tom2-1, which was distinct from tom1, a separate mutation which also affects TMV-Cg multiplication. The tom2-1 mutation affected the accumulation of TMV-related RNAs in protoplasts in a tobamovirus-specific manner, suggesting that the wild-type TOM2 gene product is necessary for efficient amplification of TMV-related RNAs within a single cell, through specific interaction with virus-coded factors. Furthermore, we found that YS241 contained a single dominant modifier named ttm1, which increased the efficiency of multiplication of TMV-Cg and a tomato strain of TMV in a tom2-1 genetic background, both in plants and in protoplasts. We propose that the ttm1 element might be a translocated form of the TOM2 gene.

Arabidopsis↗

Molecularly imprinted polymers for tobacco mosaic virus recognition.

Molecular imprinted Polymers (MIP) targeted for Tobacco mosaic virus (TMV) have been synthesized. Batch equilibrium studies using imprinted and non-imprinted polymer hydrogels in TMV and TNV solutions were conducted to determine virus-binding capacities. TMV-imprinted hydrogels showed increased binding to TMV (8.8 mg TMV/gpolymer) compared to non-imprinted hydrogels (4.2 mg TMV/gpolymer). Furthermore, TMV-imprinted hydrogels exhibited increased binding to TMV compared to TNV, while non-imprinted hydrogels bound similar amounts of TMV or TNV. This research has demonstrated that molecular imprinting of viruses can be used to selectively induce binding of target viruses based on shape differences of their virions.

Biocompatible Materials↗

Localization, conjugation, and function of salicylic acid in tobacco during the hypersensitive reaction to tobacco mosaic virus.

Salicylic acid (SA) is hypothesized to be a natural signal that triggers the systemic induction of pathogenesis-related proteins and disease resistance in tobacco. When Xanthi-nc (NN genotype) tobacco was inoculated with tobacco mosaic virus (TMV) there was an increase in endogenous SA in both inoculated and virus-free leaves. The highest levels of SA were detected in and around necrotic lesions that formed in response to TMV. Chemical and enzymatic hydrolysis of extracts from TMV-inoculated leaves demonstrated the presence of a SA conjugate tentatively identified as O-beta-D-glucosyl-SA. The SA conjugate was detected only in leaves that contained necrotic lesions and was not detected in phloem exudates or uninoculated leaves of TMV-inoculated Xanthi-nc tobacco. When exogenous SA was fed to excised tobacco leaves, it was metabolized within 10 hr. However, this reduction in free SA did not prevent the subsequent accumulation of the PR-1 family of pathogenesis-related proteins. The absence of SA accumulation in TMV-inoculated tobacco plants incubated at 32 degrees C was not a result of the glucosylation of SA. The addition of SA to the medium elevated levels of SA in the leaves of virus-free tobacco grown hydroponically. Increasing the endogenous level of SA in leaves to those naturally observed during systemic acquired resistance resulted in increased resistance to TMV, expressed as a reduction in lesion area. These data further support the hypothesis that SA is a likely natural inducer of pathogenesis-related proteins and systemic acquired resistance in TMV-inoculated Xanthi-nc tobacco.

Glucosides↗

Relationships between tobacco mosaic virus and the non-virus proteins.

1. The non-virus proteins, A4, B3, and B6, characteristically found in tobacco leaf infected with TMV exhibit specific immunochemical cross-reactions with serum prepared against the virus. The close immunochemical relations which occur among these proteins do not extend to any normal tobacco leaf proteins. 2. The rate of appearance of the non-virus proteins in newly infected cultured leaf tissue at various times after inoculation has been determined by immunochemical techniques and by direct isolation of the proteins. Both methods give comparable results. The non-virus proteins appear abruptly at about 220 hours after inoculation, when the TMV content is about one-third its final value. The amount of A4 rises rapidly and then levels off. The B6 content rises rapidly and continuously over the course of the experiment. B3 appears last, and increases in amount considerably more slowly than A4 and B6. 3. The isotope contents of TMV, B3, and B6 which appear in given intervals after inoculation in newly infected leaf cultured in nutrient containing N(15)H(4) have been compared. The isotope levels of concurrent TMV, B3, and B6 are identical within the experimental error. The isotope conditions employed in this experiment lead to the conclusion that this coincidence of N(15) levels means that the virus and non-virus proteins are probably synthesized at about the same time from the same non-protein source of nitrogen. 4. Possible interpretations of the available data on the non-virus proteins are discussed. It is likely that one or more of these proteins represents small protein units which occur in the TMV nucleoprotein.As they exist in the infected leaf, the non-virus proteins are probably no longer available to the biochemical processes which lead to TMV synthesis. They are probably not precursors of TMV protein in a temporal sense.

Nitrogen↗

Susceptibility and symptom development in Arabidopsis thaliana to Tobacco mosaic virus is influenced by virus cell-to-cell movement.

To identify host factors that regulate susceptibility to Tobacco mosaic virus (TMV), 14 Arabidopsis thaliana ecotypes were screened for their ability to support TMV systemic movement. The susceptibility phenotypes observed included one ecotype that permitted rapid TMV movement accompanied by symptoms, nine ecotypes that allowed a slower intermediate rate of systemic movement without symptoms, and four ecotypes that allowed little or no systemic TMV movement. Molecular comparisons between ecotypes representing the rapid (Shahdara), intermediate (Col-1), and slow (Tsu-1) movement phenotypes revealed a positive correlation between the ability of TMV to move cell to cell and its speed of systemic movement. Additionally, protoplasts prepared from all three ecotypes supported similar levels of TMV replication, indicating that viral replication did not account for differences in systemic movement. Furthermore, induction of the pathogenesis-related genes PR-1 and PR-5 occurred only in the highly susceptible ecotype Shahdara, demonstrating that reduced local and systemic movement in Col-1 and Tsu-1 was not due to the activation of known host defense responses. Genetic analysis of F2 progeny derived from crosses made between Shahdara and Tsu-1 or Col-1 and Tsu-1 showed the faster cell-to-cell movement phenotypes of Shahdara and Col-1 segregated as single dominant genes. In addition, the Shahdara symptom phenotype segregated independently as a single recessive gene. Taken together, these findings suggest that, within Arabidopsis ecotypes, at least two genes modulate susceptibility to TMV.

Arabidopsis↗

Complete uncoating of the 5' leader sequence of tobacco mosaic virus RNA occurs rapidly and is required to initiate cotranslational virus disassembly in vitro.

Destabilizing events required for subsequent cotranslational disassembly of tobacco mosaic virus (TMV) particles in vitro were studied. Brief treatment of U-32P-labelled TMV (strain vulgare or U2) with 1% SDS exposed only 2.5% of the RNA (160 5' nucleotides) in a susceptible subpopulation of virions. Limited uncoating occurred almost immediately and appeared to be synchronous because the amount of 5' oligonucleotide marker (omega) recovered remained constant throughout a 15 min period in SDS. Additional RNase T1-sensitive oligonucleotides were exposed only after 1 to 2 min in SDS. Coat protein (CP) subunits released from virions 'destabilized' by ultracentrifugation at between pH 7.2 and 9.2 were quantified using L-[35S]methionine-labelled particles of TMV strain U2. CP recovery and virus particle translation results were consistent with increasing numbers of virions uncoating for approximately 200 nucleotides. In the presence of sparsomycin (SPN), the TMV strain vulgare 5' leader and the first AUG codon can bind two 80S ribosomes. Electron microscopy of pH 7.5-treated TMV particles incubated in SPN-treated wheatgerm extract or rabbit reticulocyte lysate, showed that approximately 10% of virions complexed with one ribosome and approximately 10% with two bound ribosomes, confirming that omega at least had been uncoated. Nucleocapsids in these complexes were shorter than untreated TMV by 9 to 10 nm (i.e. equivalent to 192 to 217 nucleotides exposed). The template activities of virions pretreated at pH 7.2 to 9.2 were destroyed by RNase H when short cDNAs were hybridized to sequences at, or immediately 3' to, the first AUG codon. We propose that the complete 5' leader of TMV RNA interacts weakly with CP subunits and that this micro-instability is due to the absence of G residues and is essential for initiation of cotranslational virus disassembly.

Base Sequence↗

Induction of UDP-Glucose:Salicylic Acid Glucosyltransferase Activity in Tobacco Mosaic Virus-Inoculated Tobacco (Nicotiana tabacum) Leaves.

Salicylic acid (SA) is a putative signal that activates plant resistance to pathogens. SA levels increase systemically following the hypersensitive response produced by tobacco mosaic virus (TMV) inoculation of tobacco (Nicotiana tabacum L. cv Xanthi-nc) leaves. The SA increase in the inoculated leaf coincided with the appearance of a [beta]-glucosidase-hydrolyzable SA conjugate identified as [beta]-O-D-glucosylsalicylic acid (GSA). SA and GSA accumulation in the TMV-inoculated leaf paralleled the increase in the activity of a UDP-glucose:salicylic acid 3-O-glucosyltransferase (EC 2.4.1.35) ([beta]-GTase) capable of converting SA to GSA. Healthy tissues had constitutive [beta]-GTase activity of 0.076 milliunits g-1 fresh weight. This activity started to increase 48 h after TMV inoculation, reaching its maximum (6.7-fold induction over the basal levels) 72 h after TMV inoculation. No significant GSA or elevated [beta]-Gtase activity could be detected in the healthy leaf immediately above the TMV-inoculated leaf. The effect of TMV inoculation on the [beta]-GTase and GSA accumulation could be duplicated by infiltrating tobacco leaf discs with SA at the levels naturally produced in TMV-inoculated leaves (2.7-27.0 [mu]g g-1 fresh weight). Pretreatment of leaf discs with the protein synthesis inhibitor cycloheximide inhibited the induction of [beta]-GTase by SA and prevented the formation of GSA. Of 12 analogs of SA tested, only 2,6-dihydroxybenzoic acid induced [beta]-GTase activity.

Journal Article↗

Pathway of Salicylic Acid Biosynthesis in Healthy and Virus-Inoculated Tobacco.

Salicylic acid (SA) is a likely endogenous regulator of localized and systemic disease resistance in plants. During the hypersensitive response of Nicotiana tabacum L. cv Xanthi-nc to tobacco mosaic virus (TMV), SA levels rise dramatically. We studied SA biosynthesis in healthy and TMV-inoculated tobacco by monitoring the levels of SA and its likely precursors in extracts of leaves and cell suspensions. In TMV-inoculated leaves, stimulation of SA accumulation is accompanied by a corresponding increase in the levels of benzoic acid. 14C-Tracer studies with cell suspensions and mock-or TMV-inoculated leaves indicate that the label moves from trans-cinnamic acid to SA via benzoic acid. In healthy and TMV-inoculated tobacco leaves, benzoic acid induced SA accumulation. o-Coumaric acid, which was previously reported as a possible precursor of SA in other species, did not increase SA levels in tobacco. In healthy tobacco tissue, the specific activity of newly formed SA was equal to that of the supplied [14C]benzoic acid, whereas in TMV-inoculated leaves some isotope dilution was observed, presumably because of the increase in the pool of endogenous benzoic acid. We observed accumulation of pathogen-esis-related-1 proteins and increased resistance to TMV in benzoic acid- but not in o-coumaric acid-treated tobacco leaves. This is consistent with benzoic acid being the immediate precursor of SA. We conclude that in healthy and virus-inoculated tobacco, SA is formed from cinnamic acid via benzoic acid.

Journal Article↗