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 1,009 records · Page 56Linked to original sources

Comparative sensitivity of different ELISA methods for detecting monoclonal antibodies to viruses.

Five different ELISA procedures using alkaline phosphatase conjugates were compared for their sensitivity in detecting binding activity in nine monoclonal antibodies raised against tobacco mosaic virus (TMV). The two procedures in which antigen was used to coat the microtiter plates were found to be unreliable for testing the activity of monoclonal antibodies. The two most sensitive procedures utilized a multilayered sandwich of which one component imperatively had to be an avian antibody devoid of serological cross-reactivity with mammalian globulins. The avian antibody was obtained from the egg yolk of immunized chickens. In the two most sensitive assays, four out of nine monoclonal antibodies raised against TMV were also reactive with the dissociated viral protein subunits.

Antibodies, Monoclonal↗

Isolation and characterization of Fc-receptors shed from human peripheral mononuclear cells.

Supernatants of human peripheral mononuclear cells containing membrane components shed in consequence of 4--37 degrees temperature shift were used as source for isolation of Fc-receptors (FcR). Aggregated IgG1 myeloma protein and TMV-anti-TMV complexes proved suitable sorbents to adsorb quantitatively and specifically the FcR-s. The isolated FcR interacts only with IgG and not with IgM. No haemagglutination was observed when the isolated FcR was incubated with sensitized human Rh+ red blood cells. Complement dependent lysis of sheep red blood cells was not inhibited by the isolated FcR-s. The interaction between IgG and SpA from Staphylococcus aureus (Cowan I) bacteria was not inhibited when red blood cells sensitized with IgG were preincubated with the isolated FcR-s. The differences between the FcR-like material isolated from supernatants of peripheral human mononuclear cells and those secreted by stimulated T cells or produced by lymphoblastoid cell lines are discussed.

Binding Sites, Antibody↗

Protein synthesizing system from wheat germ: efficient translation of synthetic and natural messages.

Optimum conditions for translation of eukaryotic, prokaryotic and synthetic templates in wheat germ cell-free extract were determined. 1. Translation of eukaryotic message (BMV RNA and TMV RNA) was at optimum at the same concentrations of K+, Mg(2+), HEPES and spermine. In optimal conditions the efficiency of translation was high, for BMV RNA being equal to 220 pmoles and for TMV RNA, to 280 pmoles of leucine incorporated per 1 microgram of template. Prokaryotic template (Qbeta RNA) was translated under different ionic conditions. 2. Translation of synthetic template [poly(U)] was at optimum at fairly higher concentrations of K+ and Mg(2+) than those optimal for natural template translation. 3. Efficient translation of natural and synthetic templates depends on complete removal of inhibitors found in the wheat germ cell-free extract. Action of these inhibitors could be mimicked by adenine nucleotides.

Adenine Nucleotides↗

[Kinetic properties of peroxidase from intact and virus-infected tobacco leaves].

The kinetic properties of peroxidase from tobacco leaves (var. Xanthie and Samsun) infected with various viruses (TMV, Xt and Xy, were compared. The enzyme from intact plant grown under similar conditions was used as control. The pH dependencies of the peroxidase activity for o-dianisidine peroxidation in infected and control plants were identical. Viral infection produces a dramatic effect on the kinetic properties of the enzyme: the KM values for o-dianisidine were decreased by 20-40% and those for H2O2 - by 30-40% in the case of the Samsun var. infected with TMV and Xanthie var. infected with a highly virulent strain of potato X-virus. The decrease of these values in plants infected with a weakly virulent strain of the virus was insignificant.

Kinetics↗

[Induction of plant resistance to the tobacco mosaic virus with a double-stranded poly(G)-poly(C) complex].

Inoculation of double-stranded polyribonucleotide poly(G) . poly(C) complex in a concentration of 50-200 micrograms/mg into tobacco and thornapple leaves was found to produce resistance of the plants to subsequent infection with tobacco mosaic virus (TMV) manifested in decreased number and size of local virus lesions. The induced resistance may spread over the plant and be found in the upper untreated leaves. The level of systemic resistance, however, is much lower than that of the resistance demonstrated in the injected leaves. Actinomycin D (5 micrograms/ml) had no significant effect on the number but stimulated the growth of lesions developing in leaves injected with poly(G) . poly(C) as well as increased their number in the upper leaves of the same plants proximal to the treated ones. Development of tobacco resistance to TMV was accompanied by changes in the activity of terminal oxidases, particularly peroxidase. Possible mechanisms of formation of induced resistance are discussed.

Plant Diseases↗

The effect of histone-mRNA interaction in protein synthesis.

The effect of lysine-rich and arginine-rich histones on selective inhibition of translation of mRNAs of tobacco mosaic virus (TMV), brome mosaic virus (BMV) and luciferase, in rabbit reticulocyte (RRL) was evaluated. Nuclease-treated RRL were supplemented with an appropriate mRNA and incubated with lysine-rich or arginine-rich histones at 5 and 2.5 micrograms/100 microliters lysate at 30 degrees C. Protein synthesis was measured as incorporation of 3H-leucine into protein for 24 min. The lysine-rich histone was more inhibitory than arginine-rich histone. At 5 and 2.5 micrograms/100 microliters lysate concentration, the lysine-rich histone inhibited translation of TMV mRNA by 57% and 35%, respectively, after 24 min. The corresponding values for arginine-rich histone were 31% and 13%. Both histones had a more inhibitory effect on the translation of viral mRNA than luciferase mRNA. Arginine-rich histone at 2.5 micrograms/100 microliters lysate did not cause any inhibition of luciferase mRNA. The spectrophotometric analysis of histone-mRNA mixtures at 280 nm indicated that, compared with arginine-rich histone, lysine-rich histone had a stronger affinity for mRNA.

Animals↗

Tobamoviruses: Advances in Molecular Biology, Host Interactions and Integrated Disease Management.

Tobamoviruses (viruses in the genus Tobamovirus, family Virgaviridae) lead to major yield losses in economically important crops around the world. In this review, we go beyond the canonical gene expression framework by integrating recent discoveries of reverse open reading frames (rORFs) on the negative-strand RNA. These rORFs have only been experimentally validated in cucumber green mottle mosaic virus (CGMMV), with predicted sequence-conserved homologs across a subset of the genus, including TMV, ToBRFV, and PMMoV. However, they are not universally present in all tobamoviruses. We systematically dissect the infection cycle-from disassembly and replication to cell-to-cell and systemic movement-with an emphasis on the host factors hijacked at each stage. We synthesize current understanding of plant antiviral immunity, focusing on RNA silencing and NLR receptor-mediated resistance as two pillars of defense, along with the transcription factors and microRNAs that orchestrate these responses. We critically evaluate the experimental evidence for both plant defenses and viral counter-strategies, noting that many mechanistic models derive from limited model systems. We further characterize host genetic resistance and susceptibility factors applicable to crop breeding. These resources include dominant NLR and non-NLR resistance, as well as recessive resistance derived from modified host susceptibility genes. We address how viral mutations, recombination and fitness trade-offs undermine resistance durability. We then evaluate their practical deployment through conventional breeding, the exploitation of quantitative resistance, and genome editing, and outline associated agronomic drawbacks and regulatory constraints. Using ToBRFV as a case study, we analyze its epidemiological traits and assess the current arsenal of surveillance tools, from field diagnostics to remote sensing. Finally, we survey management strategies across a spectrum of maturity. Some approaches, including sanitation protocols and conventionally bred resistant cultivars, have proven effective under field conditions. The first dsRNA-based biopesticide has recently been registered in China, while other biological control agents and low-risk chemical approaches remain largely at the experimental stage. We also discuss the bottlenecks that impede lab-to-field transition and highlight promising solutions such as precision breeding and evolution-oriented cultivar deployment. By bridging molecular virology, epidemiology, and integrated disease management, this review provides a critical, bench-to-field framework for the sustainable control of tobamoviruses.

TMV↗

Purified cholera toxin B subunit from transgenic tobacco plants possesses authentic antigenicity.

Cholera toxin B subunit (CTB) mature protein was stably expressed in transgenic tobacco plants under the control of the CaMV 35S promoter and TMV Omega fragment. Fusion of the PR1b signal peptide coding sequence to the CTB mature protein gene increased the expression level by 24-fold. The tobacco-synthesized CTB (tCTB) was purified to homogeneity by a single step of immunoaffinity chromatography. The purified tCTB is predominantly in the form of pentamers with molecular weight identical to the native pentameric CTB, indicating that the PR1b-CTB fusion protein has been properly processed in tobacco cells. Furthermore, by immunodiffusion and immunoelectrophoresis, we have shown that the antigenicity of the purified tCTB is indistinguishable from that of the native CTB protein.

Animals↗

Antibody-based surface plasmon resonance detection of intact viral pathogen.

Surface plasmon resonance (SPR) technique was used to directly detect an intact form of insect pathogen: the baculovirus, Autographa californica multiple nuclear polyhedrosis virus (AcMNPV). An SPR sensor chip with three bio-functional layers was used to detect the intact AcMNPV: amine-reactive crosslinker with a disulfide bond that chemisorbs to gold film, Protein A, and a mouse IgG monoclonal antibody raised against a surface protein of the target viral pathogen. A two-channel (reference & test) micro-fluidic SPR system is used for reliable measurement. Bio-specific response to the AcMNPV is compared with the response for tobacco mosaic virus (TMV) as control. Successive exposure of the sensor chip to both viruses verifies a specific response to AcMNPV. This serves as a prerequisite to the development of a new type of viral pathogen detection sensors.

Antibodies, Viral↗

Characterization of epitopes shared by alpha-melanocyte-stimulating hormone (alpha-MSH) and the 150-kD neurofilament protein (NF150): relationship to neurotrophic sequences.

Immunoblot techniques and immunohistochemistry have been used to investigate epitopes shared by alpha-melanocyte-stimulating hormone (alpha-MSH) and the 150-kD neurofilament protein (NF150). Three anti-alpha-MSH antisera (namely 31H2T, 4394, and M5) from a total of 12 sera were found to react with NF150. The three crossreacting sera are different in their binding properties to peptide fragments related to alpha-MSH, suggesting that at least two distinct epitopes are shared by NF150 and alpha-MSH. The only known sequence common to NF150 and alpha-MSH, the N-terminal Ac-S-Y residues, appears to be essential for binding of sera 31H2T and 4394. However, the binding of antiserum M5 involves other, currently unknown, similarities between NF150 and alpha-MSH. This is shown by the binding of M5 to peptides such as ACTH(4-10), which do not contain the N-terminal Ac-S-Y sequence. Binding of M5 to tobacco mosaic virus coat protein (TMV-coat protein), which is homologous with alpha-MSH and NF150 in its Ac-S-Y residues, was negligible. The peptide structures that are recognized by M5 have previously been shown to exert neurotrophic activity. The data are discussed in the light of the hypothesis that similarity between NF150 and alpha-MSH, as illustrated by binding to M5, may be significant in the neurotrophic activity of MSH-related peptides.

Animals↗

Incidence of Leptosphaerulina crassiasca in symptomless leaves of peanut in southern India.

A Loculoascomycete fungus belonging to the genus Leptosphaerulina was found to survive as symptomless endophyte in the leaflets and rachis of peanut plant (TMV 7). Based on morphological and colony characteristics, it is identified as Leptosphaerulina crassiasca, a fungus that causes the pepper spot and leaf scorch diseases in peanut. Although several common endophytic fungi were recovered from the leaves of peanut, L . crassiasca showed a high relative density of infection. Owing to its endophytic nature, its pathogenicity could not be proved by infection studies. However, its identification as L. crassiasca suggests that this pathogen survives as symptomless endophyte in its host. There are limited studies on fungal endophytes of cultivated crops and hence, the present observation underlines the need to know more about the biology of endophytic fungi of crop plants.

Arachis↗

Pokeweed antiviral protein isoforms PAP-I, PAP-II, and PAP-III depurinate RNA of human immunodeficiency virus (HIV)-1.

Pokeweed antiviral protein (PAP) is a naturally occurring broad-spectrum antiviral agent with potent anti-human immunodeficiency virus (HIV)-1 activity by an as yet undeciphered molecular mechanism. In the present study, we sought to determine if PAP is capable of recognizing and depurinating viral RNA. Depurination of viral RNA was monitored by directly measuring the amount of the adenine base released from the viral RNA species using quantitative high-performance liquid chromatography. Our findings presented herein provide direct evidence that three different PAP isoforms from Phytolacca americana (PAP-I from spring leaves, PAP-II from early summer leaves, and PAP-III from late summer leaves) cause concentration-dependent depurination of genomic RNA (63 to 400 pmols of adenine released per micrograms of RNA) purified from human immunodeficiency virus type-I (HIV-I), plant virus (tobacco mosaic virus (TMV), and bacteriophage (MS 2). In contrast to the three PAP isoforms, ricin A chain (RTA) failed to cause detectable depurination of viral RNA even at 5 microM, although it was as effective as PAP in inhibiting protein synthesis in cell-free translation assays. PAP-I, PAP-II, and PAP-III (but not RTA) inhibited the replication of HIV-1 in human peripheral blood mononuclear cells with IC(50) values of 17 nM, 25 nM, and 16 nM, respectively. These findings indicate that the highly conserved active site residues responsible for the depurination of rRNA by PAP or RTA are not sufficient for the recognition and depurination of viral RNA. Our study prompts the hypothesis that the potent antiviral activity of PAP may in part be due to its unique ability to extensively depurinate viral RNA, including HIV-1 RNA.

Anti-HIV Agents↗

Protection of mice against challenge with foot and mouth disease virus (FMDV) by immunization with foliar extracts from plants infected with recombinant tobacco mosaic virus expressing the FMDV structural protein VP1.

A tobacco mosaic virus (TMV)-based vector has been used to express in plants the complete open reading frame coding for VP1, the major immunogenic protein of foot and mouth disease virus (FMDV). In vitro RNA transcripts were inoculated into Nicotiana benthamiana plants and detectable amounts of recombinant VP1 were identified by Western blot as soon as 4 days postinfection. Foliar extracts prepared from infected leaves were injected intraperitoneally into mice and all of the immunized animals developed a specific antibody response to both the complete virus particle and the major immunogenic region as determined by ELISA and Western blot analysis. Most importantly, all immunized mice developed a protective immune response against experimental challenge with virulent FMDV. To our knowledge, this is the first report showing the expression of a complete open reading frame of an antigenic foreign protein in plants, using a recombinant plant virus, in sufficient quantity to permit use of the crude plant extract as an experimental immunogen to protect animals against virus challenge.

Animals↗

Nuclear localization of turnip crinkle virus movement protein p8.

Turnip crinkle virus (TCV) is a single-stranded positive-sense RNA virus of the Carmovirus genus. Two of its five open reading frames (ORFs), encoding proteins of 8 and 9 kDa, are required for cell-to-cell movement of the virus. These movement proteins (MPs) were fused to green fluorescent protein (GFP) to determine their cellular localization. In protoplasts, p9-GFP, like GFP itself, is found throughout the cytoplasm, as well as in cell nuclei. In contrast, p8-GFP was confined to the cell nucleus. Similar localization patterns were observed when specific small peptide epitopes were fused to p8 and p9 proteins instead of GFP. The cytoplasmic localization of p9-GFP and nuclear localization of p8-GFP were also detected in leaves after particle bombardment of DNA encoding these fusion proteins or after overexpression of p8-GFP in transgenic Arabidopsis seedlings. The expression of the GFP fusion proteins by recombinant TCV viruses in infected protoplasts or on inoculated Arabidopsis leaves produced similar patterns. Unlike TMV-MP and other MPs studied to date, no obvious punctuate expression in the cell wall or association with the cytoskeleton was detected. The sequence analysis of p8 revealed two unique nuclear localization signals (NLSs), which were not conserved within p8 homologues of other viruses in the genus Carmovirus. Mutation in either of these NLSs did not disrupt the nuclear localization of p8-GFP. However, when both NLSs were mutated, p8-GFP expression was no longer restricted to cell nuclei. The NLSs are not required for cell-to-cell movement; TCV recombinant viruses mutated in one or both NLSs could still facilitate cell-to-cell movement of the virus. The nuclear localization of p8 suggests a novel function for this protein in the cell nucleus.

Amino Acid Sequence↗

Mapping of the Tobacco mosaic virus movement protein and coat protein subgenomic RNA promoters in vivo.

The Tobacco mosaic virus movement protein (MP) and coat protein (CP) are expressed from 3'-coterminal subgenomic RNAs (sgRNAs). The transcription start site of the MP sgRNA, previously mapped to positions 4838 (Y. Watanabe, T. Meshi, and Y. Okada (1984), FEBS Lett. 173, 247-250) and 4828 (K. Lehto, G. L. Grantham, and W. O. Dawson (1990), Virology 174, 145-157) for the TMV OM and U1 strains, respectively, has been reexamined and mapped to position 4838 for strain U1. Sequences of the MP and CP sgRNA promoters were delineated by deletion analysis. The boundaries for minimal and full MP sgRNA promoter activity were localized between -35 and +10 and -95 and +40, respectively, relative to the transcription start site. The minimal CP sgRNA promoter was mapped between -69 and +12, whereas the boundaries of the fully active promoter were between -157 and +54. Computer analysis predicted two stem-loop structures (SL1 and SL2) upstream of the MP sgRNA transcription start site. Deletion analysis and site-directed mutagenesis suggested that SL1 secondary structure, but not its sequence, was required for MP sgRNA promoter activity, whereas a 39-nt deletion removing most of the SL2 region increased MP sgRNA accumulation fourfold. Computer-predicted folding of the fully active CP sgRNA promoter revealed one long stem-loop structure. Deletion analysis suggested that the upper part of this stem-loop, located upstream of the transcription start site, was essential for transcription and that the lower part of the stem had an enhancing role.

Base Sequence↗

Plants expressing tomato golden mosaic virus AL2 or beet curly top virus L2 transgenes show enhanced susceptibility to infection by DNA and RNA viruses.

The AL2 gene of the geminivirus tomato golden mosaic virus (TGMV) encodes a transcriptional activator protein (TrAP) that is required for efficient expression of the viral coat protein (CP) and BR1 gene promoters. In contrast, L2, the positional homolog of AL2 in the related beet curly top virus (BCTV), is not required for CP expression, raising questions about the functional relationship between the AL2 and L2 gene products. In this study, transgenic Nicotiana benthamiana and N. tabacum var. Samsun plants expressing a truncated AL2 gene (AL2(1-100), lacking the activation domain) or full-length L2 were prepared. These transgenic plants showed a novel enhanced susceptibility (ES) phenotype following inoculation with TGMV, BCTV, or tobacco mosaic virus (TMV), an unrelated RNA virus. ES is characterized by a reduction in the mean latent period (from 1 to 9 days) and by a decrease in the inoculum concentration required to infect transgenic plants (ID50 reduced 6- to 60-fold). However, ES does not result in an enhancement of disease symptoms, and viral nucleic acids do not accumulate to substantially greater levels in infected transgenic plants. That both viral transgenes condition ES suggests that their products share the ability to suppress a host stress or defense response that acts against DNA and RNA viruses. The data further indicate that the transcriptional activation activity of AL2 protein is not required for suppression. The nature of the response targeted by the AL2 and L2 gene products is discussed.

Geminiviridae↗

Principles and background for the construction of transgenic plants displaying multiple virus resistance.

We investigated the possibility of reconstructing the 2'-5' oligoadenylate (2-5A) pathway into the plant kingdom to achieve multiple virus resistance. Differently phosphorylated 2-5A trimers and tetramers inhibited TMV RNA translation in cell-free systems. In wheat germ extracts the most potent inhibitors were nonphosphorylated forms of 2-5A. Triphosphorylated forms of 2-5A were deposphorylated and hydrolysed in plant extracts. Since we could not detect homologous DNA to mammalian 2-5A synthetase cDNA in tobacco or potato, we cloned rat 2-5A synthetase cDNA and transformed it by the Agrobacterium-mediated mechanism into tobacco and potato. Transformed tobacco plants were resistant to PVS infection and propagation of PVX was reduced. In transgenic potatoes tolerance to PVX and, in one transgenic clone, also to PVY was observed.

2',5'-Oligoadenylate Synthetase↗

Dark induction and subcellular localization of the pathogenesis-related PRB-1b protein.

The PRB-1b gene codes for a basic-type pathogenesis-related protein of the PR-1 family of tobacco. PRB-1b mRNA accumulation is induced in response to biotic and abiotic elicitors, such as TMV, ethylene, salicylic acid, alpha-amino butyric acid and darkness. In order to determine the location of elements that control dark-regulated PRB-1b gene expression, we tested promoter, transcribed regions and 3'-downstream regions of the gene for their ability to respond to dark induction in transgenic tobacco plants. An ethylene-inducible promoter region of 863 bp was not able to confer dark induction to a beta-glucuronidase reporter gene, while a construct containing the transcribed region of the gene and 3'-downstream sequences, driven by the cauliflower mosaic virus 35S promoter, was correctly dark-regulated. The results indicate that dark-induction of the PRB-1b gene can be controlled by 3'-downstream elements at the transcriptional level or by transcribed sequences at the post-transcriptional level. A circadian clock regulation of the PRB-1b gene was excluded, as fluctuations of PRB-1b transcript levels were not observed in plants placed in constant light or darkness. Subcellular localization of the PRB-1b protein was also determined, in tobacco protoplasts preparations and in cell cultures. The PRB-1b polypeptide was predominantly detected in protoplast vacuoles and was not secreted to the media in cell cultures. These results support an intracellular localization for the PRB-1b protein, as reported for other basic-type components of the pathogenesis-related proteins family.

Cells, Cultured↗