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510 results on '"Klessig Daniel F."'

3. Conserved nematode signalling molecules elicit plant defenses and pathogen resistance.

Author

Manosalva, Patricia, Manohar, Murli, von Reuss, Stephan H, Chen, Shiyan, Koch, Aline, Kaplan, Fatma, Choe, Andrea, Micikas, Robert J, Wang, Xiaohong, Kogel, Karl-Heinz, Sternberg, Paul W, Williamson, Valerie M, Schroeder, Frank C, and Klessig, Daniel F

Subjects
Animals, Nematoda, Pseudomonas syringae, Arabidopsis, Salicylic Acid, Cyclopentanes, Pheromones, Signal Transduction, Host-Parasite Interactions, Oxylipins, Plant Immunity
Abstract

Plant-defense responses are triggered by perception of conserved microbe-associated molecular patterns (MAMPs), for example, flagellin or peptidoglycan. However, it remained unknown whether plants can detect conserved molecular patterns derived from plant-parasitic animals, including nematodes. Here we show that several genera of plant-parasitic nematodes produce small molecules called ascarosides, an evolutionarily conserved family of nematode pheromones. Picomolar to micromolar concentrations of ascr#18, the major ascaroside in plant-parasitic nematodes, induce hallmark defense responses including the expression of genes associated with MAMP-triggered immunity, activation of mitogen-activated protein kinases, as well as salicylic acid- and jasmonic acid-mediated defense signalling pathways. Ascr#18 perception increases resistance in Arabidopsis, tomato, potato and barley to viral, bacterial, oomycete, fungal and nematode infections. These results indicate that plants recognize ascarosides as a conserved molecular signature of nematodes. Using small-molecule signals such as ascarosides to activate plant immune responses has potential utility to improve economic and environmental sustainability of agriculture.

Published
2015

4. Identification of multiple salicylic acid-binding proteins using two high throughput screens

Author

Manohar, Murli, Tian, Miaoying, Moreau, Magali, Park, Sang-Wook, Choi, Hyong Woo, Fei, Zhangjun, Friso, Giulia, Asif, Muhammed, Manosalva, Patricia, von Dahl, Caroline C, Shi, Kai, Ma, Shisong, Dinesh-Kumar, Savithramma P, O'Doherty, Inish, Schroeder, Frank C, van Wijk, Klass J, and Klessig, Daniel F

Subjects
Biotechnology, salicylic acid, salicylic acid-binding proteins, salicylic acid signaling, plant immunity, disease resistance, Plant Biology
Abstract

Salicylic acid (SA) is an important hormone involved in many diverse plant processes, including floral induction, stomatal closure, seed germination, adventitious root initiation, and thermogenesis. It also plays critical functions during responses to abiotic and biotic stresses. The role(s) of SA in signaling disease resistance is by far the best studied process, although it is still only partially understood. To obtain insights into how SA carries out its varied functions, particularly in activating disease resistance, two new high throughput screens were developed to identify novel SA-binding proteins (SABPs). The first utilized crosslinking of the photo-reactive SA analog 4-AzidoSA (4AzSA) to proteins in an Arabidopsis leaf extract, followed by immuno-selection with anti-SA antibodies and then mass spectroscopy-based identification. The second utilized photo-affinity crosslinking of 4AzSA to proteins on a protein microarray (PMA) followed by detection with anti-SA antibodies. To determine whether the candidate SABPs (cSABPs) obtained from these screens were true SABPs, recombinantly-produced proteins were generated and tested for SA-inhibitable crosslinking to 4AzSA, which was monitored by immuno-blot analysis, SA-inhibitable binding of the SA derivative 3-aminoethylSA (3AESA), which was detected by a surface plasmon resonance (SPR) assay, or SA-inhibitable binding of [(3)H]SA, which was detected by size exclusion chromatography. Based on our criteria that true SABPs must exhibit SA-binding activity in at least two of these assays, nine new SABPs are identified here; nine others were previously reported. Approximately 80 cSABPs await further assessment. In addition, the conflicting reports on whether NPR1 is an SABP were addressed by showing that it bound SA in all three of the above assays.

Published
2015

5. Identification of multiple salicylic acid-binding proteins using two high throughput screens.

Author

Manohar, Murli, Tian, Miaoying, Moreau, Magali, Park, Sang-Wook, Choi, Hyong Woo, Fei, Zhangjun, Friso, Giulia, Asif, Muhammed, Manosalva, Patricia, von Dahl, Caroline C, Shi, Kai, Ma, Shisong, Dinesh-Kumar, Savithramma P, O'Doherty, Inish, Schroeder, Frank C, van Wijk, Klass J, and Klessig, Daniel F

Subjects
disease resistance, plant immunity, salicylic acid, salicylic acid signaling, salicylic acid-binding proteins, Biotechnology, Plant Biology
Abstract

Salicylic acid (SA) is an important hormone involved in many diverse plant processes, including floral induction, stomatal closure, seed germination, adventitious root initiation, and thermogenesis. It also plays critical functions during responses to abiotic and biotic stresses. The role(s) of SA in signaling disease resistance is by far the best studied process, although it is still only partially understood. To obtain insights into how SA carries out its varied functions, particularly in activating disease resistance, two new high throughput screens were developed to identify novel SA-binding proteins (SABPs). The first utilized crosslinking of the photo-reactive SA analog 4-AzidoSA (4AzSA) to proteins in an Arabidopsis leaf extract, followed by immuno-selection with anti-SA antibodies and then mass spectroscopy-based identification. The second utilized photo-affinity crosslinking of 4AzSA to proteins on a protein microarray (PMA) followed by detection with anti-SA antibodies. To determine whether the candidate SABPs (cSABPs) obtained from these screens were true SABPs, recombinantly-produced proteins were generated and tested for SA-inhibitable crosslinking to 4AzSA, which was monitored by immuno-blot analysis, SA-inhibitable binding of the SA derivative 3-aminoethylSA (3AESA), which was detected by a surface plasmon resonance (SPR) assay, or SA-inhibitable binding of [(3)H]SA, which was detected by size exclusion chromatography. Based on our criteria that true SABPs must exhibit SA-binding activity in at least two of these assays, nine new SABPs are identified here; nine others were previously reported. Approximately 80 cSABPs await further assessment. In addition, the conflicting reports on whether NPR1 is an SABP were addressed by showing that it bound SA in all three of the above assays.

Published
2014

15. Nitric Oxide and Salicylic Acid Signaling in Plant Defense

Author

Klessig, Daniel F., Durner, Jorg, Noad, Robert, Navarre, Duroy A., Wendehenne, David, Kumar, Dhirendra, Zhou, Jun Ma, Shah, Jyoti, Zhang, Shuqun, Kachroo, Pradeep, Trifa, Youssef, Pontier, Dominique, Lam, Eric, and Silva, Herman

Published
2000

23. Public Sector Collaboration for Agricultural IP Management

Author

Atkinson, Richard, Beachy, Roger N., Conway, Gordon, Cordova, France A., Fox, Marye Anne, Holbrook, Karen A., Klessig, Daniel F., McCormick, Richard L., McPherson, Peter M., Rawlings III, Hunter R., Rapson, Rip, Vanderhoef, Larry N., Wiley, John D., and Young, Charles E.

Subjects
The Research University, The University and the Economy
Abstract

Commentary about intellectual property rights by Richard C. Atkinson and others.

Published
2003

50. Aspirin’s Active Metabolite Salicylic Acid Targets High Mobility Group Box 1 to Modulate Inflammatory Responses

Author

Choi, Hyong Woo, Tian, Miaoying, Song, Fei, Venereau, Emilie, Preti, Alessandro, Park, Sang-Wook, Hamilton, Keith, Swapna, G. V. T., Manohar, Murli, Moreau, Magali, Agresti, Alessandra, Gorzanelli, Andrea, De Marchis, Francesco, Wang, Huang, Antonyak, Marc, Micikas, Robert J., Gentile, Daniel R., Cerione, Richard A., Schroeder, Frank C., Montelione, Gaetano T., Bianchi, Marco E., and Klessig, Daniel F.

Published
2015
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