Daniel Klessig

Professor
Daniel Klessig
dfk8@cornell.edu
Office/Lab: 223/206-210
Phone: 607-254-4560
Office/Lab: 223/206-210
Email: dfk8@cornell.edu
Office Phone: 607-254-4560
Lab Phone: 607-254-1255
Affiliations: Adjunct Professor, Section of Plant Pathology & Plant-Microbe Biology / School of Integrative Plant Science / Cornell University
Graduate Fields: Plant Biology; Plant Pathology & Plant-Microbe Biology
Research Overview

Our research is focused on understanding, at the biochemical, molecular and cellular levels, how plants protect themselves against microbial pathogens. The major goal is to determine the mechanisms of action of salicylic acid (SA) in activation and regulation of the plant’s immune responses. We also are now employing the technology developed and knowledge gained from our work on SA and plant immunity to identify the targets of aspirin (acetyl SA) and its major metabolite SA in humans. The molecular/biochemical function of CRT1/MORC1 in multiple levels of plant immunity is also being deciphered. In addition, in collaboration with Frank Schroeder the induction of plant immune responses by nematode ascarosides is being investigated.

 A. Systemic acquired resistance (SAR) in Arabidopsis, tobacco, and potato

Methyl salicylate (MeSA)

Methyl salicylate (MeSA) – mediated induction of systemic acquired resistance

Systemic acquired resistance (SAR) is a state of heightened defense to a broad spectrum of pathogens that is activated throughout a plant following local infection. Development of SAR requires translocation of one or more mobile signals from the site of infection through the vascular system to distal (systemic) tissues. Between 2007 and 2011 we reported the identification of the first long-distance mobile signal, methyl salicylate, in several plant species in a series of five papers. In 2011 we published the inter-relationship between methyl salicylate and lipid signal(s). More recently several other mobile signals have been reported in addition to methyl salicylate and a DIR1/GLY1-dependent lipid signal. These include the dicarboxylic acid azelaic acid, the abietane diterpenoid dehydroabietinal, jasmonic acid, and the amino acid-derivative pipecolic acid. Our 2012 mini-review (Dempsey and Klessig) entitled “SOS – too many signals for systemic acquired resistance?” attempts to make sense of these newly discovered mobile signals.

B. Identification and characterization of new SA-binding proteins

In addition to disease resistance, SA affects many other plant processes, including flowering, seed germination, adventitious root initiation, and thermogenesis. In order to identify new SABPs through which SA exerts its many effects, we developed during the past several years two high throughput screens to identify candidate SABPS (cSABPs). The first utilizes SA analogs 4-azido SA (4AzSA) or 3-aminoethyl SA (3AESA), in conjunction with either a photoaffinity labeling technique or surface plasmon resonance (SPR)-based technology, to identify and evaluate cSABPs from Arabidopsis. The photoaffinity labeling and SPR-based approaches appear to be more sensitive than the traditional approach for identifying plant SA-binding activity using size exclusion chromatography with radiolabeled SA, as these proteins exhibited little to no SA-binding activity in such an assay. These novel approaches therefore complement conventional techniques and has help dissect the SA signaling network in plants. Our first results were reported in 2012 (Tian et al., Plant J 72:1027, 2012).

The second high throughput screen utilizes a protein microarray (PMA) to identify proteins that bind SA analogs. The initial screen, which used a 5,000 PMA (developed by S. Popescu, S. Dinesh-Kumar and M. Snyder) in conjunction with photoaffinity crosslinking to 4AzSA, yielded several dozen cSABPs, most of these were false positives. After further optimization we screened a new 10,000 PMA. Bioinformatic analysis indicated that the results were much more reproducible from microarray to microarray than in the previous screen. Using a stringent cutoff of P < 0.01, 41 cSABPs were identified. A subset of these, together with a subset from the 4AzSA crosslinking – immuno-selection screen were further characterized. The results were reported in Manohar et al., 2015, which revealed the identity of nine new SA-binding proteins (SABPs) and summarized the results from our two new, powerful screens for SABPs, which led to the discovery of a total of 23 new SABPs.

B1. AtGAPDH

     Several members of the Arabidopsis GAPDH family, including two chloroplast-localized and two cytosolic isoforms, were identified as SABPs. Since cytosolic GAPDH is an important host factor involved in Tomato Bushy Stunt Virus (TBSV) replication, the effects of SA on its replication were evaluated in collaboration with Peter Nagy using three different replication system. SA inhibited TBSV replication by disrupting the binding of cytosolic GAPDH to the negative (-) RNA strand of TBSV. Thus, this study reveals a novel mechanism through which SA mediates resistance by targeting host factors used for virus replication (Tian et al., 2015).

B2. AtHMGB3

Our results indicate that, as in humans, Arabidopsis HMGB3 functions as a Damage-Associated Molecular Pattern (DAMP), and that SA modulates this function. We discovered that extracellular HMGB3 induced a series of innate immune responses, including i) MAPK activation, ii) enhanced defense-related gene expression, iii) callose deposition, and iv) enhanced resistance to Botrytis cinerea, that are activated via a pathway that is depended on the receptor-like kinases BAK1 and BKK1. Further supporting its role as a DAMP, HMGB3 was released into the apoplast following B. cinerea infection. In addition, silencing multiple HMGB genes in transgenic plants reduced resistance to B. cinerea. HMGB3 exhibited authentic SA-binding activity in vitro, and its ability to activate MAPKs, induce callose deposition, and enhance resistance was inhibited by SA in vivo. These findings are consistent with our recent discovery that SA binds human HMGB1 (HsHMGB1), thereby inhibiting its pro-inflammatory activities (see below – Choi et al., 2015). Sequence alignment revealed that SA-binding sites in HsHMGB1 are conserved in the HMG box domain of Arabidopsis HMGB proteins. An SA-binding site mutant of HMGB3 retained its DAMP activity, but this activity was no longer inhibited by SA, consistent with its reduced ability to bind SA. Together these results provide cross-kingdom evidence that HMGB proteins function as DAMPs and that SA is their conserved inhibitor.

How does aspirin work in people?C. Human SAPBs

During the past three years, more of our focus has been on identifying and characterizing novel targets of SA, the active ingredient of aspirin that mediates aspirin’s multiple pharmacological effects, such as reduction in fever, pain, and inflammation, as well as the risk of stroke, heart attack, and cancer. We have discovered that SA binds to human High Mobility Group Box 1 (HMGB1) and Glyceraldehyde 3-Phosphate Dehydrogenase (GAPDH) and alters their activities.

C1. HsHMGB1

We demonstrated that HMGB1 is a novel SA-binding protein using affinity chromatography, 4AzSA crosslinking, SPR, and NMR. SA-binding sites on HMGB1 were identified in the HMG-box domains by NMR and confirmed by mutational analysis. Extracellular HMGB1 is a DAMP, with multiple redox states. SA suppresses both the chemo-attractant activity of fully reduced HMGB1 and the increased expression of pro-inflammatory cytokine genes and COX-2 gene induced by disulfide HMGB1. Natural and synthetic SA derivatives with stronger binding affinity for HMGB1 than SA and greater potency for inhibition of HMGB1 were identified, providing proof-of-concept that new SA-based molecules with high efficacy against inflammation are attainable. An HMGB1 protein mutated in one of the SA-binding sites identified by NMR chemical shift perturbation studies retained chemo-attractant activity, but lost binding of and inhibition by SA and its derivatives, thereby firmly establishing that SA binding to HMGB1 directly suppresses its pro-inflammatory activities. Identification of HMGB1 as a pharmacological target of SA/aspirin provides new insights into the mechanisms of action of one of the world’s longest and most used natural and synthetic drugs (Choi et al., 2015). We are trying to extend this work to animal model systems for various diseases including arthritis, cancer, and Alzheimer’s disease with collaborators. In addition, HMGB1 and GAPDH are being used to identify new, more potent SA derivatives – either synthetic or from medicinal plants. For more information, see the interview in MedicalResearch.com.

C2. HsGAPDH

In addition to its central role in glycolysis, GAPDH is a major participant in disease. GAPDH is a prime suspect in several neurodegenerative disorders, including Alzheimer’s, Parkinson’s, and Huntington’s diseases. In collaboration with Sol Snyder at Johns Hopkins, we found that SA and its more potent derivatives suppress nuclear translocation of GAPDH, induced by oxidative stress-like conditions, and the resulting cell death, just like the anti-Parkinson’s disease drug deprenyl (Choi et al., 2015). For additional information, see the interview in MedicalResearch.com.

D. CRT1/MORC1 characterization

Over the past several years we have characterized CRT1/MORC1 (Microrchidia) family, a subset of the GHKL ATPase superfamily, and discovered that it interacts with multiple immune receptors (R proteins and PAMP Recognition Receptors) and functions in multiple layers of plant immunity in Arabidopsis. CRT1/MORC1 localizes to endosomal-like vesicles but a small subpopulation translocates to the nucleus upon activation of immune responses (Kang et al., 2008, 2010, 2012). While the CRT1/MORC1 family positively modulates resistance in Arabidopsis and potato, in barley (Langen et al., 2014) and tomato this family negatively affects resistance, since its silencing results in enhanced resistance. To understand this species-specific effect of altering expression of CRT1/MORC1 on immunity, we took advantage of the differential effects in closely related tomato and potato. Using domain swapping and site-directed mutagenesis we determined that this species specificity is due to differences in the proteins themselves rather than the cellular environment in which these proteins function. This species specificity is determined by just four amino acid differences in the C-t region of these 650 amino acid proteins. We found that this C-t region also is required for i) protein dimerization and ii) interaction with 14 other proteins, iii) is phosphorylated, and iv) displays signaling activity (Manosalva et al., 2015).We recently discovered that both plant and human MORCs have DNA modifying activities similar to type II topoisomerases, but are unique in requiring additional factor(s) for full activity (Manohar et al. 2017). These findings provide important insight into their functions in gene silencing (plants and animals) and cancer (human).

E. Modulation of plant immunity by nematode ascarosides

This is our newest area of research and one that holds considerable commercial promise. It is done in collaboration with Frank Schroeder. We discovered that plant parasitic nematodes produce small molecules called ascarosides, an evolutionarily conserved family of nematode pheromones, and that plants respond to these nematode-specific molecular patterns by activating systemic defenses against a broad spectrum of pathogens. Picomolar to micromolar concentrations of ascr#18, the most abundant ascaroside in plant parasitic nematodes, induced hallmark defense responses, including the expression of genes associated with Microbe-Associated Molecular Pattern (MAMP)-triggered immunity and activation of MAPKs. Ascr#18 induced both SA- and JA-mediated defense signaling pathways, enhanced resistance to virulent viral and bacterial pathogens, and reduced cyst nematode infection in Arabidopsis. Furthermore, we found that ascr#18 perception via roots or leaves increases resistance in tomato, potato, and barley to foliar bacterial, oomycete, or fungal pathogens. Our results indicate that monocots and dicots recognize ascarosides as a conserved molecular signature of nematodes that triggers conserved plant defense signaling pathways, similar to perception of MAMPs (Manosalva et al., 2015). Currently we are attempting to identify the plant receptor for ascr#18, uncover the mechanism of ascr#18 priming of plant defenses, and with a large group of collaborators, assess ascr#18’s ability to enhance resistance to a broad spectrum of pathogens in all the major crop species, including corn, rice, soybean, and wheat.

Intern Projects
Over the past decade we have hosted 10 undergraduate research interns. All have worked closely with senior postdoctoral fellows or research associates, with most of them studying various aspects of SA-mediated defense signaling in plants. In addition, two helped characterize CRT1/MORC1.

Internship Program | Projects & FacultyApply for an Internship
How does the multifaceted plant hormone salicyle acid come disease in plants and are similar mechanisms utilized in humans?
2017
Author(s):Dempsey, D. A. and Klessig, D.F.
BioMed Central Biology
15,
23
View
DAMPs, MAMPs, and NAMPs in plant innate immunity.
2016
Author(s):Choi, H.W. and Klessig, D.F.
BMC Plant Biol
16,
232
View
Multiple targets of salicylic acid and its derivatives in plants and animals
2016
Author(s):Klessig, D.F., Tian, M., and Choi H.W.
Front. Immunol.
7,
1-10
View
Activation of Plant Innate Immunity by Extracellular High Mobility Group Box 3 and Its Inhibition by Salicylic Acid
2016
Author(s):Choi, H.W., Manohar, M., Manosalva, P., Tian, M., Moreau, M., and Klessig, D.F.
PLOS Pathog.
12,
e1005518
View
Newly identified targets of Aspirin and its primary metabolite, salicylic acid
2016
Author(s):Klessig, D.F.
DNA Cell Biol.
35,
163-166
View
Aspirin‰€™s Active Metabolite Salicylic Acid Targets Human High Mobility Group Box 1 to Modulate Inflammatory Responses
2015
Author(s):Choi, H.W., Tian, M., Song, F., Venereau, E., Preti, A., Park, S.W., Hamilton, K., Swapna, G.V.T., Manohar, M., Moreau, M., Agresti, A., Gorzanelli, A., De Marchis, F., Wang, H., Antonyak, M., Micikas, R., Gentile, D.R., Cerione, R.A., Schroeder, F.C., Montelione, G.T., Bianchi, M.E., and Klessig, D.F.
Mol. Med.
21
526-535
View
Human GAPDH is a target of aspirin‰€™s primary metabolite salicylic acid and its derivatives
2015
Author(s):Choi, H.W., Tian, M., Manohar, M., Harraz, M.M., Park, S.-W., Schroeder, F.C., Snyder, S.H., and Klessig, D.F.
PLOS ONE
10
e0143447
View
Aspirin’s Active Metabolite Salicylic Acid Targets Human High Mobility Group Box 1 to Modulate Inflammatory Responses
2015
Author(s):Choi, H.W., Tian, M., Song, F., Venereau, E., Preti, A., Park, S.W., Hamilton, K., Swapna, G.V.T., Manohar, M., Moreau, M., Agresti, A., Gorzanelli, A., De Marchis, F., Wang, H., Antonyak, M., Micikas, R., Gentile, D.R., Cerione, R.A., Schroeder, F.C., Montelione, G.T., Bianchi, M.E., and Klessig, D.F.
Mol. Med.
21,
526-535
View
Human GAPDH is a target of aspirin’s primary metabolite salicylic acid and its derivatives
2015
Author(s):Choi, H.W., Tian, M., Manohar, M., Harraz, M.M., Park, S.-W., Schroeder, F.C., Snyder, S.H., and Klessig, D.F.
PLOS ONE
10,
e0143447
View
Identification of multiple salicylic acid-binding proteins using two high throughput screens. Front
2015
Author(s):Manohar, M., Tian, M., Moreau, M., Park, S-W., Choi, H.W., Fei, Z., Friso, G., Asif, M., Manosalva, P., von Dahl, C.C., Shi, K., Ma, S., Dinesh-Kumar, S.P., O'Doherty, I., Schroeder, F.C., van Wijk, K.J., and Klessig, D.F.
Plant Sci.
5,
777
View
Conserved nematode signaling molecules elicit plant defenses and pathogen resistance
2015
Author(s):Manosalva, P., Manohar, M., von Reuss, S.H., Chen, S., Micikas, R.J., Koch, A., Choe, A., Kaplan, F., Xiaohong Wang, X., Kogel, K-H., Sternberg, P.W., Williamson, V. M., Schroeder, F.C., and Klessig, D.F.
Nature Comm
6,
7795
View
The GHKL ATPase MORC1 modulates species-specific plant immunity in Solanaceae
2015
Author(s):Manosalva, P., Manohar, M., Kogel, K-H., Kang, H-G., and Klessig, D.F.
Molecular Plant-Microbe Interactions
28,
927-942
View
Identification of multiple salicylic acid-binding proteins using two high throughput screens
2015
Author(s):Manohar, M., Tian, M., Moreau, M., Park, S-W., Choi, H.W., Fei, Z., Friso, G., Asif, M., Manosalva, P., von Dahl, C.C., Shi, K., Ma, S., Dinesh-Kumar, S.P., O'Doherty, I., Schroeder, F.C., van Wijk, K.J., and Klessig, D.F.
Front. Plant Sci.
5,
777
View
The Compromised Recognition of Turnip Crinkle Virus1 Subfamily of Microrchidia ATPases Regulates Disease Resistance in Barley to Biotrophic and Necrotrophic Pathogens
2014
Author(s):Langen, G., von Einem, S., Koch, A.,Imani, J., Pai, S.B., Manohar, M., Ehlers, K., Choi, H.W., Claar, M., Schmidt, R., Mang, H-G., Bordiya, Y., Kang, H-G., Klessig, D.F., and Kogel, K-H.
Plant Physiology
164(2),
866-878.
View
Salicylic acid binding of mitochondrial alpha-ketoglutarate dehydrogenase E2, which interacts with the downstream mitochondrial electron transport chain, plays a crucial role in basal defense against TMV in tomato
2014
Author(s):Liao, Y., Tian, M., Zhang, H., Li, X., Xia, X., Zhou, J., Zhou, Y., Yul, J., Shi, K., and Klessig, D.F.
New Phytologist
doi: 10.1111,
nph13137
View
Crystal structure of the Arabidopsis thaliana TOP2 oligopeptidase. Acta. Crystallogr
2014
Author(s):Wang, R., Rajagopalan, K., Sadre-Bazzaz, K., Moreau, M., Klessig, D.F., and Tong, L.
F. Struct. Biol. Commun.
70,
555
View
Structure of the Arabidopsis thaliana TOP2 oligopeptidase
2014
Author(s):Wang, R., Rajagopalan, K., Sadre-Bazzaz, K., Moreau, M., Klessig, D.F., and Tong, L.
Acta Cryst.
F70,
555–559
View
Double-Stranded RNA-Binding Protein 4 Is Required for Resistance Signaling against Viral and Bacterial Pathogens
2013
Author(s):Zhu, S.F., Jeong, R.D., Lim, G.H., Yu, K.S., Wang, C.X., Chandra-Shekara, A.C., Navarre, D., Klessig, D.F., Kachroo, A., and Kachroo, P.
Cell Reports
4,
1168-1184
View
SOS ‰€“ too many signals for systemic acquired resistance?
2012
Author(s):Dempsey, D.A., and Klessig, D.F.
Trends Plant Sci.
17
538-545
View
SOS – too many signals for systemic acquired resistance?
2012
Author(s):Dempsey, D.A., and Klessig, D.F.
Trends Plant Sci.
17,
538-545
View
CRT1 is a nuclear-translocated MORC endonuclease that participates in multiple levels of plant immunity
2012
Author(s):Kang, H.G., Hyong, W.C., von Einem, S., Manosalva, P., Ehlers, K., Liu, P.P., Buxa, S.V., Moreau, M., Mang, H.G., Kachroo, P., Kogel, K.H., and Klessig, D.F.
Nature Communications
3,
1297
View
Abscisic acid deficiency antagonizes high-temperature inhibition of disease resistance through enhancing nuclear accumulation of resistance proteins SNC1 and RPS4 in Arabidopsis
2012
Author(s):Mang, H.G., Qian, W.Q., Zhu, Y., Qian, J., Kang, H.G., Klessig, D.F., and Hua, J.
Plant Cell
24,
1271-1284
View
Salicylic acid binds NPR3 and NPR4 to regulate NPR1-dependent defense responses
2012
Author(s):Moreau, M., Tian, M., and Klessig, D.F.
Cell Res.
22,
1631-1633
View
The combined use of photoaffinity labeling and surface plasmon resonance-based technology identifies multiple salicylic acid-binding proteins
2012
Author(s):Tian, M., von Dahl, C.C., Liu, P.P., Friso, G., van Wijk, K.J., and Klessig, D.F.
Plant J.
72,
1027-1038
View
Coronatine promotes Pseudomonas syringae virulence in plants by activating a signaling cascade that inhibits salicylic acid accumulation
2012
Author(s):Zheng, X.Y., Spivey, N.W., Zeng, W.Q., Liu, P.P., Fu, Z.Q., Klessig, D.F., He, S.Y., and Dong, X.N.
Cell Host Microbe
11,
587-596
View
The extent to which methyl salicylate is required for signaling systemic acquired resistance is dependent on exposure to light after infection.
2011
Author(s):Liu, P.P., von Dahl, C.C., and Klessig, D.F.
Plant Physiology
157,
2216-2226
View
Interconnection between methyl salicylate and lipid-based long-distance signaling during the development of systemic acquired resistance in Arabidopsis and tobacco
2011
Author(s):Liu, P.P., von Dahl, C.C., Park, S.W., and Klessig, D.F.
Plant Physiology
155,
1762-1768
View
Salicylic acid biosynthesis and metabolism
2011
Author(s):Dempsey, D.A., Vlot, A.C., Wildermuth, M.C., and Klessig, D.F.
In The Arabidopsis Book American Society of Plant Biologists
e0156
View
NO synthesis and signaling in plants‰€“where do we stand?
2010
Author(s):Moreau, M., Lindermayr, C., Durner, J., and Klessig, D.F.
Physiol. Plant
138
372-383
View
NO synthesis and signaling in plants–where do we stand?
2010
Author(s):Moreau, M., Lindermayr, C., Durner, J., and Klessig, D.F.
Physiol. Plant
138,
372-383
View
The lesion-mimic mutant cpr22 shows alterations in abscisic acid signaling and abscisic acid insensitivity in a salicylic acid-dependent manner
2010
Author(s):Mosher, S., Moeder, W., Nishimura, N., Jikumaru, Y., Joo, S.H., Urquhart, W., Klessig, D.F., Kim, S.K., Nambara, E., and Yoshioka, K.
Plant Physiology
152,
1901-1913
View
Methyl esterase 1 (StMES1) is required for systemic acquired resistance in potato
2010
Author(s):Manosalva, P.M., Park, S.W., Forouhar, F., Tong, L., Fry , W.E., and Klessig, D.F.
Mol. Plant Microbe Interact.
, 1151-1163.,
1151-1163.
View
Endosome-associated CRT1 functions early in resistance gene-mediated defense signaling in Arabidopsis and tobacco
2010
Author(s):Kang, H.G., Oh, C.S., Sato, M., Katagiri, F., Glazebrook, J., Takahashi, H., Kachroo, P., Martin, G.B., and Klessig, D.F.
Plant Cell
22,
918-936
View
Altering expression of benzoic acid/salicylic acid carboxyl methyltransferase 1 compromises systemic acquired resistance and PAMP-triggered immunity in arabidopsis
2010
Author(s):Liu, P.P., Yang, Y., Pichersky, E., and Klessig, D.F.
Mol. Plant Microbe Interact.
23,
82-90
View
Systemic acquired resistance is induced by R gene-mediated responses independent of cell death.
2010
Author(s):Liu, P.P., Bhattacharjee, S., Klessig, D.F., and Moffett, P.
Mol. Plant Pathol.
11,
155-160
View
Cryptochrome 2 and phototropin 2 regulate resistance protein-mediated viral defense by negatively regulating an E3 ubiquitin ligase
2010
Author(s):Jeong, R.D., Chandra-Shekara, A.C., Barman, S.R., Navarre, D., Klessig, D.F., Kachroo, A., and Kachroo, P.
P. Natl. Acad. Sci. U S A
107,
13538-13543
View
Endosome-associated CRT1 functions early in resistance gene-mediated defense signaling in Arabidopsis and tobacco.
2010
Author(s):Kang, H.G., Oh, C.S., Sato, M., Katagiri, F., Glazebrook, J., Takahashi, H., Kachroo, P., Martin, G.B., and Klessig, D.F.
Plant Cell
22,
918-936
View
Salicylic acid, a multifaceted hormone to combat disease
2009
Author(s):Vlot, A.C., Dempsey, D.A., and Klessig, D.F.
Annu. Rev. Phytopathol.
47,
177-206
View
Use of a synthetic salicylic acid analog to investigate the roles of methyl salicylate and its esterases in plant disease resistance
2009
Author(s):Park, S.W., Liu, P.P., Forouhar, F., Vlot, A.C., Tong, L., Tietjen, K., and Klessig, D.F.
Journal of Biological Chemistry
284,
7307-7317
View
Enhanced defense responses in Arabidopsis induced by the cell wall protein fractions from Pythium oligandrum require SGT1, RAR1, NPR1 and JAR1
2009
Author(s):Kawamura, Y., Takenaka, S., Hase, S., Kubota, M., Ichinose, Y., Kanayama, Y., Nakaho, K., Klessig, D.F., and Takahashi, H.
Plant Cell Physiol.
50,
924-934
View
Identification of likely orthologs of tobacco salicylic acid-binding protein 2 and their role in systemic acquired resistance in Arabidopsis thaliana.
2008
Author(s):Vlot, A.C., Liu, P.P., Cameron, R.K., Park, S.W., Yang, Y., Kumar, D., Zhou, F.S., Padukkavidana, T., Gustafsson, C., Pichersky, E., and Klessig, D.F.
Plant J.
56,
445-456
View
Systemic acquired resistance: the elusive signal(s)
2008
Author(s):Vlot, A.C., Klessig, D.F., and Park, S.W.
Curr. Opin. Plant Biol.
11,
436-442
View
The Structure of YqeH: An AtNOS1/AtNOA1 ortholog that couples GTP hydrolysis to molecular recognition
2008
Author(s):Sudhamsu, J., Lee, G.I., Klessig, D.F., and Crane, B.R.
Journal of Biological Chemistry,
283,
32968-32976
View
High level expression of a virus resistance gene, RCY1, confers extreme resistance to Cucumber mosaic virus in Arabidopsis thaliana
2008
Author(s):Sekine, K.T., Kawakami, S., Hase, S., Kubota, M., Ichinose, Y., Shah, J., Kang, H.G., Klessig, D.F., and Takahashi, H.
Mol. Plant Microbe Interact.
21,
1398-1407
View
AtNOS/AtNOA1 Is a Functional Arabidopsis thaliana cGTPase and Not a Nitric-oxide Synthase
2008
Author(s):Moreau, M., Lee, G.I., Wang, Y., Crane, B.R., and Klessig, D.F.
Journal of Biological Chemistry
283,
32957-32967
View
Plant resistance to viruses: Natural resistance associated with dominant genes
2008
Author(s):Moffett, P., and Klessig, D.F.
In Encyclopedia of Virology (Mahy, B.W.J. and van Regenmortel, M. eds)
Oxford 0: Elsevier
The search for the salicylic acid receptor led to discovery of the SAR signal receptor.
2008
Author(s):Kumar, D., and Klessig, D.F.
Plant Signal Behav.
3,
691-692
View
CRT1, an Arabidopsis ATPase that interacts with diverse resistance proteins and modulates disease resistance to turnip crinkle virus
2008
Author(s):Kang, H.G., Kuhl, J.C., Kachroo, P., and Klessig, D.F.
Cell Host & Microbe
3,
48-57
View
HRT-mediated hypersensitive response and resistance to Turnip crinkle virus in Arabidopsis does not require the function of TIP, the presumed guardee protein
2008
Author(s):Jeong, R.D., Chandra-Shekara, A.C., Kachroo, A., Klessig, D.F., and Kachroo, P.
Mol. Plant Microbe Interact.
21,
1316-1324
View
The involvement of the Arabidopsis CRT1 ATPase family in disease resistance protein-mediated signaling
2008
Author(s):Kang, H.G., and Klessig, D.F.
Plant Signal Behav.
3,
689-690
View
Inactive methyl indole-3-acetic acid ester can be hydrolyzed and activated by several esterases belonging to the AtMES esterase family of Arabidopsis
2008
Author(s):Yang, Y., Xu, R., Ma, C.J., Vlot, A.C., Klessig, D.F., and Pichersky, E.
Plant Physiology
147,
1034-1045
View
The Arabidopsis gain-of-function mutant ssi4 requires RAR1 and SGT1b differentially for defense activation and morphological alterations.
2008
Author(s):Zhou, F.S., Mosher, S., Tian, M.Y., Sassi, G., Parker, J., and Klessig, D.F.
Mol. Plant Microbe Interact.
21,
40-49
View
Methyl salicylate is a critical mobile signal for plant systemic acquired resistance
2007
Author(s):Park, S.-W., Kaiyomo, E., Kumar, D., Mosher, S.L., and Klessig, D.F.
Science
318,
113-116
View
Validation of RNAi Silencing Specificity Using Synthetic Genes: Salicylic Acid-binding Protein 2 is Required for Innate Immunity in Plants
2006
Author(s):Kumar, D., Gustafsson, C., and Klessig, D.F.
Plant J.
45,
863-868
View
The Chimeric Arabidopsis CYCLIC NUCLEOTIDE-GATED ION CHANNEL11/12 Activates Multiple Pathogen Resistance Responses
2006
Author(s):Yoshioka, K., Moeder, W., Kang, H.-G., Kachroo, P., Masmoudi, K., Berkowitz, G., and Klessig, D.F.
Plant Cell
18,
747-763.
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Crystal structure and biochemical studies identify tobacco SABP2 as a methylsalicylate esterase and further implicate it in plant innate immunity
2005
Author(s):Forouhar, F., Yang, Y., Kumar, D., Chen, Y., Fridman, E., Park, S.W., Chiang, Y., Acton, T.B., Montelione, G.T., Pichersky, E., Klessig, D.F., and Tong, L.
P. Natl. Acad. Sci. U S A
102,
1773-1778
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Silencing of the Mitogen-activated Protein Kinase MPK6 Compromises Disease Resistance in Arabidopsis
2004
Author(s):Menke, F.L.H., van Pelt, J.A., Pieterse, C.M.J., and Klessig, D.F.
Plant Cell
16,
897-907
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Salicylic Acid Binding Protein (SABP2)
Dan Klessig
Technology Area:Biotic Stress - Disease
US Patent/Application(s): 7,169,966
Publication: PNAS 2003
Salicylic acid induced map kinase and its use for enhanced disease resistance in plants
Dan Klessig
Technology Area:Biotic Stress - Disease
US Patent/Application(s): 5,977,442
Method of using a pathogen-activatable map kinase to enhance disease resistance in plants
Dan Klessig
Technology Area:Biotic Stress - Disease
US Patent/Application(s): 6,765,128
Publication: PNAS 1998
Methods and compositions for improving salicylic acid-independent systemic acquired disease resistance in plants
Dan Klessig
Technology Area:Biotic Stress - Disease
US Patent/Application(s): 6,495,737
Publication: Plant J 1998
Methods for determining specificity of RNA silencing and for genetic analysis of the silenced gene or protein
Dan Klessig
Technology Area:Enabling Technology
US Patent/Application(s): 7,592,504
Publication: Plant J 2006
Compositions and methods for the generation of disease-resistant crops
Dan Klessig
Technology Area:Biotic Stress - Disease
US Patent/Application(s): PCT/US2012/043976
Genes Associated with enhanced disease resistance in plants
Dan Klessig
Technology Area:Biotic Stress - Disease
US Patent/Application(s): 5,939,601
Publication: PNAS 1996
High-affinity salicylic acid-binding protein and methods of use
Dan Klessig
Technology Area:Biotic Stress - Disease
US Patent/Application(s): 6,136,552
Assays to identify inducers of plant defense resistance
Dan Klessig
Technology Area:Biotic Stress - Disease
US Patent/Application(s): 5,989,846
Publication: Science 1993
Compositions and method for modulating immunity in plants
Dan Klessig
Technology Area:Biotic Stress - Disease
US Patent/Application(s): Provisional