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El. knyga: Fungal Pathogenesis in Plants and Crops: Molecular Biology and Host Defense Mechanisms, Second Edition 2nd edition [Taylor & Francis e-book]

(Tamil Nadu Agricultural University, Coimbatore, India)
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Dramatic progress in molecular biology and genetic engineering has recently produced an unparalleled wealth of information on the mechanisms of plant and pathogen interactions at the cellular and molecular levels. Completely revised and expanded, Fungal Pathogenesis in Plants and Crops: Molecular Biology and Host Defense Mechanisms, Second Edition offers fresh insight into the interplay of signaling systems in plant and pathogen interactions. The book delineates the battle between plant and fungal pathogen and the complex signaling systems involved.

See what's new in the Second Edition:

Chapter on the role of disease resistance genes in signal perception and emission

Chapter on cell death signaling in disease susceptibility and resistance

Revised material on phytoalexins, toxins, and signal perception and transduction in fungal pathogenesis

17 additional families of pathogenesis-related proteins and antifungal proteins

The book describes the weapons used by fungal pathogens to evade or suppress the host defense mechanisms. It covers each fungal infection process from initial contact and penetration to the subsequent invasion and symptom development. The author explains complex signaling systems in the plant-pathogen interface with flow charts and provides drawings elucidating the biosynthetic pathway of secondary metabolites. He includes figures that highlight cutting-edge breakthroughs in molecular science and tables documenting important findings in the field of molecular plant pathology. These features and more make this book not only the most up to date resource in the field, but also the most important.
Preface xxi
Author xxiii
Perception and Transduction of Plant Signals in Pathogens
1(54)
Introduction
1(1)
Signaling and Transduction Systems in ``First Touch'' and Adhesion of Fungal Spores
1(5)
First Touch or Initial Contact Triggers the Infection Process
1(2)
Adhesion or Close Contact Triggers Fungal Infection Process
3(1)
Adhesion of Spores due to Hydrophobic Interaction
3(1)
Adhesion of Spores Is Accompanied by Release of Extracellular Material
4(1)
Involvement of Cutinases in Spore Adhesion
5(1)
Some Plant Signals May Be Needed for Adhesion of Spores
5(1)
Signaling in Fungal Spore Germination
6(2)
Plant Signals Trigger Structural Changes in Spores before Germination
6(1)
Plant-Surface Signals Trigger Spore Germination
7(1)
Flavonoids Signaling Spore Germination
8(1)
Signaling in Differentiation of Germ Tubes into Infection Structures
8(8)
Adhesion of Germlings and Infection Structures
8(1)
Extracellular Matrix in Germling Adhesion
9(2)
Extracellular Matrix in Appressorial Adhesion
11(1)
Topographic Signals in Appressorium Formation
11(2)
Plant-Surface Wax Signals Appressorium Formation
13(1)
Cutin Monomers as Signal Molecules
14(1)
Ethylene Signals Appressorium Formation
14(1)
Fungal Signals in Induction of Appressorium Formation
15(1)
Signal Transduction in Fungal Pathogenesis
16(14)
Transmembrane Receptor for Extracellular Signals
16(1)
G-Proteins
17(3)
Calcium/Calmodulin-Dependent Signaling
20(1)
cAMP/Protein Kinase Signaling Pathway
21(3)
Mitogen-Activated Protein Kinase Signaling Cascades
24(4)
Lipid-Induced Protein Kinase Signaling
28(1)
PAK Signaling
28(1)
Phosphorylation and Dephosphorylation Cascades
29(1)
P-Type Adenosine Triphosphatase Signaling
29(1)
Genes Involved in Formation of Infection Structures
30(2)
Signals in Fungal Infection Process
32(5)
Magnaporthe grisea
32(2)
Blumeria graminis
34(1)
Colletotrichum gloeosporioides
35(1)
Ustilago maydis
36(1)
Fusarium oxysporum
37(1)
Conclusion
37(18)
References
38(17)
Perception and Transduction of Pathogen Signals in Plants
55(138)
Introduction
55(1)
What Are Elicitors?
56(1)
Oligosaccharide Elicitors
57(3)
Chitooligosaccharide Elicitors
57(1)
Chitosan Elicitors
58(1)
Oligoglucan Elicitors
58(2)
Other Carbohydrate Elicitors
60(1)
Protein/Peptide Elicitors
60(5)
Elicitins
60(4)
Xylanase Elicitor
64(1)
PaNie213 Elicitor
64(1)
Nep1 Elicitor
64(1)
NIP1 Elicitor
64(1)
PB90 Elicitor
65(1)
Glycoprotein Elicitors
65(2)
Carbohydrate Moiety in the Glycoprotein Elicitor May Confer Elicitor Activity
65(1)
Protein Moiety in Glycoprotein Elicitors May Confer Elicitor Activity
66(1)
Functions of Glycoprotein Elicitors
67(1)
Lipid Elicitors
67(2)
Sphingolipids
67(1)
Arachidonic and Eicosapentaenoic Acids
68(1)
Ergosterols
68(1)
Toxins as Elicitor Molecules
69(1)
Plant Cell Wall--Degrading Enzymes as Elicitors
69(1)
Race-Specific and Cultivar-Specific Elicitors
70(2)
Specificity of General Elicitors
72(1)
Endogenous Oligogalacturonide Elicitors
73(1)
Multiple Elicitors May Be Needed to Activate Defense Responses
74(1)
Elicitor Complex
74(1)
Network of Elicitor Molecules
74(1)
Availability of Fungal Elicitors at the Site of Fungal Invasion in Plants
75(1)
Receptors for Elicitor Signals in Plant Cell Membrane
76(3)
Receptor Sites for Binding Oligosaccharide Elicitors
76(1)
Receptor Sites for Binding Proteinaceous Elicitors
77(1)
Protein Kinases as Receptor Sites
78(1)
LRR-Type Receptors
78(1)
Lectins as Receptors
79(1)
Resistance Gene Products as Receptors
79(1)
Calcium Ion May Act as Second Messenger
79(4)
Function of Calcium Ion as Second Messenger
79(2)
Upstream Events of Ca2+ Signaling
81(1)
Downstream Events of Ca2+ Signaling
82(1)
Phosphorylation of Proteins as a Component in Signal Transduction System
83(1)
Phosphorylation/Dephosphorylation Events
83(1)
Calcium Ion in Phosphorylation
83(1)
Mitogen-Activated Protein Kinase Cascades in Signal Transduction
84(1)
Phospholipid-Signaling System
85(5)
Plant Cell Membrane Phospholipids as Signal Molecules
85(1)
Role of Phospholipase A in Phospholipid-Signaling System
86(1)
Phospholipase C in Phospholipid-Signaling System
87(2)
Phospholipase D in Phospholipid-Signaling System
89(1)
Anion Channels in Signal Transduction
90(1)
Anion Channels in the Signaling System
90(1)
Upstream Events of Anion Channel-Signaling System
91(1)
Downstream of Anion Channel-Signaling System
91(1)
Extracellular Alkalinization and Cytoplasmic Acidification in Signaling System
91(1)
Reactive Oxygen Species in Signal Transduction
92(5)
Oxidative Burst
92(1)
Mechanisms of Production of Reactive Oxygen Species
93(1)
Production of O-2
93(1)
Production of H2O2
94(1)
Production of •OH Radical
95(1)
Production of Singlet Oxygen (1O2)
95(1)
Upstream of ROS Signaling
96(1)
Downstream of ROS Signaling
96(1)
Nitric Oxide in Signal Transduction
97(3)
Increases in Nitric Oxide
97(1)
Biosynthesis of Nitric Oxide
97(1)
Upstream Events of Nitric Oxide Signaling
98(1)
Downstream Events of Nitric Oxide Signaling
99(1)
Salicylic Acid-Signaling System
100(5)
Salicylic Acid in Signaling Defense Response in Plants
100(1)
Biosynthesis of Salicylic Acid
101(1)
Signal Perception
102(1)
Upstream Signals for Induction of Synthesis of Salicylic Acid
102(1)
Downstream of Salicylic Acid Signaling
103(1)
Methyl Salicylate
104(1)
Salicylate-Independent Signaling Systems
105(1)
Jasmonate-Signaling Pathway
105(6)
Jasmonate Signaling in Induction of Defense Responses
105(1)
Biosynthesis of Jasmonates
106(2)
Perception of Jasmonate Signals
108(1)
Jasmonate-Signaling System May Behave Differently in Protecting Plants against Various Pathogens
108(1)
Induction of Intercellular and Interplant Systemic Transduction of Jasmonate Signals
109(1)
Upstream of Jasmonate Signaling
109(1)
Downstream of Jasmonate Signaling
109(1)
Transcriptional Regulation of JA-Responsive Genes
109(1)
Jasmonic Acid, Methyl Jasmonate, and Cyclic Precursors and Derivatives of Jasmonic Acid as Signal Molecules
110(1)
Role of Systemin in Signal Transduction System
111(1)
Ethylene-Dependent Signaling Pathway
112(3)
Ethylene-Signaling System Inducing Disease Resistance or Susceptibility
112(1)
Biosynthesis of Ethylene
112(1)
Upstream Signals in Induction of Synthesis of Ethylene
113(1)
Ethylene Signal Perception
114(1)
Downstream Events in Ethylene Signaling
114(1)
Abscisic Acid Signaling
115(1)
Fatty Acids as Systemic Signal Molecules
116(1)
Other Signaling Systems
116(1)
Network and Interplay of Signaling Pathways
116(5)
Regulatory Interaction and Coordination among Salicylate-, Jasmonate-, and Ethylene-Signaling Pathways
116(1)
Coordinated Regulation of Ethylene- and Jasmonate-Signaling Pathways
117(1)
Interplay between Salicylate- and Jasmonate-Signaling Pathways
118(1)
Interplay between Salicylate and Ethylene Pathways
118(1)
Cross Talk between Salicylate and Jasmonate/Ethylene Pathways
119(1)
Cross Talk between Abscisic Acid-, Jasmonate-, and Ethylene-Dependent Signaling Pathways
120(1)
Regulatory Switches to Fine-Tune Signaling Pathways
121(1)
Induction of Defense Genes May Require Different Signal Transduction Systems
121(2)
Perception and Transduction of Pathogen Signals in Plants Leading to Susceptibility
123(20)
Differential Expression of Signaling System Leading to Susceptibility or Resistance
123(1)
Slower Accumulation of Elicitor-Releasing Enzymes in Susceptible Interactions
124(1)
Susceptible Varieties May Release Less Amount of Elicitors from Fungal Pathogen Cell Walls
124(3)
Delayed Release of Elicitors in Susceptible Interactions
127(1)
Elicitor of Compatible Pathogens Induces Less Defense-Related Actions than That of Incompatible Pathogens
127(1)
Degradation of Fungal Elicitors by Plant Enzymes in Plant Tissues May Lead to Susceptibility
128(1)
Fungal Pathogens May Degrade Host Elicitors during Susceptible Interactions
129(1)
Elicitors May Be Released during Pathogenesis but May Not Be Active or Less Active in Susceptible Plants
130(2)
Some Elicitors Do Not Act or Show Little Activity on Susceptible Cultivars
132(2)
Speed of Expression of Signal Transduction System May Determine Susceptibility or Resistance
134(1)
Reduced Accumulation of Signals May Lead to Susceptibility
134(1)
Elicitors May Induce Genes Involved in Suppression of Defense-Related Genes in Susceptible Interactions
135(2)
Suppressors Negating Elicitor-Induced Defense Responses in Susceptible Interactions
137(3)
Susceptible Plants May Have Suppressors to Suppress Action of Fungal Elicitors
140(1)
Downregulation of Functions of Elicitors in Susceptible Interactions
140(1)
Activation of an Unsuitable Signaling System for Induction of Defense Responses May Lead to Susceptibility
141(2)
Signaling Systems in Susceptible Interactions
143(1)
Abscisic Acid-Signaling System
143(1)
Ethylene-Signaling System
144(1)
Signal Transduction Systems May Induce Susceptibility-Related Responses
144(1)
Conclusion
144(49)
References
147(46)
Disease Resistance and Susceptibility Genes in Signal Perception and Emission
193(50)
Introduction
193(2)
Molecular Structure of Resistance Genes
195(1)
LRR Domains
195(1)
NBS Domains
195(1)
Classification of Resistance Genes Based on Molecular Structure of R Gene-Encoded Proteins
196(6)
Resistance Genes Encoding TIR--NBS--LRR Proteins
196(1)
Resistance Genes Encoding Non-TIR--NBS--LRR Proteins
197(2)
Resistance Genes Encoding LRR Proteins Lacking NBS Domain
199(1)
Resistance Genes Encoding Proteins Lacking LRR Domain
200(1)
LRD Proteins
200(1)
Intracellular Protein Kinases
200(1)
Transmembrane Proteins
201(1)
Lectin-Type Proteins
202(1)
Heat Shock Protein-Like Proteins
202(1)
NADPH-Dependent Reductase-Type Protein
202(1)
Plant eR Genes Encoding Photorespiratory Peroxisomal Enzyme Proteins
202(1)
Molecular Structure of Recessive Genes
202(2)
Barley mlo Gene
202(1)
Arabidopsis PMR6 Gene
203(1)
Arabidopsis RRS1-R Gene
203(1)
Arabidopsis ssi4 Gene
203(1)
Perception of Pathogen Signals by Resistance Genes
204(5)
Functions of Different Domains of R Proteins in Pathogen Recognition
204(1)
LRR Domain
204(1)
NBS Domain
204(1)
TIR Domain
205(1)
CC Domain
205(1)
C-Terminal Non-LRR Region
206(1)
C-Terminus Transcriptional Activation Domain
206(1)
Protein Kinase Domain
206(1)
Transmembrane Domain
206(1)
Calmodulin-Binding Protein
207(1)
Lectin-Type Protein
207(1)
Heat Shock Protein (HSP)-Like Protein
207(1)
R Gene Product May Act as a Receptor That Recognizes an AVR Gene Product
207(1)
R Protein May Detect Binding of an AVR Protein to a Different Protein in the Plant
208(1)
Activation of R Protein and Emission of Signals to Other Components in the Cell
209(2)
Downstream Components of R Gene-Signaling Systems
211(10)
Regulatory Genes (or Complementary Genes or R Gene-Signaling Components)
211(1)
EDS1--PAD4 Proteins
212(1)
NDR1 Proteins
213(1)
RAR1--SGT1--HSP90 Proteins
214(1)
RAR1
214(1)
SGT1
215(2)
RAR1/SGT1 Complex
217(1)
Interaction of RAR1/SGT1 with HSP90
217(1)
NPR1
218(1)
Prf--Pto--Pti Signaling System
219(1)
Other Regulatory Genes
219(2)
Downstream Signaling Events in R Gene-Mediated Resistance
221(1)
Susceptibility Genes in Signal Transduction
222(3)
Susceptibility Alleles of Resistance Genes
222(1)
Susceptibility Genes
222(1)
Resistance Gene May Act as Susceptibility Gene against Some Pathogens
223(1)
Low Expression of Resistance Genes May Lead to Susceptibility
224(1)
Susceptibility Alleles of Resistance Genes May Negate the Function of Resistance Genes
224(1)
Suppressor Genes
225(1)
Conclusion
225(18)
References
227(16)
Cell Death Programs during Fungal Pathogenesis
243(32)
Introduction
243(1)
Cell Death in Resistant Interactions
243(2)
Programmed Cell Death
243(1)
Hypersensitive Cell Death
244(1)
Spontaneous Cell Death
244(1)
Runaway Cell Death
245(1)
Cell Death-Inducing Systemic Acquired Resistance
245(1)
Molecular Mechanism of Induction of Hypersensitive Cell Death
245(8)
Mediators, Regulators, and Executioners of Cell Death
245(1)
R Gene Signals Involved in Triggering Cell Death
246(1)
Reactive Oxygen Species in Cell Death
246(3)
Nitric Oxide in Cell Death
249(1)
Bax Family of Proteins
250(1)
Ion-Conducting Channels
251(1)
Function of Mitochondrion in Induction of Cell Death
251(1)
Proteolytic Enzymes
251(1)
Plant Caspases
251(1)
Vacuolar Processing Enzymes (VPEs)
252(1)
Metacaspases
252(1)
Other Types of Proteolytic Enzymes
253(1)
Probable Sequence in Induction of Hypersensitive Cell Death
253(1)
Molecular Mechanism of Induction of Spontaneous Cell Death
253(3)
Spontaneous Cell Death-Regulating Genes
253(2)
Salicylic Acid
255(1)
Ethylene
255(1)
Phosphatidic Acid
255(1)
Molecular Mechanism of Induction of Runaway Cell Death
256(1)
Role of Cell Death in Induction of Systemic Acquired Resistance
257(1)
Susceptibility-Related Cell Death
258(1)
Molecular Mechanisms in Induction of Cell Death in Susceptible Interactions
258(4)
Mediators, Regulators, and Executioners of Susceptibility-Related Plant Cell Death
258(1)
Reactive Oxygen Species
259(1)
Proteolytic Enzymes
259(1)
Calcium Ion
260(1)
Salicylate, Ethylene, and Jasmonate
260(2)
Sphingolipid Metabolism
262(1)
Extracellular ATP Levels
262(1)
What Is the Function of Cell Death in Fungal Pathogenesis?
262(2)
Conclusion
264(11)
References
264(11)
Cell Wall Degradation and Fortification
275(70)
Introduction
275(1)
Structure of Cuticle
275(1)
Penetration of Epicuticular Waxy Layer by Pathogens
276(1)
Production of Cutinases to Breach Cuticle Barrier
276(1)
Genes Encoding Cutinases
277(1)
Plant Signals Triggering Fungal Cutinases
278(1)
Importance of Cutinases in Penetration of Cuticle
279(1)
Cutinases as Virulence/Pathogenicity Factors
280(1)
Melanins in Fungal Penetration of Cuticle Barrier
281(4)
Biosynthesis of Melanins
281(2)
Melanins Aid in Penetration of Cuticle Barrier by Fungal Pathogens
283(2)
Degradation of Pectic Polysaccharides
285(9)
Types of Pectic Polysaccharides
285(1)
Types of Pectic Enzymes
285(1)
Fungal Pathogens Produce Multiple Pectic Enzymes
286(1)
Genes Encoding Pectic Enzymes
287(1)
Evidences to Show That Pectic Enzymes Aid Pathogens to Penetrate Cell Wall
288(1)
Immunocytochemical Evidences
288(1)
Evidences by Showing Protection of the Host by Inhibition of Pectic Enzymes with Specific Antibodies
289(1)
Evidences Showing Protection of Host Plants by Inhibition of Pectic Enzymes with Selective Inhibitors
290(1)
Evidences Using Pectic Enzyme-Deficient Fungal Isolates
290(1)
Evidences Showing Correlation between the Level of Pectic Enzymes and Virulence
291(1)
Evidences Showing Enhancement of Virulence by Gene Transfer
291(1)
Evidences Showing Decrease in Virulence by Gene Disruption
291(1)
Plant Signals to Induce Pectic Enzymes
291(1)
Host Cell Wall Differs in Its Susceptibility to Pectic Enzymes
292(1)
Cell Wall Proteins Modulate Pectic Enzyme Activity
292(2)
Pathogens Produce Cellulolytic Enzymes to Breach Cell Wall Barrier
294(1)
Fungal Hemicellulases in Plant Cell Wall Degradation
295(1)
Degradation of Cell Wall Structural Proteins
296(1)
Requirement of Several Cell Wall--Degrading Enzymes to Degrade the Complex-Natured Cell Wall
297(1)
Production of Suitable Enzymes in Appropriate Sequence by Fungal Pathogens
297(1)
Reinforcement of Host Cell Wall during Fungal Invasion
298(1)
Papillae Suppress Fungal Penetration
298(2)
Callose Deposition in Cell Wall
300(1)
How Do Pathogens Overcome the Papillae and Callose Barriers?
301(3)
Pathogen Delays Papillae Formation
301(1)
Pathogens May Suppress Callose Synthesis in Susceptible Interactions
302(1)
Pathogens May Be Able to Penetrate the Papillae Barrier
303(1)
Pathogens May Degrade Callose by Producing β-1,3-Glucanase
303(1)
Accumulation of Hydroxyproline-Rich Glycoproteins in Plant Cell Walls
304(3)
Host Cell Wall Responds to Fungal Invasion by Accumulating HRGP
304(1)
Signals Triggering Accumulation of HRGPs
304(1)
Host Cell Wall Responds to Fungal Invasion by Strengthening Its HRGPs by Glycosylation
305(1)
Insolubilization of HRGPs in Host Cell Wall
305(1)
Enrichment of HRGPs by Lignin Deposition
305(1)
Some HRGPs May Immobilize Plant Pathogens
306(1)
How Does Pathogen Overcome HRGP Barrier?
306(1)
Less Accumulation of HRGPs in Compatible Interactions
306(1)
Pathogen Overcomes HRGP Barrier by Delaying Accumulation of HRGPs in Host Cell Wall
306(1)
Cell Wall--Bound Phenolics and Lignins
307(9)
Fortification of Plant Cell Wall by Phenolics and Lignin
307(1)
Biosynthesis of Phenolics and Lignins
308(1)
Phenolic Deposition in Host Cell Wall in Response to Fungal Invasion
308(2)
Host Cell Wall Responds to Fungal Invasion by Activating Enzymes Involved in Synthesis of Wall-Bound Phenolics
310(1)
How Does the Pathogen Overcome the Cell Wall--Bound Phenolics to Cause Disease?
311(1)
Pathogen Suppresses Accumulation of Phenolics in Host Cell Wall
311(1)
Pathogen Delays Synthesis of Cell Wall--Bound Phenolics
312(1)
Lignification during Fungal Pathogenesis
312(1)
Host Cell Wall Responds to Fungal Invasion by Increasing Lignification Process
312(1)
Pathogen Suppresses Lignin Deposition
313(1)
Pathogen Suppresses Enzymes Involved in Lignin Biosynthesis
314(1)
How Does Pathogen Suppress Lignification in Host Cell Wall?
315(1)
Suberization during Fungal Pathogenesis
316(2)
Host Cell Wall Responds to Fungal Invasion by Suberization
316(1)
Biosynthesis of Suberin in Pathogen-Inoculated Host Cell Wall
316(1)
Pathogen Delays Suberin Accumulation
317(1)
Pathogen May Suppress Suberin-Synthesizing Enzymes
317(1)
Pathogens May Penetrate the Suberized Walls of Host Cells
318(1)
Deposition of Mineral Elements in Host Cell Wall in Response to Fungal Invasion
318(1)
Silicon Deposition
318(1)
Calcium Deposition in Papillae
318(1)
Manganese Accumulation in Papillae
319(1)
Conclusion
319(26)
References
320(25)
Induction and Evasion of Pathogenesis-Related Proteins
345(66)
Introduction
345(1)
Multiplicity of PR Proteins
346(1)
Classification of PR Proteins
347(8)
PR-1 Proteins
347(1)
PR-2 Proteins
348(1)
PR-3 Proteins
349(1)
PR-4 Proteins
350(1)
PR-5 Proteins
351(1)
PR-6 Proteins
351(1)
PR-7 Proteins
352(1)
PR-8 Proteins
352(1)
PR-9 Proteins
352(1)
PR-10 Proteins
353(1)
PR-11 Proteins
353(1)
PR-12 Proteins
353(1)
PR-13 Proteins
354(1)
PR-14 Proteins
354(1)
PR-15 Proteins
354(1)
PR-16 Proteins
355(1)
PR-17 Proteins
355(1)
Chitosanases
355(1)
Induction of PR Proteins during Fungal Pathogenesis
355(1)
Genes Encoding PR Proteins
356(1)
Transcription of PR Genes
357(1)
Signals Involved in Transcriptional Induction of PR Genes
358(6)
Induction of PR Genes by Elicitors
358(1)
Induction of PR Genes by Salicylic Acid
359(1)
Induction of PR Genes by Ethylene
360(2)
Induction of PR Genes by Jasmonic Acid/Jasmonate
362(1)
Induction of PR Proteins May Require Different Signal Transduction Systems
363(1)
Synergistic Effect of Different Signals
364(1)
Antagonistic Effect of Different Signals
364(1)
PR Proteins Are Synthesized as Larger Precursors
364(1)
Secretion of PR Proteins
365(2)
Secretory Pathways
365(1)
Site of Accumulation of PR Proteins
366(1)
PR Proteins May Be Involved in Inhibition of Pathogen Development
367(3)
Inhibition of Fungal Growth by PR Proteins In Vitro
367(2)
Inhibition of Fungal Growth by PR Proteins In Vivo
369(1)
Some PR Proteins May Be Involved in Release of Elicitor Molecules in Planta
370(1)
Some PR Proteins May Be Involved in Reinforcement of Cell Wall Structures
370(1)
PR Proteins May Be Involved in Triggering Disease Resistance
370(3)
Demonstration of the Role of PR Proteins in Disease Resistance Using Chemical or Biological Elicitors
370(1)
Demonstration of Role of PR Proteins in Disease Resistance by Inducing Mutation
371(1)
Demonstration of Role of PR Proteins in Disease Resistance by Developing Transgenic Plants
371(2)
Demonstration of the Role of PR Proteins by Developing Transgenic Plants with Antisense Suppression of PR Genes
373(1)
How Do Pathogens Overcome Fungitoxic PR Proteins of the Host?
373(12)
Slower Accumulation of PR Proteins May Enable Pathogens to Escape the Antifungal Action of PR Proteins
373(6)
Pathogens May Shed Away from Their Cell Wall the Substrate for the PR Proteins of Enzymatic Nature and Avoid Their Lytic Enzyme Action
379(1)
Pathogens May Produce Enzymes That Protect Them from Fungitoxic Action of PR-3 Proteins
380(1)
Pathogens May Produce Enzymes to Inhibit Activity of Some PR Proteins
381(1)
Less Elicitor Is Released from Pathogen's Cell Wall to Activate Synthesis of PR Proteins
381(1)
PR Proteins Are Degraded Quickly in the Susceptible Host Tissues
382(1)
Site of Accumulation of Some PR Proteins May Determine Susceptibility or Resistance
382(2)
Adaptation of Pathogens to PR Proteins
384(1)
Some PR Proteins May Not Be Involved in Disease Resistance
385(1)
Conclusion
385(26)
References
386(25)
Evasion and Detoxification of Secondary Metabolites
411(58)
Introduction
411(1)
Chemical Structural Classes of Phytoalexins
412(2)
Biosynthesis of Isoflavonoid Phytoalexins
414(10)
Phaseollin and Related Compounds
414(4)
Glyceollins
418(2)
Medicarpin
420(3)
Pisatin
423(1)
Biosynthesis of Flavanone Phytoalexins
424(1)
Biosynthesis of Coumarin Phytoalexins
424(2)
Biosynthesis of Stilbene Phytoalexins
426(1)
Biosynthesis of Terpenoid Phytoalexins
426(4)
Biosynthesis of Indole-Based Sulfur-Containing Phytoalexins
430(1)
Biosynthesis of Alkaloid Phytoalexins
431(1)
Site of Synthesis of Phytoalexins
432(1)
Phytoalexins Are Fungitoxic
432(1)
How Do Pathogens Overcome the Antifungal Phytoalexins?
433(7)
Pathogens May Detoxify Phytoalexins
433(3)
Induction of Phytoalexins May Be Delayed in Susceptible Interactions
436(2)
Pathogen May Suppress Accumulation of Phytoalexins in Susceptible Hosts
438(1)
Amount of Accumulation of Phytoalexins May Be Less in Susceptible Interactions Compared with Resistant Interactions
439(1)
Highly Toxic Phytoalexins May Not Accumulate in Susceptible Interactions
439(1)
Some Phytoalexins May Not Be Produced in Susceptible Interactions
439(1)
Some Phytoalexins May Not Have Any Role in Defense Mechanisms of Plants
440(1)
Chemical Structural Classes of Phytoanticipins
440(1)
Phenolics as Phytoanticipins
440(1)
Toxicity of Phenolics to Pathogens
441(1)
How Does Pathogen Overcome the Antifungal Phenolics?
441(4)
Pathogen May Degrade Phenolics to Nontoxic Products
441(2)
Pathogen May Suppress Increased Synthesis of Phenolics in Plants
443(1)
Pathogen May Suppress Phenol Biosynthetic Enzymes
443(1)
Pathogen May Suppress Phenolic Metabolism by Its Suppressor Molecule
443(1)
Pathogen May Suppress Phenolic Metabolism by Producing Toxins
443(1)
Pathogen May Suppress Oxidation of Phenolics by Inhibiting Polyphenol Oxidase
444(1)
Phenolics Are Fungitoxic but They May Not Accumulate to Fungitoxic Level during Pathogenesis in Some Plant--Pathogen Interactions
444(1)
Saponins as Phytoanticipins
445(2)
Glucosinolates as Phytoanticipins
447(3)
Biosynthesis of Glucosinolates
447(1)
Toxicity of Glucosinolates to Fungal Pathogens
448(1)
How Does the Pathogen Overcome Toxicity of Glucosinolates?
448(1)
Concentration of Glucosinolates May Be Less in Susceptible Tissues
448(1)
Glucosinolates May Not Be Involved in Disease Resistance Unless the Tissue Is Damaged
448(2)
Cyanogenic Glucosides
450(1)
Dienes
450(1)
Conclusion
450(19)
References
451(18)
Toxins in Disease Symptom Development
469(30)
Introduction
469(2)
Importance of Toxins in Disease Development
471(1)
Toxins Suppress Host-Defense Mechanisms
472(1)
Toxins Cause Cell Membrane Dysfunction
473(10)
Permeability Changes
473(1)
Changes in Membrane-Bound ATPases
474(1)
H+-ATPase Is Stimulated
474(3)
H+-ATPase Is Inhibited
477(1)
Inhibition of Calmodulin Activity
477(1)
Alteration in Membrane Potential
477(2)
Toxins Form Ion Channels in Plant Cell Membranes
479(1)
Modification of Membrane Phospholipids
479(1)
Toxin-Induced Active Oxygen Species Induce Membrane Dysfunction
480(1)
Mitochondrial Membrane Dysfunction
481(2)
How Do Pathogens Induce Membrane Dysfunction Only in Susceptible Hosts?
483(5)
Detoxification of Phytotoxins, Which Occurs in Resistant Hosts, Does Not Occur in Susceptible Hosts
483(1)
Susceptible Tissues May Have Toxin Receptors Which May Be Absent in Resistant Tissues
484(2)
Susceptible Tissues May Be More Sensitive to Toxins
486(1)
Specific Protein Synthesized after Toxin Exposure May Confer Host Specificity
487(1)
Proteins of Susceptible Hosts May Enhance Potential of Pathogens to Produce Toxins
487(1)
Sucrose Influx May Have Correlation with Sensitivity to Toxin
487(1)
Transport of Toxin to Cytoplasm May Occur Only in Susceptible Interactions
488(1)
Conclusion
488(11)
References
489(10)
Index 499


Tamil Nadu Agric. University, Coimbatore, India