Insect Pharmacology

Name: Insect Pharmacology | Channels, Receptors, Toxins and Enzymes
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Channels, Receptors, Toxins and Enzymes

Lawrence I. Gilbert Sarjeet S. Gill(Editor)

Academic Press

Published on 14. May 2014

392 pages

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Front Cover
Insect Pharmacology
Copyright Page
Contents
Preface
Contributors
Chapter 1 Sodium Channels
1.1 Introduction
1.1.1 Function and Structure of Voltage-Sensitive Sodium Channels
1.1.2 Sodium Channels as Targets for Neurotoxicants
1.1.3 Progress in Insect Sodium Channel Research Since 1985
1.2 Sodium Channel Genes in Insects
1.2.1 Sodium Channel Genes in Drosophila melanogaster
1.2.1.1 dsc1
1.2.1.2 para
1.2.1.3 tipE
1.2.1.4 Genetic and functional characterization of D. melanogaster mutants
1.2.2 Sodium Channel Genes in Other Insect Species
1.2.2.1 Orthologs of para
1.2.2.2 Orthologs of dsc1
1.2.2.3 Orthologs of tipE
1.3 Functional Expression of Cloned Insect Sodium Channels
1.3.1 Expression of Functional Sodium Channels in Xenopus Oocytes
1.3.2 Pharmacological Properties of Expressed Insect Sodium Channels
1.3.3 Functional Characterization of Sodium Channel Splice Variants
1.4 Sodium Channels and Knockdown Resistance to Pyrethroids
1.4.1 Knockdown Resistance
1.4.2 Altered Sodium Channel Regulation as a Mechanism of Knockdown Resistance
1.4.3 Genetic Linkage between Knockdown Resistance and Sodium Channel Genes
1.4.4 Identification of Resistance-Associated Mutations
1.4.5 Functional Analysis of Resistance-Associated Mutations
1.4.5.1 Functional analysis of the kdr and super-kdr mutations
1.4.5.2 Functional analysis of other putative primary resistance mutations
1.4.5.3 Functional analysis of putative secondary mutations
1.5 Conclusions
1.5.1 Unique Features of Insect Sodium Channels
1.5.2 Sodium Channels and Pyrethroid Resistance
1.5.3 Future Exploitation of the Sodium Channel as an Insecticide Target
References
Chapter A1 Addendum: Recent Progress in Insect Sodium Channel Research
A1.1 How Many Sodium Channel Genes Are in a Given Insect Species?
A1.2 More Auxiliary Subunits of Insect Sodium Channels?
A1.3 Generation of Sodium Channel Diversity by Alternative Splicing and RNA Editing
A1.4 Sodium Channel Mutations and Pyrethroid Resistance in Insects
References
Chapter 2 GABA Receptors of Insects
2.1 Introduction
2.2 Ionotropic GABARs of Insects
2.2.1 Lessons from Vertebrate GABARs
2.2.2 Pharmacology of In Situ Insect GABARs
2.2.2.1 Agonist site
2.2.2.2 Competitive antagonists
2.2.2.3 Noncompetitive antagonists and convulsants
2.2.2.4 Allosteric modulators
2.2.2.4.1 Benzodiazepines
2.2.2.4.2 Barbiturates
2.2.2.4.3 Other allosteric modulators
2.2.3 Diversity: Existence of Subtypes
2.2.4 Molecular Biology
2.2.4.1 Cloned receptors
2.2.4.2 RDL: a model insect ionotropic GABAR
2.2.4.2.1 Comparison of RDL with in situ GABARs of insects
2.2.4.3 Pharmacology of heterologously expressed RDL
2.2.4.3.1 The agonist site
2.2.4.3.2 The convulsant antagonist site
2.2.4.3.3 Allosteric modulators
2.2.4.3.4 Other (RDL) ligands
2.2.4.4 Conclusions
2.2.4.5 Alternative splicing in GABA receptor subunits
2.2.4.6 Does RDL form a homomer in situ?
2.2.5 Intracellular Modulation of GABARs
2.2.6 GABARs as Targets for Insecticides
2.2.6.1 Picrotoxin
2.2.6.2 Polychlorocyclohexanes
2.2.6.3 Bicyclophosphorus esters and bicycloorthobenzoates
2.2.6.4 Phenylpyrazoles
2.2.6.5 Avermectins
2.2.7 Mechanisms of Insecticide Resistance
2.2.8 Molecular Basis of Selectivity of Insecticides for Insect GABARs
2.2.9 Single Channel Properties of Insect GABARs
2.2.10 Distribution
2.2.11 GABARs and Behavior
2.2.11.1 Insect learning
2.2.11.2 Stimulus encoding and tuning
2.2.11.2.1 Odor representation in the antennal lobes
2.2.11.2.2 Fine-tuning of odor representation
2.2.11.2.3 Involvement of GABA inputs in fine-tuning of sensory pathways may be a general phenomenon
2.2.11.3 Other behaviors involving GABARs
2.3 Metabotropic GABARs of Insects
2.3.1 A Cloned Insect Metabotropic (GABAB) Receptor
2.4 Conclusions
References
Chapter A2 Addendum: Recent Progress in Insect GABA Receptors
A2.1 GABAA Receptor Diversity by Alternative Splicing and RNA Editing
A2.2 GABAB Receptors
A2.3 GABAA Receptor Mutations and Resistance in Insects
A2.4 Role of GABAA Receptors in Behavior and Sleep
Chapter 3 The Insecticidal Macrocyclic Lactones
3.1 Discovery
3.2 Chemistry
3.2.1 Chemical Structure
3.2.2 Structure-Activity Relationships
3.3 Mode of Action
3.3.1 Biochemical and Molecular Action
3.3.2 Physiological Activity
3.3.2.1 Insects
3.3.2.2 Acarids and helminths
3.3.2.3 Vertebrates
3.3.3 Sublethal Toxicity
3.3.4 Metabolism
3.4 Biological Activity
3.4.1 Spectrum and Potency
3.4.1.1 Insects
3.4.1.2 Acarids, copepods, and helminths
3.4.2 Bioavailability
3.4.2.1 Crop protection uses
3.4.2.2 Animal health uses
3.4.3 Safety and Selectivity
3.4.3.1 Crop protection uses
3.4.3.2 Animal health uses
3.5 Uses
3.5.1 Crop Protection
3.5.2 Animal and Human Health
3.6 Resistance
3.6.1 Insects
3.6.2 Acarids
3.6.3 Helminths
3.Summary
References
Chapter A3 Addendum: The Insecticidal Macrocyclic Lactones
Chapter 4 Spider Toxins and their Potential for Insect Control
4.1 Introduction
4.2 Chemical Control of Insect Pests
4.3 Spiders and Their Venoms: A Brief Overview
4.4 Insecticidal Acylpolyamine Toxins from Spider Venom
4.5 Insecticidal Peptide Toxins from Spider Venom
4.5.1 Spider Venom Polypeptides: An Underexploited Pharmacological Reservoir
4.5.2 Expression and Evolution of Spider Venom Polypeptides: Rolling the Dice
4.5.3 Three-Dimensional Structure of Spider Venom Polypeptides: A Tale of Ropes and Knots
4.6 Toxin-Based Target Validation and Screening
4.7 Toxin-Based Bioinsecticides: A New Era of Biological Control
4.7.1 A Brief History of Conventional Biological Control Methods
4.7.2 Biological Control in the New Millennium
4.8 Spider Toxins as Templates for Mimetic Design
4.9 Future Directions
Acknowledgments
References
Chapter A4 Addendum: Spider Toxins and Their Potential for Insect Control
Acknowledgments
References
Chapter 5 Baculoviruses: Biology, Biochemistry, and Molecular Biology
5.1 Introduction
5.1.1 Taxonomy
5.1.2 Nomenclature
5.2 Structure
5.2.1 Nucleocapsids
5.2.2 Budded Virus
5.2.3 Occlusion-Derived Virus
5.2.4 Occlusion Bodies
5.3 Life Cycle
5.3.1 Infection
5.3.2 Dissemination within the Host
5.3.3 Dissemination from the Host
5.4 Virus Replication
5.4.1 Early Gene Expression
5.4.2 DNA Replication
5.4.3 Late and Very Late Gene Expression
5.5 Effects on the Host
5.5.1 Virulence
5.5.2 Host Range
5.5.2.1 Host range genes
5.5.2.2 Antiapoptotic genes
5.5.3 Survival Time and Yield
5.5.4 Sublethal Effects and Latent Infections
5.5.5 Resistance
5.6 Baculovirus Genomics
5.6.1 General Properties of Baculovirus Genomes
5.6.2 Baculovirus Evolution
5.6.3 Identification of Genes Involved in Virus-Insect Interactions
5.6.4 Identification of Genes that Have Undergone Adaptive Molecular Evolution
5.7 Conclusion
References
Chapter A5 Addendum: Baculoviruses: Biology, Biochemistry, and Molecular Biology
A5.1 Introduction
A5.1.1 Taxonomy
A5.2 Structure
A5.2.1 Nucleocapsids
A5.2.2 Budded Virus
A5.2.3 Occlusion-Derived Virus
A5.2.4 Occlusion Bodies
A5.3 Life Cycle
A5.3.1 Infection
A5.3.2 Dissemination Within the Host
A5.3.3 Dissemination from the Host
A5.4 Virus Replication
A5.4.1 Early Gene Expression
A5.4.2 DNA Replication
A5.4.3 Late and Very Late Gene Expression
A5.5 Effects on the Host
A5.5.1 Virulence
A5.5.2 Host Range
A5.5.2.1 Host Range Genes
A5.5.2.2 Antiapoptotic Genes
A5.5.3 Survival Time and Yield
A5.5.4 Sublethal Effects and Latent Infections
A5.5.5 Resistance
A5.6 Baculovirus Genomics
A5.6.1 General Properties of Baculovirus Genomes
A5.6.2 Baculovirus Evolution
References
Chapter 6 Amino Acid and Neurotransmitter Transporters
6.1 Introduction
6.1.1 Role of Amino Acid Transporters in Insects
6.1.2 Uniporters, Symporters, and Antiporters
6.1.3 Energization and Electrochemistry of Amino Acid Uptake
6.1.4 Structural Organization of Known Transporters
6.1.5 How Many Amino Acid Transporters Are Required?
6.1.6 Neurotransmitter Transporters and Nutrient Amino Acid Transporters
6.2 Physiology of Insect NTTs
6.2.1 Synaptic Neurotransmission
6.2.2 Role of Plasma Membrane NTTs in Synaptic Transmission
6.2.3 Study of Insect NTTs
6.2.4 Potential for Use of NTTs as Insecticide Targets
6.3 Molecular Biology of Insect NTTs
6.3.1 Classification of NTTs
6.3.2 Plasma Membrane Neurotransmitter Transporters
6.3.3 Excitatory Amino Acid Transporters (EAAT
SLC1)
6.3.3.1 Roles of glutamate and EAATs in insects
6.3.3.2 Insect EAATs
6.3.4 Na+/Cl---Driven Neurotransmitter Symporters (SNF
SLC6)
6.3.4.1 GABA transporters
6.3.4.2 Monoamine transporters
6.3.4.2.1 Serotonin transporter (SERT
5HTT)
6.3.4.2.2 Dopamine transporter (DAT)
6.3.4.2.3 Octopamine transporter (OAT)
6.3.4.3 Glycine and proline transporters
6.3.4.4 Orphan inebriated (ine) and bloated tubules (blot) transporters
6.3.5 Choline Transporters (CHTs)
6.3.6 Vesicular Membrane Transporters
6.3.6.1 Vesicular inhibitory amino acid transporters (vIAATs or vGATs)
6.3.6.2 Vesicular monoamine and acetylcholine transporters (vMATs and vAChTs)
6.3.6.3 Vesicular glutamate transporters (vGLUTs)
6.4 Nutrient Amino Acid Transport in Insects
6.4.1 Early Studies of Insect Amino Acid Uptake
6.4.2 Amino Acid Uptake by Brush Border Membrane Vesicles
6.5 Postgenomic Analysis of Insect AATs
6.6 AAT Cluster I (SLC1)
6.7 AAT Cluster II (SLC7)
6.7.1 Cationic Amino Acid Transporters (CATs).
6.7.2 Heterodimeric Amino Acid Transporters (HATs)
6.7.2.1 SLC7 related genes in dipteran models
6.7.2.2 SLC3-related genes in dipteran models
6.7.2.3 Cloned insect HATs from Ae. aegypti
(AeaLAT + AeaCD98hc)
6.8 AAT Cluster III (SLC6, SLC32, SLC36, SLC38)
6.8.1 SNATs and PATs (SLC38, SLC32, SLC36)..
6.8.2 Sodium Neutral Amino Acid Transporters, SNATs (SLC38)
6.8.3 Vesicular GABA Transporters, vGATs (SLC32)
6.8.4 Proton Amino Acid Transporters, PAT (SLC36)
6.8.5 Sodium Neurotransmitter Symporter Family (SNF
SLC6)
6.8.5.1 Neurotransmitter transporters, NTTs
6.8.5.2 Nutrient amino acid transporters (NATs)
6.8.5.3 Orphan transporters: transitions between SNF clusters
6.9 AAT Cluster IV (SLC15, SLC16, SLC17, SLC18)
6.9.1 Vesicular Monoamine and Acetylcholine Transporters, vMATs and vAChT (SLC18)
6.9.2 Monocarboxylate Transporters and T System Amino Acid Transporters, MCTs and TATs (SLC16)
6.9.3 Oligopeptide Transporters, OPTs (SLC15)
6.9.3.1 Drosophila oligopeptide transporters, OPTs
6.9.3.2 Phylogenetic characteristics of dipteran OPTs
6.9.4 Vesicular Glutamate and Phosphate Transporters, vGLUTs and PiTs (SLC17)
6.9.4.1 Inorganic phosphate transporter, type I PiTs (SLC17A1)
6.9.4.2 Sialin (SLC17A5)
6.9.4.3 vGlutT (SLC17A6, 7, 8)
6.9.4.4 Phylogenetic characteristics of SLC17 transporters
6.1Summary and Perspectives
Acknowledgments
References
Chapter A6 Addendum: Amino Acid and Neurotransmitter Transporters
References
Chapter 7 Biochemical Genetics and Genomics of Insect Esterases
7.1 Introduction
7.1.1 Historical Perspective
7.1.2 Functional Definitions and Classifications
7.2 Comparative Genomics of Insect Esterases
7.2.1 Overview
7.2.2 The Structural Context
7.3 Acetylcholinesterase and Noncatalytic Neurodevelopmental Clades
7.3.1 Acetylcholinesterase
7.3.1.1 General biochemistry and genetics
7.3.1.2 Target site insecticide resistance
7.3.2 Noncatalytic Clades
7.4 Secreted Catalytic Clades
7.4.1 Glutactin and Related Proteins
7.4.2 Juvenile Hormone Esterases
7.4.3 beta-Esterases
7.4.3.1 The Drosophila beta-esterase cluster
7.4.3.2 Amplified hemipteran beta-esterases
7.4.4 Semiochemical Esterases
7.5 Intracellular Catalytic Clades
7.5.1 Lower Dipteran Microsomal alpha-Esterases
7.5.2 Higher Dipteran Microsomal alpha-Esterases
7.5.3 Nonmicrosomal Esterases
7.6 Other Esterases Implicated in Insecticide Resistance
7.6.1 Resistance against Organophosphates and Carbamates
7.6.2 The Special Case of Malathion Carboxylesterase
7.6.3 Resistance against Synthetic Pyrethroids
7.7 Concluding Remarks
Acknowledgments
References
Chapter A7 Addendum: New Genomic Perspectives on Insect Esterases and Insecticide Resistance
References
Chapter 8 Glutathione Transferases
8.1 Introduction
8.2 Methods Used to Study Insect GSTs
8.2.1 Isolation of Insect GSTs
8.2.1.1 Biochemical purification
8.2.1.2 Cloning of insect GSTs
8.2.2 Characterization of Substrate Specificity
8.3 Classification and Nomenclature
8.3.1 Nomenclature Guidelines for Insect GSTs
8.3.2 Classes of Insect GSTs
8.3.2.1 Delta class
8.3.2.2 Epsilon class
8.3.2.3 Omega class
8.3.2.4 Sigma class
8.3.2.5 Theta class
8.3.2.6 Zeta class
8.3.2.7 Microsomal GSTs
8.4 Protein Structure
8.4.1 Cytosolic GSTs
8.4.2 Microsomal GSTs
8.5 GST Gene Organization
8.5.1 Clustering of Paralogous Genes
8.5.2 Intron Size and Position
8.5.3 Mechanisms for Generating Additional Heterogeneity
8.5.3.1 Alternative splicing of GSTs
8.5.3.2 GST fusion genes
8.5.3.3 Allelic variation
8.5.4 GST Pseudogenes
8.6 Functions of Insect GSTs
8.6.1 Endogenous Substrates
8.6.2 Protection against Oxidative Stress
8.6.3 Detoxification of Xenobiotics
8.6.3.1 Metabolism of insecticides
8.6.3.1.1 Organophosphates
8.6.3.1.2 Organochlorines
8.6.3.2 Pyrethroids
8.6.3.3 Plant chemicals
8.7 Regulation and Induction of GST Expression
8.7.1 Tissue and Life Stage Specificity of Expression
8.7.2 Induction of GSTs
8.7.3 Regulation of GST Expression
8.8 Evolution of GSTs
8.9 Conclusions
References
Chapter A8 Addendum: Glutathione Transferases
References
Chapter 9 Insect G Protein-Coupled Receptors: Recent Discoveries and Implications
9.1 Introduction
9.2 Structure-Function Relationships for GPCRs
9.3 Evolution of Insect GPCRs
9.4 Insect GPCRs
9.4.1 Classification of GPCRs
9.4.2 Family A: Biogenic Amine, Rhodopsin, and Neuropeptide Receptors
2.4.2.1 Biogenic amine receptors
9.4.2.2 Rhodopsin
9.4.2.3 Neuropeptide receptors in family A
9.4.3 Family B: Secretin-Like Receptors
9.4.4 Family C: Metabotropic Glutamate Receptor and GABAB Receptor
9.4.5 Other GPCRs: Odorant Receptor, Gustatory Receptor, Atypical 7TM Proteins
9.5 Intracellular Signaling Pathways Triggered by GPCRs
9.6 Assignment of GPCR Functions
9.6.1 Functional GPCR Assays: Coupling with Reporters
9.6.2 Expression of GPCRs in Xenopus Oocytes
9.6.3 Assay of GPCR Activation in Cell Lines
9.6.4 Other GPCR Reporter Assays
9.6.5 Identifying Biological Functions of GPCRs
9.7 Conclusions
References
Chapter A9 Addendum: Insect G Protein-Coupled Receptors
A9.1 GPCR Genes in Comprehensive Genome Surveys
A9.2 New Functions for GPCRs Revealed in Recent Studies
References
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Insect Pharmacology

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