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Insect midgut and insecticidal proteins /

This volume of Advances in Insect Physiology contains comprehensive interdisciplinary reviews on basic and practical aspects relevant to Insect Midgut and Insecticidal Proteins. Contains important, comprehensive and in-depth reviews An essential reference source for invertebrate physiologists and ne...

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Bibliographic Details
Corporate Author: ScienceDirect (Online service)
Other Authors: Dhadialla, Tarlochan S. (Editor), Gill, Sarjeet S. (Editor)
Format: eBook
Language:English
Language Notes:Text in English.
Published: London, England ; Oxford, England : Elsevier : AP, 2014.
Edition:First edition.
Series:Advances in insect physiology ; v. 47.
Subjects:
Insect biochemistry > Periodicals.
Insects > Physiology.
Insects > Molecular aspects.
Insectes > Physiologie.
Insectes > Aspect moléculaire.
Insectes > Biochimie > Périodiques.
Insect biochemistry
Insects > Molecular aspects
Insects > Physiology
Electronic books.
Periodical
periodicals.
Periodicals
Periodicals.
Périodiques.
Online Access:Connect to the full text of this electronic book
Table of Contents:
  • Front Cover
  • Insect Midgut and Insecticidal Proteins
  • Copyright
  • Contents
  • Contributors
  • Preface
  • Chapter One: Insect Gut Structure, Function, Development and Target of Biological Toxins
  • 1. Introduction
  • 2. Mosquito Larval Alimentary Canal
  • 3. Other Insects
  • 3.1. Lepidopteran larvae (caterpillars)
  • 3.2. Coleopterans (beetles and their larvae)
  • 3.3. Hemipterans (aphids)
  • 4. Conclusions and Comment
  • References
  • Chapter Two: Diversity of Bacillus thuringiensis Crystal Toxins and Mechanism of Action
  • 1. Introduction
  • 2. General Characteristics of B. thuringiensis Crystal Toxins
  • 2.1. Definition and classification of crystal toxins
  • 2.2. The diversity of Cry toxins
  • 2.3. The parasporin toxins
  • 2.4. The ricin domain
  • 2.5. Toxin discovery
  • 3. Cry Toxin Structure: Function
  • 3.1. Overview of Cry structure
  • 3.2. Cry domain I
  • 3.3. Cry domain II
  • 3.4. Cry domain III
  • 3.5. Cry intoxication process
  • 3.6. Cry toxin solubilization and proteolytic processing
  • 4. Midgut Cry-Binding Proteins and Receptor Function
  • 4.1. Aminopeptidase
  • 4.2. Cadherin
  • 4.3. Alkaline phosphatase
  • 4.4. ABC transporter
  • 4.5. Other Cry-binding (receptor) proteins and molecules
  • 5. Models of Cry Toxin Action
  • 6. Cytolytic Toxins
  • Acknowledgements
  • References
  • Chapter Three: Lysinibacillus sphaericus: Toxins and Mode of Action, Applications for Mosquito Control and Resistance Man...
  • 1. Introduction
  • 1.1. Background
  • 1.2. General features and strains
  • 1.3. The relevance of L. sphaericus as a mosquito-control agent
  • 2. Toxins and Mode of Action
  • 2.1. Spectrum of action
  • 2.2. Binary toxin
  • 2.3. Cry48/Cry49
  • 2.4. Mosquitocidal toxin 1
  • 2.5. Other Mtx toxins
  • 2.6. Sphaericolysin
  • 2.7. S-layer proteins
  • 2.8. Safety issues
  • 3. Receptors of the Binary Toxin.
  • 3.7. Mechanisms of resistance to Bt insecticidal proteins
  • 4. Discovery and Development of Bt Crops
  • 4.1. The discovery and development process
  • 4.2. Gene discovery
  • 4.3. First demonstrated success of Bt Cry GE plants
  • 4.4. Transformation technologies
  • 4.5. Introgression and testing
  • 5. Regulation
  • 5.1. Product identification and characterization
  • 5.2. Human health assessment
  • 5.3. Environmental effects
  • 5.4. Considerations for stacks
  • 5.5. Continued regulatory oversight of commercialized GE events
  • 6. Insect Resistance Management
  • 7. Bt Crops-A Snapshot of Today
  • 7.1. Commercialized Bt proteins
  • 7.1.1. Cry1Ab
  • 7.1.2. Cry1Ac
  • 7.1.3. Cry1Fa2
  • 7.1.4. Cry1A.105
  • 7.1.5. Cry2Ab
  • 7.1.6. Cry2Ae
  • 7.1.7. Vip3Aa
  • 7.1.8. mCry3Aa (modified Cry3Aa)
  • 7.1.9. eCry3.1Ab
  • 7.1.10. Cry3Bb1
  • 7.1.11. Cry34Ab1/Cry35Ab1
  • 7.2. Global adoption of Bt crops
  • 7.3. Commercialized products
  • 7.3.1. Bt corn
  • 7.3.2. Bt cotton
  • 7.3.3. Bt soybean
  • 7.3.4. Bt potato
  • 8. Bt Crops-Prospects for the Future
  • 8.1. Novel Bt proteins
  • 8.1.1. Protease activation
  • 8.1.2. Site directed mutagenesis
  • 8.1.3. Gene shuffling
  • 8.1.4. Domain 3 exchange
  • 9. Conclusions
  • Acknowledgements
  • References
  • Chapter Five: Progress Towards RNAi-Mediated Insect Pest Management
  • 1. Introduction
  • 2. Environmental RNAi
  • 3. Insect Sensitivity to Environmental RNAi
  • 3.1. Coleoptera
  • 3.2. Diptera
  • 3.3. Lepidoptera
  • 3.4. Hemiptera
  • 3.5. Other agricultural pests
  • 4. Barriers to Delivery and Efficacy in Recalcitrant Species
  • 5. Commercial Development of RNAi Actives
  • 5.1. Next-generation rootworm-resistant corn
  • 5.2. Topical application
  • 6. Safety Considerations
  • 7. Insect Resistance Management
  • 8. Concluding Remarks
  • Acknowledgements
  • References.
  • Chapter Six: Detection and Mechanisms of Resistance Evolved in Insects to Cry Toxins from Bacillus thuringiensis
  • 1. Introduction
  • 2. Detection Methods and Current Status of Insect Resistance to Bt Crops
  • 2.1. Definition of resistance
  • 2.2. Resistance detection methods
  • 2.2.1. Concentration-response and diagnostic concentration assays
  • 2.2.2. F1 screen
  • 2.2.3. F2 screen
  • 2.2.4. DNA screen
  • 2.3. Current status of field-evolved resistance to Bt crops
  • 3. Resistance Mechanisms
  • 3.1. Mode of action of Bt Cry toxins
  • 3.1.1. Structure of Bt Cry toxins
  • 3.1.2. Receptors for Bt Cry toxins
  • 3.1.3. Models for mode of action
  • 3.2. Alterations in proteolytic processing of Cry toxins in resistant insects
  • 3.3. Modifications of Cry toxin receptors in resistant insects
  • 3.3.1. Cadherin
  • 3.3.2. Aminopeptidase
  • 3.3.3. Alkaline phosphatase
  • 3.3.4. ABCC2
  • 4. Genetic Diversity of Resistance and Implications for Resistance Management
  • 4.1. Laboratory-selected and field-evolved resistance
  • 4.2. Resistance dominance and the refuge strategy
  • 4.3. Cross-resistance and the pyramid strategy
  • 5. Conclusions
  • Acknowledgements
  • References
  • Chapter Seven: Photorhabdus Toxins
  • 1. Photorhabdus Lifestyles, Relatives and Genomes
  • 1.1. The life cycle of Photorhabdus temperata and Photorhabdus luminescens
  • 1.2. The unusual life cycle of Photorhabdus asymbiotica
  • 1.3. Xenorhabdus and comparative genomics
  • 2. The Toxin Complexes
  • 2.1. Tc discovery, gene cloning and ABC nomenclature
  • 2.2. Diversity of tc-like genes from other bacteria
  • 2.3. Structure, function and biophysics of the Tc ABC complexes
  • 2.3.1. 'A' subunit assembly
  • 2.3.2. Low-resolution structure of the Tc ABC holotoxin
  • 2.3.3. Encapsulation and auto-proteolysis of the C subunit.
  • 2.3.4. Insights from the high-resolution structure of the ABC holotoxin
  • 2.3.5. Potential Tc chaperones, release factors and delivery co-factors
  • 2.4. The Tcs as 'polymorphic' toxins
  • 2.5. The role of the Tcs in the biology of infection
  • 2.6. The potential role of Tcs in crop protection
  • 3. Photorhabdus Virulence Cassettes
  • 3.1. Discovery and organization of PVCs
  • 3.2. The role of PVC-like structures in other bacteria
  • 3.3. Implications for PVC biology
  • 4. The Mcf Toxins
  • 4.1. Discovery and mode of action of Mcf1
  • 4.2. Diversity of Mcf-like toxins
  • 4.2.1. The Mcf toxin 2
  • 4.2.2. The Mcf-like `Fit toxin from Pseudomonas
  • 4.2.3. The MCF1-SHE domain as a novel serine peptidase
  • 4.3. Studying Mcf-like toxins in vivo
  • 4.3.1. The Drosophila embryo as a microcosm for toxin mode-of-action studies
  • 4.3.2. Regulation of Fit toxin expression in the insect host
  • 5. Patox and Photox
  • 5.1. PaTox structure and function
  • 5.2. Photox as a novel mART toxin
  • 6. Binary Toxins
  • 6.1. The PirAB binary toxins
  • 6.2. The XaxAB and YaxAB cytotoxins
  • 7. Classical Secretions Systems and Novel Screens
  • 7.1. Type III and other classical secretion systems
  • 7.2. RVA-like screens for novel effectors
  • 7.3. Clustering methods to look for novel effector phenotypes
  • 8. Perspectives for the Future of Photorhabdus Toxins
  • Acknowledgements
  • References
  • Chapter Eight: Methods for Deployment of Spider Venom Peptides as Bioinsecticides
  • 1. Introduction
  • 2. Spider Venom Peptides as Bioinsecticides
  • 3. Transcytosis of Spider Venom Peptides Across the Insect Gut Epithelium via Fusion to Molecular Transport Vehicles
  • 4. Use of Entomopathogens for ISVP Delivery
  • 4.1. Entomopathogens as bioinsecticides
  • 4.2. Entomopathogens as a delivery vehicle for ISVPs
  • 5. In Planta Expression of Spider Venom Peptides
  • 6. ISVP Mimetics.