Insect midgut and insecticidal proteins / edited by Tarlochan S. Dhadialla, Sarjeet S. Gill.

Format:

Book

Contributor:

Dhadialla, Tarlochan S., editor.

Gill, Sarjeet S., editor.

Series:

Advances in insect physiology ; Volume 47.

Advances in Insect Physiology, 0065-2806 ; Volume 47

Language:

English

Subjects (All):

Insect biochemistry--Periodicals.

Insect biochemistry.

Insects--Physiology.

Insects.

Insects--Molecular aspects.

Physical Description:

1 online resource (465 pages, 28 unnumbered pages of plates) : color illustrations.

Edition:

First edition.

Place of Publication:

London, England ; Oxford, England : Elsevier : AP, 2014.

Language Note:

English

Summary:

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 neurobiologists, entomologists, zoologists, and insect biochemists First published in 1963, this serial is ranked second in the highly competitive ISI category of Entomology.

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

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

Chapter Three: Lysinibacillus sphaericus: Toxins and Mode of Action, Applications for Mosquito Control and Resistance Man...

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.

3.1. Binding of the binary toxin to larvae midgut

3.2. Receptors

3.3. Comparative analysis of the Cqm1 and Aam1 α-glucosidases

4. Applications for Mosquito Control

4.1. Field trials

4.2. Factors affecting field performance

4.3. Trials against the vectors of lymphatic filariasis

4.4. Recent large-scale trials

4.5. Operational use in mosquito-control programmes

5. Resistance

5.1. Factors involved in the selection of resistance

5.2. Laboratory and field reports

5.3. Mechanisms and inheritance of resistance

5.4. Resistance alleles of the cpm1/cqm1 gene

5.5. Diagnosis and field survey of resistance

5.6. Biological cost of resistance

6. Management of Resistance

6.1. Integrated mosquito-control programmes

6.2. Factors involved in the prevention of resistance

6.3. Candidates for managing Bin-toxin resistance

6.3.1. Bacillus thuringiensis mosquitocidal toxins

6.3.2. Other L. sphaericus mosquitocidal toxins

6.3.3. Other control agents

Chapter Four: Discovery and Development of Insect-Resistant Crops Using Genes from Bacillus thuringiensis

2. Bt-Based Biopesticides

2.1. History of use of Bt for insect control

2.2. Biopesticides based on Bt

2.3. Molecular era-First cloned Bt insecticidal protein genes

2.4. Transconjugation, recombinant strains and alternative delivery systems for Bt-based biopesticides

3. Discovery, Characterization and Development of Insecticidal Protein Genes as Crop Traits

3.1. Diversity of Bt insecticidal proteins

3.2. Biological activity of Bt insecticidal proteins

3.3. Bt insecticidal protein structure and function: Cry proteins

3.4. Cry protein mechanism of action

3.5. Bt insecticidal protein structure and function: Cyt proteins

3.6. Bt insecticidal protein receptors.

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

Chapter Five: Progress Towards RNAi-Mediated Insect Pest Management

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

References.

Chapter Six: Detection and Mechanisms of Resistance Evolved in Insects to Cry Toxins from Bacillus thuringiensis

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

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

Chapter Eight: Methods for Deployment of Spider Venom Peptides as Bioinsecticides

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.

6.1. Synthetic mimics of venom peptides.

Notes:

Bibliographic Level Mode of Issuance: Monograph

Includes bibliographical references and index.

Description based on online resource; title from PDF title page (ebrary, viewed September 5, 2014).

ISBN:

0-12-800330-8