Handbook of venoms and toxins of reptiles / edited by Stephen P. Mackessy.

Format:

Book

Contributor:

Mackessy, Stephen P., editor.

Language:

English

Subjects (All):

Poisonous snakes--Venom.

Poisonous snakes.

Physical Description:

1 online resource (681 pages)

Edition:

Second edition.

Place of Publication:

Boca Raton, Florida ; London ; New York : CRC Press, [2021]

Summary:

The most comprehensive review of reptile venoms on the market, this completely updated and greatly expanded handbook offers a "one-stop shop" to all those interested in the biology of venomous reptiles, the biochemistry and molecular biology of venoms, and the effects and treatment of human envenomation.

Contents:

Cover

Half Title

Title Page

Copyright Page

Table of Contents

Preface

About the Editor

Contributors

Section I Introduction and Technologies Used in Toxinology

Chapter 1 Reptile Venoms and Toxins: Unlimited Opportunities for Basic and Applied Research

1.1 Introduction

1.2 Venom - Definition, Composition and Variation

1.2.1 What Is a Venom?

1.2.2 Venom Composition - General Trends

1.2.2.1 Proteins and Peptides

1.2.2.2 Metal Ions

1.2.3 Variation - Levels and Sources

1.2.3.1 Viperid Venom Composition

1.2.3.2 Elapid Venom Composition

1.2.3.3 Venoms from Rear-fanged Snakes ("Colubridae")

1.2.3.4 Helodermatid Venom Composition

1.2.4 Unusual Aspects of Venoms

1.3 Conservation of Venomous Reptiles

1.3.1 Habitat Modification and Effects on Reptile Populations

1.4 Conclusions

References

Chapter 2 Present and Future of Snake Venom Proteomics Profiling

2.1 Introduction: The Mutually Enlightening Relationship between Ecological and Translational Venomics

2.2 Bottom-Up Snake Venomics: Concepts and Workflow

2.3 Top-Down Proteomics: Towards Proteoform-Resolved Venom Proteomes

2.4 The Evils of Quantification: Towards Absolute Quantification of Venom Proteomes

2.5 Concluding Remarks and a Look Into the Future

2.6 Acknowledgments

Chapter 3 Applications of Genomics and Related Technologies for Studying Reptile Venoms

3.1 Introduction

3.2 The Genomic Context for Reptile Venoms

3.2.1 What a "Complete Genome" Is, and Why They Are Not Created Equal

3.2.2 The Structural and Evolutionary Context for Venom in Squamate Reptile Genomes

3.2.3 Venom Gene Cluster Structure, and Why Venom Genes Are Difficult to Assemble and Identify Accurately

3.2.4 Where Are Venom Genes Located in the Genome?.

3.3 Regulation of Venom Genes - The Black Box Linking the Genome With Venom

3.3.1 Towards an Understanding of Venom Regulation

3.3.2 Genomes Add Value to Transcriptomic and Proteomic Data

3.3.3 Understanding the Factors that Direct the Regulation of Venom Production

3.4 Population-Level Studies of Venom Variation and Evolution

3.4.1 Population-Level Sampling of Venomous Reptile Genomes

3.4.2 The Relevance of Hybrid Zones for Studying Venom

3.5 Conclusions

Chapter 4 Snake Venom Gland Transcriptomics

4.1 Introduction

4.2 Venom Gland Transcriptome Assembly

4.2.1 Assembly Programs

4.2.2 Evaluation of Assembly Quality

4.3 Toxin Annotation

4.3.1 Known Toxins

4.3.2 Uncharacterized Toxins

4.4 Quantifying Toxin Gene Expression

4.5 Regulation of Toxin Gene Expression

4.5.1 Toxin Transcripts

4.5.2 MicroRNAs

4.6 RNA-Seq Evolutionary Insights

4.6.1 Venom Evolution

4.6.2 Natural History of Venomous Organisms

4.7 Conclusions

Chapter 5 X-ray Crystallography and Structural Studies of Toxins

5.1 Introduction

5.2 A Brief History: Milestones

5.3 Outline of the Steps to Crystallize Proteins

5.3.1 The Magic of Crystallization

5.3.2 The X-ray Diffraction Experiment

5.3.3 Solving the Structure: the Phase Problem

5.4 Resolution and What It Means

5.5 Snake Venom Toxin Structural Timeline

5.5.1 Crystallization of Snake Venom Proteins

5.5.2 Catalytic Mechanisms

5.5.3 Multimeric Forms

5.5.4 Nuclear Magnetic Resonance in the Study of Macromolecular Toxins

5.6 Future Prospects

5.7 Acknowledgments

Chapter 6 Envenomations and Treatment: Translating between the Bench and the Bedside

6.1 Origin of Antivenom Development

6.2 Translational Research

6.3 Phases of Translation

6.3.1 The Bench.

6.3.2 Phases of Drug Development

6.4 Barriers to Progression During Each Phase

6.4.1 Translational Challenges at the Preclinical Development Phase

6.4.2 Common Problems Experienced During Clinical Trials

6.5 Medications from Venom

6.6 Antivenoms and Novel Technologies

6.7 Conclusions

Chapter 7 Current Assessment of the State of Snake Venom Toxinological Research with a View to the Future

7.1 Introduction

7.2 Snake Antivenom Research

7.2.1 Validation of Antivenoms

7.2.2 Novel Approaches to Antivenom Production

7.2.3 Non-Antibody-Based Approaches to Neutralize Venoms for Therapeutic Applications

7.2.4 Summary

7.3 Snake Toxin Isolation and Characterization

7.3.1 Characterization of Venom Toxins Belonging to Known Structural and Functional Classes

7.3.2 Characterization of the Molecular and Structural Elements of Toxins That Define Toxin Activity

7.3.3 Characterization of Venom Toxins with Undescribed Biological Activities

7.3.4 Summary

7.4 Snake Venomics

7.4.1 Transcriptomics and Proteomics

7.4.2 Genomics and Metabolomics

7.4.3 Summary

7.5 Snake Venom and Drug Discovery

7.5.1 Discovering a New Drug from Snake Venoms

7.5.2 Anti-Hypertension Drug Discovery

7.5.3 Pro- and Anticoagulant Drug Design

7.5.4 Antimicrobial and Antitumor Drug Design

7.5.5 Ion Channel Blockers and Analgesics

7.5.6 Summary

7.6 Snake Venom and Evolution

7.6.1 Snake Biology and Evolution

7.6.2 Snake Venom Evolution

7.6.3 Summary

7.7 Snake Venom Pathophysiology

7.7.1 Clinical Characterization and Descriptions of Envenoming

7.7.2 Pharmacokinetics and Pharmacodynamics of Envenomation and Antivenom Administration

7.8 Non-Antibody-Based Antivenom Agents

7.8.1 Traditional Medicine Applied to Toxinology

7.8.2 Natural and Synthetic Inhibitors Applied as Antivenom.

7.8.3 Aptamers Applied to Snakebite Diagnosis and Treatment

7.8.4 Biosynthetic Oligoclonal Antivenom (BOA) Associated with Small Molecule Enzyme Inhibitors Approach

7.8.5 Summary

Section II Venom Gland Structure, Systematics and Ecology

Chapter 8 Reptile Venom Glands: Form, Function, Future, Concepts and Controversies

8.1 Introduction

8.2 Gland Structure

8.2.1 Phylogeny

8.2.2 Anatomy of Reptilian Oral Glands

8.2.2.1 Lizards

8.2.2.2 Front-Fanged Venomous Snakes

8.2.2.3 Non-Front-Fanged Snakes and Technicalities of Terminology

8.3 Functions of the Venom Apparatus

8.3.1 Delivery of Oral Secretions

8.3.2 Biological Roles of NFFC Venom

8.3.3 Multi-Functionality of Venoms

8.3.3.1 Locomotor Inhibition

8.3.3.2 Precipitous Hypotension and Prey Subjugation

8.3.3.3 Other "Means to an End": Unique Snake Venom Toxins and Prey Subjugation

8.3.4 Clinical Implications of NFFC Venoms: Comparable to Elapids, Atractaspis spp. and Viperids?

8.4 Discussion and Conclusions

8.4.1 Multiple Functions and Biological Role(s) in the Wild

8.4.2 "Protovenoms": Exapted for Later Roles

8.5 Dedication

8.6 Acknowledgments

Chapter 9 Advances in Venomous Snake Systematics, 2009-2019

9.1 Introduction

9.2 Taxonomic Changes to Venomous Reptiles

9.2.1 Old World Elapid Snakes - Subfamily Elapinae

9.2.1.1 Bungarus - Kraits

9.2.1.2 Calliophis - Asian Coralsnakes

9.2.1.3 Hemibungarus - Philippine False Coralsnakes

9.2.1.4 Micrurus - New World Coralsnakes

9.2.1.5 Naja - Cobras

9.2.1.6 Sinomicrurus - Asian Coralsnakes

9.2.2 Australasian and Marine Elapid Snakes - Subfamily Hydrophiinae

9.2.2.1 Acanthophis - Death Adders

9.2.2.2 Aipysurus - Seasnakes

9.2.2.3 Antaioserpens - Burrowing Snakes

9.2.2.4 Emydocephalus - Turtle-Headed Seasnakes.

9.2.2.5 Hydrophis - Seasnakes

9.2.2.6 Pseudechis - Australian Blacksnakes

9.2.2.7 Pseudonaja - Australian Brownsnakes

9.2.2.8 Toxicocalamus - Forest Snakes

9.2.2.9 Vermicella - Bandy-Bandys

9.2.3 Fea's Vipers - Subfamily Azemiopinae

9.2.4 Pitvipers - Subfamily Crotalinae

9.2.4.1 Agkistrodon - Moccasins

9.2.4.2 Atropoides / Metlapilcoatlus - Jumping Vipers

9.2.4.3 Bothriechis - Palm Pitvipers

9.2.4.4 Lance-Headed Pitvipers (Bothrops and Relatives) - Genus-Level Classification

9.2.4.5 Bothrops - Lanceheads

9.2.4.6 Cerrophidion - Montane Pitvipers

9.2.4.7 Crotalus - Rattlesnakes

9.2.4.8 Sistrurus - Pigmy Rattlesnakes

9.2.4.9 Gloydius - Asian Moccasins

9.2.4.10 Ophryacus - Mexican Horned Pitvipers

9.2.4.11 Asiatic Pitvipers (Trimeresurus and Relatives) - Genus-Level Classification

9.2.4.12 Subgenus Trimeresurus

9.2.4.13 Subgenus Parias

9.2.4.14 Subgenus Himalayophis

9.2.4.15 Subgenus Popeia

9.2.4.16 Subgenus Sinovipera

9.2.4.17 Hypnale - Hump-Nosed Pitvipers

9.2.4.18 Ovophis - Mountain Pitvipers

9.2.4.19 Protobothrops - Asian Lanceheads or Habus

9.2.5 Old World Vipers - Subfamily Viperinae

9.2.5.1 Atheris - Bush Vipers

9.2.5.2 Bitis harenna - Bale Mountains Adder

9.2.5.3 Causus rasmusseni - Rasmussen's Night Adder

9.2.5.4 Cerastes boehmei

9.2.5.5 African Daboia - Moorish Vipers

9.2.5.6 Echis - Saw-Scaled Vipers

9.2.5.7 Macrovipera - Blunt-Nosed or Levantine Vipers

9.2.5.8 Montivipera - Mountain Vipers

9.2.5.9 Vipera - Eurasian Vipers

9.2.6 Stiletto Snakes - Family Lamprophiidae, Subfamily Atractaspidinae

9.2.7 Sand Snakes - Family Lamprophiidae, Subfamily Psammophiinae

9.2.8 Colubrid Snakes - Colubridae

9.2.8.1 Subfamily Colubrinae

9.2.8.2 Subfamily Natricinae

9.2.8.3 Subfamily Dipsadinae

9.2.8.4 Boiga (Cat Snakes).

9.2.9 Mud Snakes - Family Homalopsidae.

Notes:

Description based on print version record.

ISBN:

0-429-62345-3

OCLC:

1247673175