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PARASITIC NEMATODES Molecular Biology, Biochemistry and Immunology PARASITIC NEMATODES Molecular Biology, Biochemistry and Immunology Parasitic Nematodes Molecular Biology, Biochemistry and Immunology Edited by M.W. Kennedy Division of Infection and Immunity Institute of Biomedical and Life Sciences University of Glasgow Glasgow UK and W. Harnett Department of Immunology University of Strathclyde Glasgow UK CABI Publishing CABI Publishing is a division of CAB International CABI Publishing CABI Publishing CAB International 10 E 40th Street Wallingford Suite 3203 Oxon OX10 8DE New York, NY 10016 UK USA Tel: +44 (0)1491 832111 Tel: +1 212 481 7018 Fax: +44 (0)1491 833508 Fax: +1 212 686 7993 Email: [email protected] Email: [email protected] Web site: http://www.cabi.org © CAB International 2001. All rights reserved. No part of this publication may be reproduced in any form or by any means, electronically, mechanically, by photocopying, recording or otherwise, without the prior permission of the copyright owners. A catalogue record for this book is available from the British Library, London, UK. A catalogue record for this book is available from the Library of Congress, Washington DC, UK. ISBN 0 85199 423 7 Typeset by AMA DataSet Ltd, UK. Printed and bound in the UK by Biddles Ltd, Guildford and King’s Lynn. Contents Contents Contributors xvii Preface xxi Access to Colour Illustrations xxiii Part I Genetics and Phylogeny 1 Molecular Analysis of Nematode Evolution 1 Mark L. Blaxter Introduction 1 The Molecular Revolution 2 Molecular Markers 3 The Structure of the Nematoda and the Origins of Parasitism 4 Strongylid Evolution Revealed by Three Different Genes 9 Resolution of Species Complexes by Molecular Phylogenetics 11 The Evolution of Parasitic Phenotypes 13 Concluding Remarks 18 References 18 2 The Wolbachia Endosymbionts of Filarial Nematodes 25 Claudio Bandi, Timothy J.C. Anderson, Claudio Genchi and Mark L. Blaxter v vi Contents Introduction 25 The Discovery and Rediscovery of Intracellular Symbiosis in Filarial Nematodes 25 Background Information on Bacterial Symbiosis in Invertebrates 26 Phylogenetic positionings of Wolbachia and other intracellular bacteria 26 Wolbachia, vertical transmission, mutualistic symbiosis and reproductive parasitism 27 Distribution of Wolbachia in arthropods 28 Distribution of Wolbachia in Filarial Worms 28 Phylogeny of Wolbachia in Filarial Worms 31 Interphylum transmission 32 Is Wolbachia monophyletic? 32 Horizontal transmission of Wolbachia between nematodes 32 Should Nematode Wolbachia Behave Differently from Arthropod Wolbachia?33 The Wolbachia–Filaria Relationship: an Obligate Mutualism? 33 The Wolbachia Catalase 35 Genomics and Proteomics 35 Implications for the Pathogenesis of Filarial Diseases 36 Implications for Treatment 37 Concluding Remarks 38 References 38 3 Forward Genetic Analysis of Plant-parasitic Nematode–Host Interactions 45 Charles H. Opperman Introduction 45 Soybean Cyst Nematode Biology 46 Genetic Analysis of Parasitism 47 Concluding Remarks 50 References 50 4 Identification of Parasitic Nematodes and Study of Genetic Variability Using PCR Approaches 53 Robin B. Gasser Introduction 53 Technical Aspects and Choice of the DNA Target for PCR 54 Template preparation 54 PCR: precautions, optimization and errors 55 Target region 56 Approaches to the Identification of Nematode Species and Strains 58 Amplification from specific DNA regions 58 Contents vii PCR-linked restriction fragment length polymorphism (PCR-RFLP) analysis 59 Arbitrarily primed PCR 60 Analysis of mini- and microsatellites, and other repetitive elements 61 DNA sequencing approaches 62 Analysis of Genetic Variability by PCR-coupled Mutation Detection Methods 63 Denaturing gradient gel electrophoresis (DGGE) 64 Single-strand conformation polymorphism (SSCP) analysis 65 SSCP protocol 67 Concluding Remarks 70 Acknowledgements 71 References 71 5 Diversity in Populations of Parasitic Nematodes and its Significance 83 Mark E. Viney Introduction 83 A Developmental Choice for Strongyloides ratti 83 Diversity in Developmental Route 85 Artificial Selection for Developmental Route 86 The Environment and Developmental Route 87 Phenotypic Plasticity in Response to Temperature 87 The Molecular Basis of Variation in Sensitivity 89 Developmental Route and Host Immunity 90 Interaction of Host Immunity and Temperature on Developmental Route 91 Phenotypic Diversity and Arrested Development 93 Phenotypic Diversity and Immunology 94 Summary So Far 96 Parasite Modulation of Host Immune Responses 97 Consequences of Laboratory Maintenance 98 Concluding Remarks 99 References 100 Part II Host Modulation and Manipulation – Making Themselves at Home 6 New Insights into the Intestinal Niche of Trichinella spiralis 103 Judith A. Appleton Introduction 103 Excretory/Secretory and Surface Glycoproteins of T. spiralis L1 Larvae 104 viii Contents Tyvelose and Trichinella Glycoprotein Function 104 Function of ES Products 105 Protective Activity of Anti-Tyvelose IgG 106 Mucus Trapping and Expulsion 107 Invasion of Epithelia in vitro 108 Tyvelose and Invasion 112 Cell Wounding and Pore Formation 113 Interference with the Epithelial Niche of T. spiralis by Anti-Tyv IgG in vitro 114 Concluding Remarks 116 Acknowledgements 116 References 116 7 Genetic Reprogramming of Mammalian Skeletal Muscle Cells by Trichinella spiralis 121 Douglas P. Jasmer Introduction 121 Genetic Reprogramming of the Host Muscle Cell 123 Repositioning of the Host Cell in the Cell Cycle 123 Repression of the Differentiated Skeletal Muscle Phenotype 125 Acquisition of the Infected Cell Phenotype 126 Parasite Regulation of the Infected Cell Phenotype 128 General Consideration of Parasite Products 129 Nuclear Antigens 130 Other Possible T. spiralis Regulators of Host Muscle Cells 131 Concluding Remarks 132 References 133 8 Plant-parasitic Nematodes 139 David McK. Bird and Alan F. Bird Introduction 139 Root-knot and Cyst Nematodes 140 The Impact of Plant-parasitic Nematodes 140 Nematode Adaptations for Plant Parasitism 142 Mouthparts 142 Pharynx and Pharyngeal Glands 143 Rectal Glands 145 Developmental Changes 145 Niches Occupied by Plant-parasitic Nematodes 147 An Aerial Plant Parasite 149 Root Parasites 149 Feeding Sites of Sedentary Endoparasites 150 Feeding Site Induction 151 Induction of Giant Cells 151 Contents ix Genes Expressed in Feeding Cells 153 Cell Cycle Regulation 154 Evolution of Parasitism: an Ancient Symbiosis? 155 Acquisition of Parasitism Genes by Horizontal Gene Transfer 156 Clade IV Nematode–Bacterial Associations 156 Concluding Remarks 159 References 159 Part III Specialist Products and Activities 9 The Nematode Cuticle: Synthesis, Modification and Mutants 167 Antony P. Page Nematode Cuticle: Structure 167 Moulting 168 Control of moulting 169 The Cuticle Collagens 170 Collagen Gene Expression 172 C. elegans Cuticle Collagen-related Mutants 173 Collagen Folding 174 Catalysts of Collagen Folding, Co- and Post-Translational Modification 175 Peptidyl-prolyl cis–trans isomerase (PPI, cyclophilins/FKBPs) (EC 5.3.4.1) 177 Prolyl 4-hydroxylase (PHY) (EC 1.14.11.2) 179 Protein disulphide isomerase (PDI) (EC 5.2.1.8) 181 Lysyl hydroxylase (LHY) (EC 1.14.11.4) 182 Non-collagenous Cuticle Structural Components: the Cuticulins 183 Cuticle Collagen/Cuticulin Cross-linking Enzymes 184 Tyrosinase (EC 1.14.18.1) and phenol oxidase (EC 1.10.3.1) 184 Transglutaminases (TGA) (EC 2.3.2.13) 184 Concluding Remarks 185 Acknowledgements 185 References 186 10 Chitinases of Filarial Nematodes 195 Ralf Adam, Birgit Drabner and Richard Lucius Introduction 195 The Role of Filarial Chitinases in Microfilariae 195 The Role of Chitinases in the Infective Larva Stage 198 Biochemistry and Molecular Biology of Filarial Chitinases 200 Chitinase-like Proteins in Vertebrates 201 Immunological Aspects of Filarial Chitinases 204 x Contents Acknowledgements 207 References 207 11 Acetylcholinesterase Secretion by Nematodes 211 Murray E. Selkirk, Siân M. Henson, Wayne S. Russell and Ayman S. Hussein Introduction and Historical Perspective 211 Cholinesterase Structure and Function 211 Nematode Acetylcholinesterases 212 Acetylcholinesterase Secretion by Parasitic Nematodes 213 Forms and Properties of the Secreted Enzymes 215 Putative Functions for Secreted Acetylcholinesterases 217 Regulation of intestinal peristalsis or local spasm 217 Regulation of intestinal transport processes 218 Regulation of lymphoid/myeloid cell functions 219 Hydrolysis of alternative substrates 220 Binding to ingested AChE inhibitors 220 Acetylcholine Receptor Expression in the Intestinal Tract 221 Nematode Acetylcholinesterases as Drug Targets 222 Concluding Remarks 223 Acknowledgements 224 References 224 12 The Surface and Secreted Antigens of Toxocara canis: Genes, Protein Structure and Function 229 Rick M. Maizels and Alex Loukas Introduction 229 Developmental Biology of Toxocara 230 Immune Evasion 230 Excreted/Secreted Glycoproteins (TES) 231 Recombinant Excreted/Secreted Proteins 231 TES-26, Tc-PEB-1, phosphatidylethanolamine-binding protein 232 TES-32, Tc-CTL-1, C-type lectin-1 233 TES-45 and TES-55 236 TES-70, Tc-CTL-4, C-type lectin-4 236 TES-120, Tc-MUC-1, MUC-2 and MUC-3 mucins 237 TES-400 237 Novel ES proteins? 238 Secreted Enzymes 238 Proteases 238 Superoxide dismutases 238 The Surface Coat 239 The NC6/SXC Domain in T. canis 239 Contents xi Venom Allergen Homologues: Tc-CRISP (Tc-VAH-1) and Tc-VAH-2 240 Carbohydrate Moieties 241 Concluding Remarks 242 Acknowledgements 242 References 243 13 Nematode Gut Peptidases, Proteins and Vaccination 247 David P. Knox, Philip J. Skuce, George F.
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