Advances in insect physiology, volume 47

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Academic Press is an imprint of Elsevier 32 Jamestown Road, London NW1 7BY, UK The Boulevard, Langford Lane, Kidlington, Oxford OX5 1GB, UK 225 Wyman Street, Waltham, MA 02451, USA 525 B Street, Suite 1800, San Diego, CA 92101-4495, USA First edition 2014 Copyright © 2014 Elsevier Ltd All rights reserved No part of this publication may be reproduced or transmitted in any form or by any means, electronic or mechanical, including photocopying, recording, or any information storage and retrieval system, without permission in writing from the publisher Details on how to seek permission, further information about the Publisher’s permissions policies and our arrangements with organizations such as the Copyright Clearance Center and the Copyright Licensing Agency, can be found at our website: www.elsevier.com/permissions This book and the individual contributions contained in it are protected under copyright by the Publisher (other than as may be noted herein) Notices Knowledge and best practice in this field are constantly changing As new research and experience broaden our understanding, changes in research methods, professional practices, or medical treatment may become necessary Practitioners and researchers must always rely on their own experience and knowledge in evaluating and using any information, methods, compounds, or experiments described herein In using such information or methods they should be mindful of their own safety and the safety of others, including parties for whom they have a professional responsibility To the fullest extent of the law, neither the Publisher nor the authors, contributors, or editors, assume any liability for any injury and/or damage to persons or property as a matter of products liability, negligence or otherwise, or from any use or operation of any methods, products, instructions, or ideas contained in the material herein ISBN: 978-0-12-800197-4 ISSN: 0065-2806 For information on all Academic Press publications visit our website at store.elsevier.com CONTRIBUTORS Michael J Adang Department of Entomology, and Department of Biochemistry and Molecular Biology, University of Georgia, Athens, Georgia, USA Md Shohidul Alam Division of Chemistry and Structural Biology, Institute for Molecular Bioscience, The University of Queensland, St Lucia, Queensland, Australia James A Baum Monsanto Company, Chesterfield, Missouri, USA Niraj S Bende Division of Chemistry and Structural Biology, Institute for Molecular Bioscience, The University of Queensland, St Lucia, Queensland, Australia Colin Berry Cardiff School of Biosciences, Cardiff University, Cardiff, United Kingdom Neil Crickmore School of Life Sciences, University of Sussex, Falmer, Brighton, United Kingdom Rhoel R Dinglasan Department of Molecular Microbiology and Immunology, The Johns Hopkins Bloomberg School of Public Health, Baltimore, Maryland, USA Andrea J Dowling Biosciences, University of Exeter, Cornwall, United Kingdom Richard H ffrench-Constant Biosciences, University of Exeter, Cornwall, United Kingdom Volker Herzig Division of Chemistry and Structural Biology, Institute for Molecular Bioscience, The University of Queensland, St Lucia, Queensland, Australia Juan Luis Jurat-Fuentes Department of Entomology and Plant Pathology, University of Tennessee, Knoxville, Tennessee, USA Robert M Kennedy Vestaron Corporation, Kalamazoo, Michigan, USA Glenn F King Division of Chemistry and Structural Biology, Institute for Molecular Bioscience, The University of Queensland, St Lucia, Queensland, Australia Paul J Linser The University of Florida Whitney Laboratory, St Augustine, Florida, USA vii viii Thomas Meade Dow AgroSciences, LLC., Indianapolis, Indiana, USA Kenneth E Narva Dow AgroSciences, LLC., Indianapolis, Indiana, USA Leˆda Regis Centro de Pesquisas Aggeu Magalha˜es-Fiocruz, Recife-Pernambuco, Brazil James K Roberts Monsanto Company, Chesterfield, Missouri, USA Maria Helena Neves Lobo Silva Filha Centro de Pesquisas Aggeu Magalha˜es-Fiocruz, Recife-Pernambuco, Brazil Nicholas P Storer Dow AgroSciences, LLC., Indianapolis, Indiana, USA H William Tedford Vestaron Corporation, Kalamazoo, Michigan, USA Yidong Wu College of Plant Protection, Nanjing Agricultural University, Nanjing, China Contributors PREFACE The idea for this volume on “Insect midgut and insecticidal proteins” was conceived from the realization that not a single source of reviews covers the insect midgut and insecticidal proteins isolated from bacteria or arthropods This volume benefits anyone researching to find solutions for insect pest control in agriculture and in public health The first chapter reviews “Insect gut structure, function, development and target of biological toxins” The insect midgut is the first barrier or a target for ingested toxophores (small-molecule insecticides or insecticidal proteins) For insecticidal proteins from the bacteria, Bacillus, Lysinibacillus and Photorhabdus, the midgut provides several target sites by which these proteins manifest their toxic action However, for many target sites in other tissues, the midgut can be a barrier for efficient delivery, like peptides from spider venom (Chapter 8) Although a lot of the information reviewed here is from mosquito and Drosophila midguts, these approaches and understanding can help draw parallels and differences between phytophagous insects (agriculturally important) versus hematophagus insects (medical importance) Additional proteomic studies on the midgut to identify and characterize putative target sites would be beneficial for developing or discovering alternate mechanisms of action Linser and Dinglasan have provided an excellent review of the insect midgut with a discussion of possible target sites Chapters 2–5 review various aspects of insecticidal proteins from Bacillus and Lysinibacillus In Chapter 2, Adang et al review the diversity of insecticidal proteins (three domain crystal (Cry), Cytolytic (Cyt), Binary Cry and other parasporal toxins) from Bacillus They review the mode of action of these proteins, providing similarities and differences in the receptors used for manifesting toxicity The identification and characterization of toxin receptors is important not only to create opportunities for discovering newer toxins but also to modify known toxins to target insect pests that are less or non-susceptible Moreover, such investigations allow the development of strategies to overcome or delay the development of resistance to insecticidal proteins In Chapter 3, Filha et al review the Binary (Bin) proteins from Lysinibacillus sphaericus (Ls) that are mosquitocidal The authors discuss the structure, function and mechanisms by which these proteins cause toxicity ix x Preface in mosquito larvae Unlike genes encoding insecticidal proteins from Bacillus species, which are now used as transgenes in crops for creating insect pest resistance, the Ls bacteria have been used as biolarvicides The potential of using Bacillus thuringiensis (Bt) as bioinsecticides was recognized in the early twentieth century, and subsequently many Bt products from Bt strains were developed for commercial use However, these products suffered from a lack of stability in the sprayed environment and reduced efficacies It was not until the first genes encoding Cry insecticidal proteins were cloned that research to their use as transgenes was initiated Between 1995 and 1996, the first transgenic crop (potato, corn and cotton) carrying a Cry gene for controlling an insect species was developed Since then, there has been a rapid adoption of transgenic crops worldwide, increasing from 1.7 million hectares in 1996 to just over 175 million hectares in 2013 This trend for reliance on transgenic crops will continue to grow until newer, better and more effective approaches to prevent damage from insect pests are discovered and developed In Chapter 4, Narva et al review the discovery and use of genes encoding insecticidal Bt Cry proteins for developing transgenic crops that provide control of insect pests In this chapter, the use of multiple Cry genes (gene stacking or pyramiding) is also reviewed to describe approaches to not only broaden the spectrum of insect pests controlled within a crop but also providing an approach to delay the development of insect resistance to a single Bt gene product The authors not only review the various Bt genes that have been used for developing transgenic crops but also provide an overview of approaches used for transferring genes into crops, selection of transgenic events and what needs to be done to register and the deployment of such transgenic crops in different geographic regions Every time a new mechanism for insect pest control is developed, it comes with the possibility of the target insect developing resistance, making the product less efficacious The authors provide a brief overview of insect resistance management strategies, which is reviewed more extensively in Chapter by Wu In Chapter 5, Baum and Roberts review yet another approach that relies on knocking down or down regulating genes encoding proteins essential for target insect pest survival The use of double-stranded RNAi (dsRNAi) has been very effectively used in non-arthropods and plants to knock down genes to understand gene function in specific pathways This approach has now been used for inactivating specific genes critical to the survival of insect pests This approach is an alternative to the use of chemical Preface xi insecticides for interfering with the function of target site proteins However, the use of dsRNAi provides a much higher level of selective toxicity to insect pests and serves as an attractive approach Although there are no commercial products harnessing this approach as yet, it will not be long before such products are commercially available In the last chapter (Chapter 6) related to Bt insecticidal proteins, Wu reviews resistance development and resistance management strategies for transgenic crops carrying Bt genes The development of resistance is inevitable, and the challenge faced is how strategies can be deployed to delay the targeted insect pests from developing resistance to the insecticidal proteins in host transgenic crops In this respect, it is also important to understand the mechanisms and target site receptors/proteins these insect toxins use for manifesting insecticidal activity and the mechanisms that lead to resistance development This aspect of resistance ties very well with the review in Chapter on mode of action of Bt proteins Chapters and review alternate sources of insecticidal proteins or peptides The discovery of insecticidal proteins from the bacteria Photorhabdus and Xenorhabdus created a lot of interest among academic labs and industry to understand the structure–function and mode of action of these very large (molecular size) and complex proteins This is reviewed in Chapter Although genes encoding these proteins or their peptides have not been used as transgenes in crops to control specific insect pests, the information generated can be leveraged with new approaches and capabilities to possibly make use of such genes (modified or unmodified) ffrench-Constant and Dowling have provided an extensive review of the many proteins from the two bacteria, high-resolution structures and possible mechanisms of action of the insecticidal proteins In Chapter on “Methods for deployment of spider venom peptides as bioinsecticides”, the authors describe a novel source of peptides from spider venom that show very interesting and selective toxic activities in insects Most of these act on neuropeptide targets and provide a challenging opportunity as how to make use of these peptides as biopesticides or use knowledge of their structures to invent new small-molecule toxophores that can interact at the same target sites used by the peptides from the spider venom Chapters in this volume were chosen to provide a single comprehensive review of structure and function of the insect midgut and the insecticidal proteins and genes that have been used as alternatives to chemical insecticides for controlling insect pests of agricultural and medical importance xii Preface Discovery of newer insect control approaches and their use will be an important component of increasing crop yields in an ever-shrinking arable land and continued insect transmission of many human diseases in an increasing world population that is projected to increase to billion by 2050 TARLOCHAN S DHADIALLA SARJEET S GILL CHAPTER ONE Insect Gut Structure, Function, Development and Target of Biological Toxins Paul J Linser*, Rhoel R Dinglasan† *The University of Florida Whitney Laboratory, St Augustine, Florida, USA † Department of Molecular Microbiology and Immunology, The Johns Hopkins Bloomberg School of Public Health, Baltimore, Maryland, USA Contents Introduction Mosquito Larval Alimentary Canal Other Insects 3.1 Lepidopteran larvae (caterpillars) 3.2 Coleopterans (beetles and their larvae) 3.3 Hemipterans (aphids) Conclusions and Comment References 27 28 30 31 32 33 Abstract Insects as vectors of disease to humans and domesticated animals and as direct agricultural pests are a source of tremendous economic and health-related challenge The eating habits of insects can provide the bases for disease transmission or the outright destruction of crops The alimentary canal of insects is a common target and often barrier for pest control strategies Recent advances in technology have made it possible to develop ever better understanding of the structure/function of the insect gut and hence provide new and better targets for developing novel methods for limiting the burdens that insects can present to humanity In this review, we focus attention on recent developments in our understanding of insect gut structure/function with particular emphasis on a few of the most challenging groups of insects: mosquitoes (dipterans), caterpillars (lepidopterans), beetles (coleopterans) and aphids (hemipterans) INTRODUCTION The alimentary canal of any higher organism is part of that organism’s first order environmental contact Consequently insects have evolved highly Advances in Insect Physiology, Volume 47 ISSN 0065-2806 http://dx.doi.org/10.1016/B978-0-12-800197-4.00001-4 # 2014 Elsevier Ltd All rights reserved Paul J Linser and Rhoel R Dinglasan specialised capacities to live in many varied ecological niches ranging from aquatic to terrestrial to airborne In all cases, gut function is crucial for survival and hence is specifically adapted to the life style of the insect Details associated with the ingestion of biological substrate (food), digestion of that material into useable small molecules and finally the absorption of the liberated nutrients into the cells, tissues and hemolymph of the animal are complex and varied from specie to specie The purpose of this review is to address structural details of the insect alimentary canal with commentary on the structural interface for targeting of the gut with biological toxins The importance of developmental changes and lifestyle differences between life stages will also be addressed It is beyond the scope of any single review to address specific details for the wide variety of insects and their specialisations of the gut Therefore, we have selected a few representative model systems for discussion The importance of insects to life on earth including human existence is indisputable For us as co-inhabitants of the planet, insects have particular relevance in their capacity to interfere with aspects of our health and wellbeing Many insects have evolved complex relationships with organisms and viruses that can cause human disease Hematophagy has evolved in arthropods over 20  (Black and Kondratieff, 2005) The propensity to take blood meals from vertebrates in general has been accompanied by the development of the capacity to harbour and transmit disease microbes and viruses This reality creates numerous challenges for human beings ranging from negative impacts on domesticated animal stocks as well as the vectoring of human pathogens directly Therefore, one of the most important groups of insects for the purposes of this review is mosquitoes, which transmit some of the deadliest known human pathogens The morbidity and mortality brought about by hematophagy of mosquitoes results in incalculable losses of life and human potential Our efforts to control mosquito populations with various pesticides and integrated strategies are continuously thwarted by the capacity of mosquitoes to adapt and evolve rapidly under selective pressure Hence, a deep understanding of mosquito biology is essential for the development of new disease control strategies The gut of the mosquito (Dipterans) in both larval and adult stages is a productive target for control strategies and hence a point of emphasis in this review Human development and the use of agriculture has provided a basis for the expansion of our species from hunter-gatherers dependent on the whim of Mother Nature to the truly dominating natural force on our planet Agricultural development has been continuously challenged by opportunistic Insect Gut Structure, Function, Development and Target of Biological Toxins and natural competitors for the crops in the field Relevant to this review of course are a range of insect “pests” which consume or damage crops in a variety of ways including the transmission of plant diseases The impact of pest insects on the world economy and the security of the human food supply is gigantic Hence, we will also review the structural biology of certain groups of agricultural threats: Lepidopteran and coleopteran larvae and hemipteran life stages that impact crops Of course, there are many and diverse insects that will not be covered in this review but we hope to present structural considerations that can be instructive and of fairly generalised relevance MOSQUITO LARVAL ALIMENTARY CANAL For the purpose of this review, we will not go into detailed discussion of structure/function analyses that have been reviewed in great detail previously There are superb resources for examining the depth of analyses performed with the foundational techniques of traditional microscopy and biochemistry (e.g Billingsley, 1990; Billingsley and Lehane, 1996; Lehane and Billingsley, 1996) Herein, we will focus on a broad structural view associated with fairly recent applications of newer techniques for structure/function analysis Development of the insect alimentary canal has been investigated exhaustively and excellent reviews and reference texts are available (e.g Klowden, 2007) A generalised summary of the embryological origins of the cells of the gut is shown in Fig 1.1 Posterior and anterior invaginations of the embryonic ectoderm give rise to the anus and mouth respectively Masses of endodermal cells emerge from the invaginating epithelium and give rise to the endodermal tube that will eventually connect forming the midgut The invaginating ectodermal cells will become the hindgut and foregut Fusion of the epithelial primordia eventually produces the continuity of the alimentary canal and all of its subdivisions (Klowden, 2007) Dipterans such as mosquitoes are holometabolous This term means that they exhibit very distinct larval developmental stages, pupation and the emergence of an adult imago that does not resemble the larval stages (Klowden, 2007) Similarly lepidopterans that includes butterflies and moths such as Manduca sext and coleopterans (beetles) have very distinct larval and adult stages such that casual observation might lead one to believe the different life stages are actually different organisms Differences in organismal structures are quite severe such that environmental niches of dissimilar stages of a given organism can be vastly different representing very distinct selective 408 Volker Herzig et al Thus, in summary, there are a wide variety of methods by which ISVPs can be deployed as natural insecticides We also recently demonstrated for the first time that the pharmacophore of ISVPs can be used to rationally develop small-molecule mimetics with improved oral activity, thereby providing another approach by which these peptides can be exploited for the control of insect pests ACKNOWLEDGEMENTS The authors would like to thank the Australian Research Council for financial support R.M Kennedy was funded in part by a grant from the Foundation for the National Institutes of Health through the Vector-based Transmission of Control: Discovery Research (VCTR) program of the Grand Challenges in Global Health initiative REFERENCES Atkinson, R.K., Howden, M.E.H., Tyler, M.I., Vonarx, E.J., 1998 Insecticidal toxins derived from funnel web (Atrax or Hadronyche) spiders U.S Patent No 5,763,568 Audsley, N., Matthews, J., Nachman, R., Weaver, R.J., 2007 Metabolism of cydiastatin and analogues by enzymes associated with the midgut and haemolymph of Manduca sexta larvae Gen Comp Endocrinol 153, 80–87 Audsley, N., Matthews, J., Nachman, R.J., Weaver, R.J., 2008 Transepithelial flux of an allatostatin and analogs across the anterior midgut of Manduca sexta larvae in vitro Peptides 29, 286–294 Baell, J.B., Forsyth, S.A., Gable, R.W., Norton, R.S., Mulder, R.J., 2001 Design and synthesis of type-III mimetics of ω-conotoxin GVIA J Comput Aided Mol Des 15, 1119–1136 Baell, J.B., Duggan, P.J., Forsyth, S.A., Lewis, R.J., Lok, Y.P., Schroeder, C.I., 2004 Synthesis and biological evaluation of nonpeptide mimetics of ω-conotoxin GVIA Bioorg Med Chem 12, 4025–4037 Bailey, K.L., Boyetchko, S.M., 2010 Social and economic drivers shaping the future of biological control: a Canadian perspective on the factors affecting the development and use of microbial biopesticides Biol Control 52, 221–229 Bingham, J.P., Mitsunaga, E., Bergeron, Z.L., 2010 Drugs from slugs—past, present and future perspectives of ω conotoxin research Chem Biol Interact 183, 1–18 Blackledge, T.A., Scharff, N., Coddington, J.A., Szuts, T., Wenzel, J.W., Hayashi, C.Y., Agnarsson, I., 2009 Reconstructing web evolution and spider diversification in the molecular era Proc Natl Acad Sci U.S.A 106, 5229–5234 Bloom, D.E., 2011 billion and counting Science 333, 562–569 Bonning, B.C., Chougule, N.P., 2014 Delivery of intrahemocoelic peptides for insect pest management Trends Biotechnol 32, 91–98 Bonning, B.C., Hammock, B.D., 1996 Development of recombinant baculoviruses for insect control Annu Rev Entomol 41, 191–210 Bonning, B.C., Pal, N., Liu, S., Wang, Z., Sivakumar, S., Dixon, P.M., King, G.F., Miller, W.A., 2014 Toxin delivery by the coat protein of an aphid-vectored plant virus provides plant resistance to aphids Nat Biotechnol 32, 102–105 Boyer, S., Zhang, H., Lemperiere, G., 2012 A review of control methods and resistance mechanisms in stored-product insects Bull Entomol Res 102, 213–229 Brady, R.M., Baell, J.B., Norton, R.S., 2013 Strategies for the development of conotoxins as new therapeutic leads Mar Drugs 11, 2293–2313 Spider Venom Peptides as Bioinsecticides 409 Cao, C.W., Liu, G.F., Wang, Z.Y., Yan, S.C., Ma, L., Yang, C.P., 2010 Response of the gypsy moth, Lymantria dispar to transgenic poplar, Populus simonii  P nigra, expressing fusion protein gene of the spider insecticidal peptide and Bt-toxin C-peptide J Insect Sci 10, 200 Casartelli, M., Corti, P., Giovanna Leonardi, M., Fiandra, L., Burlini, N., Pennacchio, F., Giordana, B., 2005 Absorption of albumin by the midgut of a lepidopteran larva J Insect Physiol 51, 933–940 Chong, Y., Hayes, J.L., Sollod, B., Wen, S., Wilson, D.T., Hains, P.G., Hodgson, W.C., Broady, K.W., King, G.F., Nicholson, G.M., 2007 The ω-atracotoxins: selective blockers of insect M-LVA and HVA calcium channels Biochem Pharmacol 74, 623–638 De Faria, M.R., Wraight, S.P., 2007 Mycoinsecticides and mycoacaricides, a comprehensive list with worldwide coverage and international classification of formulation types Biol Control 43, 237–256 Escoubas, P., Sollod, B., King, G.F., 2006 Venom landscapes: mining the complexity of spider venoms via a combined cDNA and mass spectrometric approach Toxicon 47, 650–663 Fitches, E., Woodhouse, S.D., Edwards, J.P., Gatehouse, J.A., 2001 In vitro and in vivo binding of snowdrop (Galanthus nivalis agglutinin; GNA) and jackbean (Canavalia ensiformis; Con A) lectins within tomato moth (Lacanobia oleracea) larvae; mechanisms of insecticidal action J Insect Physiol 47, 777–787 Fitches, E., Edwards, M., Mee, C., Grishin, E., Gatehouse, A., Edwards, J., Gatehouse, J., 2004 Fusion proteins containing insect-specific toxins as pest control agents: snowdrop lectin delivers fused insecticidal spider venom toxin to insect haemolymph following oral ingestion J Insect Physiol 50, 61–71 Fitches, E.C., Pyati, P., King, G.F., Gatehouse, J.A., 2012 Fusion to snowdrop lectin magnifies the oral activity of insecticidal ω-hexatoxin-Hv1a peptide by enabling its delivery to the central nervous system PLoS One 7, e39389 Fletcher, J.I., Smith, R., O’donoghue, S.I., Nilges, M., Connor, M., Howden, M.E., Christie, M.J., King, G.F., 1997 The structure of a novel insecticidal neurotoxin, ω-atracotoxin-HV1, from the venom of an Australian funnel web spider Nat Struct Biol 4, 559–566 Gassmann, A.J., Petzold-Maxwell, J.L., Clifton, E.H., Dunbar, M.W., Hoffmann, A.M., Ingber, D.A., Keweshan, R.S., 2014 Field-evolved resistance by western corn rootworm to multiple Bacillus thuringiensis toxins in transgenic maize Proc Natl Acad Sci U.S.A 111, 5141–5146 Gatehouse, A.M.R., Ferry, N., Edwards, M.G., Bell, H.A., 2011 Insect-resistant biotech crops and their impacts on beneficial arthropods Philos Trans R Soc Lond B Biol Sci 366, 1438–1452 Hardy, M.C., Daly, N.L., Mobli, M., Morales, R.A., King, G.F., 2013 Isolation of an orally active insecticidal toxin from the venom of an Australian tarantula PLoS One 8, e73136 Hernandez-Campuzano, B., Suarez, R., Lina, L., Hernandez, V., Villegas, E., Corzo, G., Iturriaga, G., 2009 Expression of a spider venom peptide in transgenic tobacco confers insect resistance Toxicon 53, 122–128 Ikonomopoulou, M., King, G.F., 2013 Natural born insect killers: spider-venom peptides and their potential for managing arthropod pests Outlooks Pest Manag 24, 16–19 Inceoglu, A.B., Kamita, S.G., Hammock, B.D., 2006 Genetically modified baculoviruses: a historical overview and future outlook Adv Virus Res 68, 323–360 James, C., 2012 Global Status of Commercialized Biotech/GM Crops: 2012 ISAAA Brief 44-2012 International Service for the Acquisition of Agri-Biotech Applications, Ithaca, NY Jiang, H., Zhu, Y.X., Che, Z.L., 1996 Insect resistance of transformed tobacco plants with the gene of the spider insecticidal peptide J Integr Plant Biol (Acta Bot Sin.) 38, 95–99 410 Volker Herzig et al Kennedy, R.M., Steinbaugh, B.A., 2013 Insecticidal triazines and pyrimidines U.S Patent Application 8389718 B2 Khan, S.A., Zafar, Y., Briddon, R.W., Malik, K.A., Mukhtar, Z., 2006 Spider venom toxin protects plants from insect attack Transgenic Res 15, 349–357 King, G.F., 2011 Venoms as a platform for human drugs: translating toxins into therapeutics Expert Opin Biol Ther 11, 1469–1484 King, G.F., Hardy, M.C., 2013 Spider-venom peptides: structure, pharmacology, and potential for control of insect pests Annu Rev Entomol 58, 475–496 King, G.F., Tedford, H.W., Maggio, F., 2002 Structure and function of insecticidal neurotoxins from Australian funnel-web spiders J Toxicol Toxin Rev 21, 359–389 Klint, J.K., Senff, S., Saez, N.J., Seshadri, R., Lau, H.Y., Bende, N.S., Undheim, E.A., Rash, L.D., Mobli, M., King, G.F., 2013 Production of recombinant disulfide-rich venom peptides for structural and functional analysis via expression in the periplasm of E coli PLoS One 8, e63865 Kuhn-Nentwig, L., St€ ocklin, R., Nentwig, W., 2011 Venom composition and strategies in spiders: is everything possible? Adv Insect Physiol 40, 1–86 Lomer, C.J., Bateman, R.P., Johnson, D.L., Langewald, J., Thomas, M.B., 2001 Biological control of locusts and grasshoppers Annu Rev Entomol 46, 667–702 Maggio, F., Sollod, B.L., Tedford, H.W., Herzig, V., King, G.F., 2010 Spider toxins and their potential for insect control In: Gilbert, L.I., Gill, S.S (Eds.), Insect Pharmacology: Channels, Receptors, Toxins and Enzymes Academic Press, London, pp 101–123 McKay, G.A., Reddy, R., Arhin, F., Belley, A., Lehoux, D., Moeck, G., Sarmiento, I., Parr, T.R., Gros, P., Pelletier, J., Far, A.R., 2006 Triaminotriazine DNA helicase inhibitors with antibacterial activity Bioorg Med Chem Lett 16, 1286–1290 Menzler, S., Bikker, J.A., Suman-Chauhan, N., Horwell, D.C., 2000 Design and biological evaluation of non-peptide analogues of ω-conotoxin MVIIA Bioorg Med Chem Lett 10, 345–347 Michiels, K., Van Damme, E.J., Smagghe, G., 2010 Plant-insect interactions: what can we learn from plant lectins? Arch Insect Biochem Physiol 73, 193–212 Miller, W.A., Bonning, B.C., 2007 Plant resistance to insect pests mediated by viral proteins U.S Patent No 7,312,080 Moar, W.J., Anilkumar, K.J., 2007 Plant science The power of the pyramid Science 318, 1561–1562 Mukherjee, A.K., Sollod, B.L., Wikel, S.K., King, G.F., 2006 Orally active acaricidal peptide toxins from spider venom Toxicon 47, 182–187 Nartey, R., Owusu-Dabo, E., Kruppa, T., Baffour-Awuah, S., Annan, A., Oppong, S., Becker, N., Obiri-Danso, K., 2013 Use of Bacillus thuringiensis var israelensis as a viable option in an Integrated Malaria Vector Control Programme in the Kumasi Metropolis, Ghana Parasit Vectors 6, 116 Nyffeler, M., Sunderland, K.D., 2003 Composition, abundance and pest control potential of spider communities in agroecosystems: a comparison of European and US studies Agric Ecosyst Environ 95, 579–612 Oerke, E.C., 2006 Crop losses to pests J Agric Sci 144, 31–43 Omar, A., Chatha, K.A., 2012 National Institute for Biotechnology and Genetic Engineering (NIBGE): genetically modified spider cotton Asian J Manag Cases 9, 33–58 Pal, N., Yamamoto, T., King, G.F., Waine, C., Bonning, B., 2013 Aphicidal efficacy of scorpion- and spider-derived neurotoxins Toxicon 70, 114–122 Pallaghy, P.K., Nielsen, K.J., Craik, D.J., Norton, R.S., 1994 A common structural motif incorporating a cystine knot and a triple-stranded β-sheet in toxic and inhibitory polypeptides Protein Sci 3, 1833–1839 Pardo-Lo´pez, L., Sobero´n, M., Bravo, A., 2013 Bacillus thuringiensis insecticidal threedomain Cry toxins: mode of action, insect resistance and consequences for crop protection FEMS Microbiol Rev 37, 3–22 Spider Venom Peptides as Bioinsecticides 411 Platnick, N.I., 2013 The world spider catalog, version 13.5, American Museum of Natural History Online at http://research.amnh.org/entomology/spiders/catalog/index.html Que, Q., Chilton, M.D., De Fontes, C.M., He, C., Nuccio, M., Zhu, T., Wu, Y., Chen, J.S., Shi, L., 2010 Trait stacking in transgenic crops: challenges and opportunities GM Crops 1, 220–229 Ripka, A.S., Rich, D.H., 1998 Peptidomimetic design Curr Opin Chem Biol 2, 441–452 Roberts, D.W., 1973 Means for insect regulation: fungi Ann N Y Acad Sci 217, 76–84 Saez, N.J., Senff, S., Jensen, J.E., Er, S.Y., Herzig, V., Rash, L.D., King, G.F., 2010 Spidervenom peptides as therapeutics Toxins 2, 2851–2871 Sandhu, S., Sharma, A.K., Beniwal, K., Goel, G., Batra, P., Kumar, A., Jaglan, S., Sharma, A.K., Malhotra, S., 2012 Myco-biocontrol of insect pests: factors involved, mechanism, and regulation J Pathog 2012, 126819 Shah, P.A., Pell, J.K., 2003 Entomopathogenic fungi as biological control agents Appl Microbiol Biotechnol 61, 413–423 Shah, A.D., Ahmed, M., Mukhtar, Z., Khan, S.A., Habib, I., Malik, Z.A., Mansoor, S., Saeed, N.A., 2011 Spider toxin (Hvt) gene cloned under phloem specific RSs1 and RolC promoters provides resistance against American bollworm (Heliothis armigera) Biotechnol Lett 33, 1457–1463 Skaer, H.B., Maddrell, S.H., Harrison, J.B., 1987 The permeability properties of septate junctions in Malpighian tubules of Rhodnius J Cell Sci 88, 251–265 Smith, J.J., Herzig, V., King, G.F., Alewood, P.F., 2013 The insecticidal potential of venom peptides Cell Mol Life Sci 70, 3665–3693 Sobero´n, M., Fernandez, L.E., Perez, C., Gill, S.S., Bravo, A., 2007 Mode of action of mosquitocidal Bacillus thuringiensis toxins Toxicon 49, 597–600 Tabashnik, B.E., Brevault, T., Carriere, Y., 2013 Insect resistance to Bt crops: lessons from the first billion acres Nat Biotechnol 31, 510–521 Tedford, H.W., Fletcher, J.I., King, G.F., 2001 Functional significance of the β hairpin in the insecticidal neurotoxin ω-atracotoxin-Hv1a J Biol Chem 276, 26568–26576 Tedford, H.W., Gilles, N., Menez, A., Doering, C.J., Zamponi, G.W., King, G.F., 2004a Scanning mutagenesis of ω-atracotoxin-Hv1a reveals a spatially restricted epitope that confers selective activity against insect calcium channels J Biol Chem 279, 44133–44140 Tedford, H.W., Sollod, B.L., Maggio, F., King, G.F., 2004b Australian funnel-web spiders: master insecticide chemists Toxicon 43, 601–618 Tedford, H.W., Steinbaugh, B.A., Bao, L., Tait, B.D., Tempczyk-Russell, A., Smith, W., Benzon, G.L., Finkenbinder, C.A., Kennedy, R.M., 2013 In silico screening for compounds that match the pharmacophore of omega-hexatoxin-Hv1a leads to discovery and optimization of a novel class of insecticides Pestic Biochem Physiol 106, 124–140 Tice, C.M., 2001 Selecting the right compounds for screening: does Lipinski’s Rule of for pharmaceuticals apply to agrochemicals? Pest Manag Sci 57, 3–16 Vilcinskas, A., Matha, V., Gotz, P., 1997 Effects of the entomopathogenic fungus Metarhizium anisopliae and its secondary metabolites on morphology and cytoskeleton of plasmatocytes isolated from the greater wax moth, Galleria mellonella J Insect Physiol 43, 1149–1159 Vollrath, F., Selden, P., 2007 The role of behavior in the evolution of spiders, silks, and webs Annu Rev Ecol Evol Syst 38, 819–846 Wang, C., St Leger, R.J., 2007 A scorpion neurotoxin increases the potency of a fungal insecticide Nat Biotechnol 25, 1455–1456 Windley, M.J., Herzig, V., Dziemborowicz, S.A., Hardy, M.C., King, G.F., Nicholson, G.M., 2012 Spider-venom peptides as bioinsecticides Toxins 4, 191–227 INDEX Note: Page numbers followed by “f ” indicate figures and “t ” indicate tables A ABCC2 proteins chromosome 15, 323 Cry1Ab resistance, 323 HvCad, 323 YHD2 strain, 323 A disintegrin and metalloprotease (ADAM), 62–63, 191 ADP-ribosyltransferases, 351–352, 356–357 Aedes A aegypti α–glucosidases, 118t larvae, 4–6 SEM image, 10–12 ALPs, 60–61 Bin toxin, 96–97 cadherin, 15 Cry11Aa and Cry11Ba, 59 and Culex, 127–129 GC cells, 17–20, 21f SEM image, 4–6, 5f, 10–12, 11f Agrobacterium, 196–197 Alkaline phosphatase, 60–61 Amber disease-associated plasmid (pADAP), 349–350 AMG See Anterior midgut (AMG) Aminopeptidase-N (APN), 58–59 Anopheles A gambiae alimentary canal, 22f dsRNAs, 263–264 human HeLa cells, 106–107 maltase 3, 114 mosquito control, 128t A merus, 13–14 and Culex, 93 larvae, 125–126 Anterior midgut (AMG) caecal neck adjoins, 10 GC and PMG, 10 lumen pH, 4–6 proton pump, 17–20 Anti-feeding pro-phage (Afp) locus, 365, 367–368 APN See Aminopeptidase-N (APN) Arabidopsis thaliana, 251, 307–308 Aspartyl autoprotease, 356 ATP-binding cassette (ABC) transporter, 61–62, 121, 316 B Bacillus thuringiensis (Bt) biopesticides, 179–184 and BTI, 4–6 BT-R1, 59–60 characteristics, 41–42 cotton, 399–400 crops (see Bt crops) Cry35 and Cry36, 102 Cry11Ba toxin, 17 Cry toxins (see Crystal toxins (Cry toxins)) Cyt1Aa protein, 99 description, 179 discovery and development, 40–41 δ-endotoxins, 178–179 GE crops (see Genetically engineered (GE) crops) GM crops, 31–32 insecticidal proteins (see Bt insecticidal proteins) and Ls strains, 128t mosquitocidal toxins, 145–148 phenotypic trait, 41 S-layer protein, 109 Baculoviruses, 397–398 Barriers to RNAi B germanica and M sexta, 275 cellular uptake, 271–272 Dicer and Argonaute proteins, 271–272 Drosophila, 274–275 dsRNA degradation, 272, 273f endocytic pathways, C elegans, 274–275 “housekeeping” gene, 270–271 mechanism, dsRNA uptake, 275 413 414 Barriers to RNAi (Continued ) mRNA transcript levels, 270–271 nutrients, absorption, 271–272 Sid-1 and Sid-2 genes, 272–274 virus infections, 275 BBM See Brush border membrane (BBM) BBMF See Brush-border membrane fractions (BBMF) Binary (Bin) toxins analysis, 99 BinA and BinB proteins, 97–99 binding, receptor, 101 block mutation, BinB, 102–104 circular dichroism analysis, 99–100 cross-resistance, 102–104 Cry49, 102 Cx pipiens, 101 gastric caecum and posterior midgut, 100 ingestion, mosquito larvae, 100 mosquitocidal, 43–46 N-and C-termini, 102–104 patch-clamp experiments, 101–102 PirAB, 379 pore formation, 102 P20 protein, 99 receptors (see Receptors, Bin toxin) tryptophan residues, 104 Vip1Aa1 and Vip2Aa1, 186–187 XaxAB cytotoxin, 379–380 YaxAB cytotoxin, 379–380 Bioinsecticides entomopathogens, 397–399 ISVPs (see Insecticidal spider-venom peptides (ISVPs)) Biolarvicides accumulation of spores, 111–112 in China, 131–134 Lysinibacillus sphaericus, 93 vector-control programmes, 127–129 Blattella germanica, 275 Bollgard II® cotton, 225, 400 Bombyx mori ABCC2 genes, 61–62 C2 strain, 323–324 polycalin family, 63 Brush border membrane (BBM) black lipid membranes, 350–351 B thuringiensis spore, 55–56 GC cells, 18f Index microvillar array, 28–30 midgut epithelium, 55f physiological targeting/binding, 22–23 and PMG, 18f topography, 271–272 Brush-border membrane fractions (BBMF), 113–114, 115f, 135 Bt biopesticides DipelT and ThuricideT, 180 endophytes, 184 israelensis (H 14), 180–181 lepidopteran pests, 180–181 plasmid-based DNA cloning, 181–182 products, 180, 181t properties, 182–183 Pseudomonas fluorescens, 183–184 recombinant strains, 182–183, 183t “sporeine”, 179–180 Bt corn Cry1A.105 and Cry2Ab, 217 Cry1Ab, Cry1Ac, Cry9C, Cry1Fa and Vip3Aa, 215 cultivation and commercialization, 215, 216t high-rootworm pressure, 217–224, 224f MON810 and Bt11, 215–217 mycotoxin contamination, 214 products, 217–224, 218t Bt cotton BollGard®, 225 cultivation and commercialization, 225, 227t development, 224–225, 226f H zea, 208 products, United States, 225, 228t reductions, 214 Bt crops adoption, 214 Cry GE plants, 196–197 Cry toxins, 314–317 discovery and development process, 193–194 DNA shuffling, 231 domain exchange, 231–232 field-evolved resistance, 300, 312–314 gene discovery, 194–196 germplasm, 198 insect resistance management, 207–210 IRAC, 300 Index lepidopterans, 314, 315f protease activation, 230–231 refuge strategy, 298–299 resistance detection methods (see Resistance detection, Bt) resistance management, 324–331 resistance mechanisms, 314–324 site directed mutagenesis, 231 transformation technologies, 197–198 transgenic crops, 298 Bt insecticidal proteins ABCC2, 193 Bt Toxin Specificity Database, 185–186 cross-order activity, 185–186 Cry proteins, 187–190 Cyt proteins, 190–191 diversity, 184–185 mechanisms of resistance, 191–193 receptors, 191 Vip3 proteins, 186–187 Bt potato, 226–230 Bt soybean, 225–226 C Cabbage moths, 395 Cadherins (CADs) BBM, 22–23 BtR1, Bt4R strain, 319 cell–cell interactions, 59–60 Cry3Aa and Cry3Bb toxins, 59–60 Cry1Ac resistance, 320 Cry toxin receptors, 59–60 DsCad, 320 extracellular and intracellular domain, 320, 321f HvCad, 319 Lepidoptera, 192 locus, 306f mutants, 310 Caenorhabditis elegans, 191, 250–251, 283–284 Caudate phage-derived proteins, 365 Coat protein (CP), 395–396, 396f Coleopterans agricultural pests, 30–31 corn roots, 186–187, 253–261 Cry3Bb toxins, 59–60 415 Dibrotica virgifera virgifera, 30–31 extracellular matrix, 30 “housekeeping” gene, 270–271 midguts, 271–272 red flour beetle, 261–262 sensitivity level, ingested dsRNA, 253 Snf7 dsRNAs, 253–261, 280–281 Tc-ASH and UBX genes, 261–262 Tribolium and Diabrotica, 261–262 type I peritrophic matices, 30–31 Concentration–response and diagnostic concentration assays Bt protein source and forms, 303 diagnostic concentration test, 301–302 laboratory strains, 301, 302 MVPII, 303 protein source, 303 target pest populations, 302 Corn events with Bt genes, 216t Costelytra zealandica, 349–350, 361–362 Cotton events with Bt genes, 227t CP See Coat protein (CP) Cqm1 vs Aam1 α–glucosidases, 119–121 Crystalline (Cry) proteins ALPs, 60–61 Cry1A.105, 211 Cry1Ab, 210 Cry1Ac, 210–211 Cry1Fa2, 211 Cry2Ab, 211 Cry2Ae, 212 Cry3Aa1 and Cry1Aa1, 187–188, 188f Cry34Ab1/Cry35Ab1, 213 Cry3Bb1, 213 eCry3.1Ab, 212–213 δ-endotoxins, 187 GPI-anchored APN, 192–193 mCry3Aa, 212 mechanism of action, 188–190, 190f pore formation, 317 structures, PDB accession, 188, 189t Vip3Aa, 212 Crystal toxins (Cry toxins) ABCC2, 323–324 alkaline phosphatase, 322–323 aminopeptidase, 321–322 bacterial pore-forming, 67 cadherin, 319–320 cell death, 317 416 Crystal toxins (Cry toxins) (Continued ) Cry1Aa, 49–50, 50f Cry1Ac protoxin, 318 Cry34 protein, 67–68 definition and classification, 42–43 diversity, 43–46 domain I, 50–51 domain II, 51–53 domain III, 53–55 δ-endotoxins, 314 enterocyte death, 66–67 genomic sequencing, 49 α4 helix lining, 66 insect-resistance trait, 397 intoxication process, 55–56, 55f midgut Cry-binding proteins, 57–63 models, 63–68 oligomer formation, 317 parasporin, 47–48 PCR and next-generation sequencing, 49 proteins and molecules, 62–63 protoxin, 49–50 receptors, 316 ricin domain, 48 sequential binding model, 316 signalling pathway, 316 solubilization and proteolytic processing, 56–57 structural domains, 315–316 Culex and Aedes species, 127–129 and Anopheles, 93 C pipiens, 97t, 102–104, 113–114, 132t C quinquefasciatus Cry48Aa/Cry49Aa toxin, 105f growth and mortality, 102–104 maltase 1, 114, 132t Synergism, 69–70 larvae, 99 mosquitoes, 104 Cytolytic (Cyt) proteins description, 184–185 mosquitoes and blackflies, toxicity, 187 structure and function, 190–191, 190f D Dibrotica virgifera virgifera, 30–31, 253 Diptera Index Aedes aegypti and Anopheles gambiae, 263–264 Drosophila, 262–263 DNA screening bioassay, 310–311 cadherin mutations, 311 HaCad, 311 PCR method, 311 r15 cadherin allele, 311–312 DNA shuffling, 231 Dolichus biflorus agglutinin (DBA), 15–17, 16f Dorsal anterior rectum (DAR) cells, 13–14, 26f Drosophila melanogaster Cry1Ac, 64–65 dsRNA, 262 embryo system, 374–375 S2 cells, 275 E Egg shell structures, 352–353 δ-Endotoxins, 178–179, 187, 314, 379, 397 Entomopathogens Bacillus thuringiensis (Bt), 397 baculoviruses, 397–398 bioinsecticides, 397–398 Cry toxins, 397 δ-endotoxins, 397 fungi and parasites (nematodes), 149–150 Green Muscle®, 398 ISVPs, 398–399 Mycotrol®, 398 Entropic spring mechanism, 355–356, 356f Environmental effects, GE crops agronomic properties, 205 cultivation, 203 gene flow, 205 grain importation, 205 hazard testing, 203–204 monarch butterflies, larvae, 204 non-GE isoline, 205 Environmental RNAi arthropod pests, 269–270 Coleoptera, 253–262 components, 252–253 definitions, 252 417 Index Diptera, 262–264 Hemiptera, 267–269 ingested dsRNAs, 252–253, 254t Lepidoptera, 264–267 Escherichia coli Bin toxin, 148 clones, 370–371 dsRNAs, 266 host cells, 106–107 F Fibrobacter succinogenes, 361–362 Field-evolved resistance, Bt crops Cry1Ac resistance, 325–328, 328f F1 and F2 screens, 325 high-dose/refuge strategy, 312–314 hypothesis, 324–325 incipient and practical resistance, 312 lepidopterans, 325, 326t target pests, 312, 313t, 325–328 Flea-rodent enzootic cycles, 362–363 Fluorescent nanoparticles (FNPs), 278–279 Food safety, 202–204, 281–282 Fruit fly, 262 F1 screen, resistance detection Cry1Ab, 304–305 Cry1Ac, 304 laboratory strain, 305, 306f locus, 306 resistance allele frequencies, 304–305 F2 screen, resistance detection cadherin mutants, 310 Cry1Ac resistance, 307–308 diagnostic concentration assay, 307 lepidopteran pests, 307 resistance alleles, 308–310, 309t target pests, 308–310 G Galanthus nivalis agglutinin (GNA), 395–397 Gene duplication, 107–108 Genetically engineered (GE) crops environmental effects, 203–205 environmental, food and feed safety profile, 199 EPA, 206–207 human health assessment, 201–203 PMM, 207 product identification and characterization, 201 recombinant DNA techniques, 198–199 regulatory systems, 199 safety assessments, 199, 200t stacks, 206 GNA See Galanthus nivalis agglutinin (GNA) Gram-negative Rhs proteins, 352–353 Green Muscle®, 398 Guanine nucleotide-binding protein (GNBP), 269–270 H HBA See Hydrogen-bond acceptor (HBA) HBDs See Hydrogen-bond donors (HBDs) Heat shock protein (Hsp) 90, 360 Helicoverpa armigera Bt cotton, 224–225 Cry1Ac binding, 58 EcR gene, 265–266 and 1642 iso-female lines, 307–308 RNA interference, 59 Helicoverpa punctigera in Australia, 325–328 cropping areas, 305 Cry2Ab resistance, 307–308 Cry1Ac resistance, 307–308 Helicoverpa zea Bt cotton, 208 Cry1Ac-selected AR1 strain, 322–323 GE plants resistance, 196–197 Heliothis virescens and cotton bollworm, 53–55 Cry1Ac-expression, 225 and M sexta, 60–61 YHD3, 323 Hemimetabolous macroscopic features, 27–28 nymph to adults, Hemipterans aphids, 31–32 dietary concentrations, 267–268 dsRNA feeding, 267–268 hunchback gene, 267–268 nitrophorin (Np2) gene, 267–268 N lugens, 269 Rack-1 and C002, 268–269 Herbivorous insects, 2–3, 390 418 ωHexatoxin (Hv1a) Asn27, 403 development, small-molecule mimetics, 402, 403f 3D solution structure, 402 Gly8, 403 pharmacophore model, 404, 404t physical properties, 404–405 primary pharmacophore residues, 402 residues, 3D pharmacophore, 404, 404t SAR data, 403 site-directed mutagenesis and synthetic truncates, 402 type-II mimetics, development, 407 Val33 side chain, 402 VNX-000440, 404–405 Holometabolous adult stages, dipterans, 3–4 Human health assessment allergenic potential, 201–202 breeding and crop improvement techniques, 202–203 Bt proteins, 201 nutritional profile, 202 protein levels, 202 soil and phylloplane microorganism, 201 toxicity, 202 Hv1a See ωHexatoxin (Hv1a) Hydrogen-bond acceptor (HBA), 402 Hydrogen-bond donors (HBDs), 403 I Influenza virus, 353–354 Inhibitor cystine knot, 391 In planta expression, ISVPs Bt corn, 399–400 Bt crops, 400 Cry toxins, 399–400 engineer plants, 400 genetically modified (GM) crops, 399 Lepidoptera and Coleoptera, 400 transgenic tobacco, ω-HXTX-Ar1a, 400 U7-HXTX-Mg1a (Magi-6), 400 Insect alimentary canal disease control strategies, gut function, 1–2 Index human development, 2–3 human disease, mosquito, 3–27 structure and function, 23–25 Insecticidal spider-venom peptides (ISVPs) chemical cocktails, 391 description, 391 disadvantages, 394 entomopathogens, 397–399 heterologous expression systems, 391 in planta expression, 399–400 inhibitor cystine knot, 391 insect control agents, 407–408 insecticidal effects, 394 mimetics, 401–407 oral activity, 394, 407–408 paracellular and transcellular transport routes, 394 properties, 391, 392t septate junctions, 394 transcytosis, 394–397 Insecticide Resistance Action Committee (IRAC), 300 Insect pest management See also RNA interference (RNAi) Arabidopsis, 251 description, 252 development, insecticides, 251 environmental RNAi (see Environmental RNAi) eukaryotic cells, 250 RISC, 250–251 Insect resistant crops, Bt See Bacillus thuringiensis (Bt) IRAC See Insecticide Resistance Action Committee (IRAC) ISVP mimetics Hv1a pharmacophore, 402–405, 407 type II mimic VNX-000440, 405–406 venom peptides, 401–402 J Juvenile hormone (JH), 266, 379 Juvenile nematodes, 345 L Larval feeding assays, 280–281 Lepidopteran larvae (caterpillars), 28–30, 29f, 59–60 Index Lepidopteran pests beet armyworm β1 subunit integrin (βSe1), 264–265 brown apple moth, 264 Bt genes, 283–284 chitinase genes, 264–265 Cry1Ac and Cry2Ab proteins, 282–283 Escherichia coli, 266 H armigera, 265–266 20 -O-methoxy nucleotides and deoxythymidin, siRNAs, 266 Ostrinia furnacalis, 266–267 Spodoptera frugiperda, 272, 273f tobacco plants, 265–266 WCR Snf7 dsRNA, 284–285 Luteoviruses, 395–396 Lymphatic filariasis transmission, 126–127 Lysinibacillus sphaericus (Ls) Bin toxin, 97–104 biolarvicides, 95–96 biological control agents, 149–150 classification, 91–92 Culex spp., 96–97 in DNA group IIA, 95–96 insecticidal factors, 91 micrography, 91, 92f mosquitocidal toxins, 148–149 as mosquito-control agent, 93–95 pathogen, mosquito, 90–91 safety studies, 109–111 saprophytic organism, 91 SSII-1 strain, 90–91 strains and larvicidal properties, 92–93, 94t M Makes caterpillars floppy (Mcf ) toxins 2929-amino acid protein, 371 Bcl2-homology 3-like (BH3-like) domain, 371–372, 371f caterpillar immune system, 370–371 cytotoxin B-like, 371, 371f description, 370 in vivo, 374–376 Mcf2, 372 MCF1-SHE domain, 373 Pseudomonas, Fit toxin, 373 repeats in toxins (RTX), 371, 371f 419 Malaria in Africa, 121–122 Plasmodium falciparum, 17 Manduca sexta BtR1, 52–53 caterpillars, 370–371 and coleopterans, 3–4 GalNAc, 58 tobacco hornworm, 264 Marine worm larva, 368–369 Mcf-like fit toxin in vivo Drosophila embryo, 374–375 regulation, Fit toxin expression, 375–376 Midgut Cry-binding (receptor) proteins ABC transporter, 61–62 alkaline phosphatase, 60–61 APN, 58–59 cadherin-like proteins, 59–60 Molecular transport vehicles, 394–397 Mono-ADP-ribosyltransferase (mART) toxin, 378–379 Mosquitocidal toxin (Mtx1) ADP-ribosyl transferase, 106–107 catalytic subunit, 107 double mutants, 107–108 gene encoding, 106 gut enzymes, 106–107 low-toxicity strain SSII-1, 107–108 LP1-G, 104–106 Mosquito control anophelines, 122–125 aquatic habitats, 121–122 biotic and abiotic factors, 125–126 large-scale field tests, 127–129, 128t LS-based products, 122–125, 123t lymphatic filariasis, 126–127 operational use, 129–130 small-and medium-scale, 122–125 transgenic corn plants, 276 Mosquito larval alimentary canal Aedes aegypti larvae, SEM, 4–6, 5f AgAPN1, 17, 18f Anopheles gambiae, 17–20, 19f anterior intestine/ileum, 13 apical-to-basal movement, 14 caecal diverticuli, 10 “CAP” cells, 8–10 cell biology and polarity, 14–15 420 Mosquito larval alimentary canal (Continued ) Cry-IVB toxin damage, 20–22 culicenes, 25–26, 26f disease vector species, embryonic development, 3, 4f endodermal epithelial cells, 8–10 gastric caeca cells, 8–10, 9f GC and CM, glycocalyx-type extracellular matrix, 15–17 hemimetabolous and holometabolous, 3–4 ileum/posterior intestine, 25–26 lepidopterans, 3–4 midgut, Aedes aegypti, 10–12, 11f MT cell biology, 22–23, 24f Na+/K+-ATPase and CA9, 20–22, 22f pH gradient, 17–20 physiological and immunohistochemical analyses, 12–13 PM, 7–8 pyloris and MTs, 12–13 rectum, 13–14 salivary glands, 6–7, 6f SG function, 15 V-ATPase, 17–20, 21f Mtx1 See Mosquitocidal toxin (Mtx1) Mu-like phage, 365 Mycotrol®, 398 N Neuraminidases, 353–354 Next-generation DNA sequencing technology, 195–196 Next-generation rootworm-resistant corn Bt insecticidal proteins, 277–278 Cry3Bb1 protein, 276–277, 276f Snf7 gene expression, 277–278 V-ATPase dsRNA, 276–277, 277f, 284 Nilaparvata lugens, 267–268, 269 N-terminal peptidase domain, 365–366 O Oral activity cell-free bacterial supernatant of Photorhabdus, 348 dietary small RNAs and longer dsRNAs, 281–282 Index Hv1a and SFI1, 395 ISVPs, 394, 401 Ostrinia furnacalis, 266–267, 278–279, 313t Ostrinia nubilalis Cry1Ab, 215–217 resistant strains, 192–193 stalk boring Lepidoptera, 215–217 P Paracellular transport, 394 Parasporin ETX/MTX family, 47–48 graphical representation, 44f, 47–48 P asymbiotica toxin (PaTox) description, 376–377 DxD motif, 376–377 heterotrimeric G proteins, 376–377 PaToxG domain, 376–378 Rho proteins, 376–378 SseI-like domain, 377–378 structure-function analysis, 377–378 Pea enation mosaic virus (PEMV), 395–396 Pectinophora gossypiella Bt crops, 313t field control efficacy, 299 Peptidomimetics classification, 401 pharmaco-kinetic properties, 401 Peptidyl prolyl cis/trans isomerases (PPIases), 360 Photorhabdus temperata, 344–345 Photorhabdus toxin (Photox) binary toxins, 379–380 Mcf Toxins, 370–376 P asymbiotica, 345–346 and Patox, 376–379 P temperata and P luminescens, 344–345 PVCs (see Photorhabdus virulence cassettes (PVCs)) toxin complexes (Tcs), 347–364 Photorhabdus virulence cassettes (PVCs) Afp toxin delivery system, 367–368 ‘bacteriocins’, 367 candidate effector proteins, 366–367 caudate phage-derived proteins, 365 description, 364–365 discovery and organization, 365–367 E coli, 366–367 421 Index infective juvenile, 369–370 injection of larvae, 366–367 Macs, 367, 368–369 marine worm larva, 368–369 open reading frames, 365–366 pADAP plasmid, 367–368 PaPVCpnf, 366–367 peptidoglycan hydrolytic activity, 369 phage-like structures, 367 Phage P2 gpX, 369 P luminescens TT01 and P asymbiotica ATCC43949, 365 putative PVC encoded effectors, 365–366 PVC-SS, 365–366, 369 receptors, 369–370 tailocins, 369–370 TEM, 366–367 type VI secretion system, 367 PirAB binary toxins, 379 P luminescens ABC Tc holotoxin ADP-ribosyltransferase domain, 356–357 B/C-formed shell, 356–357 cryo-EM structure, 357, 359f crystal structure B and C subunits, 356 egg-shell-like structure, 357, 359f entropic spring/linker, 355–356, 356f interaction of B/C (TcB/TcC) subunits, 356–357, 358f neuraminidase-like region, 353–354 PCT3 and PCT5, 353–354 pre-pore to pore state, 354 β-propeller, 356–357 receptor domains, 353–354, 355f PMM See Post market monitoring (PMM) Polymerase chain reaction (PCR) Bt cry gene, 195 RNAi, 253–261 toxin genes, 49 Polymorphic toxin systems, 361 Posterior midgut (PMG) and BBM, 18f Culex quinquefasciatus, 11f and GC cells, 10 granular surface, 10–12 larval mosquitoes, 22–23 Post market monitoring (PMM), 207 β-Propeller, 352–353, 356–357 Pseudomonas fluorescens, 183–184, 373 Pseudomonas syringae, 361–362, 373 PVCs See Photorhabdus virulence cassettes (PVCs) Pyramid, Bt crops Cry2Ab, 211 Cry proteins, 330–331 insect resistance, 282 pesticides, 329–330 target pests, 330–331 Pyrethroid, 127–129, 139–140 R Rapid virulence annotation (RVA)-like screens, 381–382 Rearrangement hotspot (Rhs), 351–353 Receptors, Bin toxin Cpm1 α-glucosidases, 117, 118t Cqm1/Cpm1 proteins, 119 Cry toxins, 119 fluorescent-labelled Bin toxin, 112–113, 113f α-glucosidases, 117 in vitro saturation, 113–114, 115f larvae midgut, 112–114 midgut-bound proteins, 114 mosquito susceptibility to Ls, 113–114, 116t quantitative assays, 113–114 Spodoptera frugiperda, 117–119 Refuge, Bt crops Cry toxins, 329 field-evolved resistance, 329 heterozygous progeny, 328–329 high dose, 209 insect resistance, 208 pest resistance, 328–329 Resistance detection, Bt allele frequency, 301 concentration-response and diagnostic concentration assays, 301–304 DNA screen, 310–312 field-evolved resistance, 301 F1 screen, 304–306 F2 screen, 307–310 pesticides, 301 422 Resistance management Bin-toxin, 145–150 biological cost, 141–143 biological risks, 209–210 Bt proteins, 283–284 Caenorhabditis, 283–284 cqm1 gene, 135–139, 137f development, 207–208 diagnosis and field survey, 139–140 factors, 129–130 field-evolved resistance, 324–328 heterozygous/homozygous, alleles, 209 high dose/refuge strategy, 282–283 host plants, 208 inheritance, 135 integrated mosquito-control programmes, 143–144 laboratory and field reports, 131–134, 132t natural refuges, 208 O nubilalis, 208 population genetics theory and simulation models, 209 prevention factors, 144 pyramid strategy, 329–331 refuge strategy, 328–329 stacking/pyramiding, 282 Ricin domain, 48 RNAi See RNA interference (RNAi) RNA-induced silencing complex (RISC), 250–251, 271–272 RNA interference (RNAi) barriers to delivery, 270–275 cost of goods, 279–280 environmental, 252–270 FNPs, 278–279 insect resistance management, 282–284 mechanism and delivery strategies, 278, 278f next-generation rootworm-resistant corn, 276–278 safety assessments, 280–282 siRNA formulation, 279 transfection agents, 278–279 S Septate junctions, 394 Sequential binding model, Cry1A, 64–65 Index Serine peptidase, 373 Site directed mutagenesis, 231 S-layer proteins, 109 Soybean and potato events with Bt genes, 229t Sphaericolysin, 108–109, 110f, 112f Spodoptera frugiperda, 117–119, 272, 273f Systemic RNAi arthropod pests, 269–270 Drosophila, 262–263 dsRNA degradation, 272 nematode, 283–284 sid-3 and sid-5 mutants, C elegans, 274–275 Snf7 dsRNA, 261–262 T Tail sheath protein, 365 Tc ABC complexes chaperones, 357–360 encapsulation and auto-proteolysis, C subunit, 352–353 holotoxin high-resolution structure, 353–357 low-resolution structure, 351–352 A subunit assembly, 350–351 Tomato moths, 395 Toxin complexes (Tcs) ABC complexes, 350–360 crop protection, 363–364 description, 347–348 discovery, gene cloning and ABC nomenclature, 348–349 infection Bacillus thuringiensis, 361–362 C zealandica midgut, 361–362 Fibrobacter succinogenes, 361–362 plague bacillus, 362–363 Pseudomonas syringae pv tomato, 361–362 Treponema denticola, 361–362 Y pestis, 362–363 ‘polymorphic’ toxins, 361 tc-like genes, diversity, 349–350 Toxin complex secretion system (TC-SS), 381–382, 383 Transcellular transport route, 394 Transcytosis, ISVPs aphids, 395–396 CP, 395–397 423 Index GNA, 395–397 insect haemocoel, 395, 396f lectins, 395 luteoviruses, 395–396 PEMV, 395–396 Transgenic baculovirus, 398–399 Treponema denticola, 361–362 Tribolium castaneum, 62–63, 191 Type II integral membrane proteins, 352–353 Type III secretion systems, 380–381 Type II mimic VNX-000440, 405–406, 406f Whiskers, 197–198 X XaxAB cytotoxin, 379–380 Xenorhabdus and Photorhabdus, 357–360, 361–362, 380–381 Tc subunits, 350–351 X bovienii, 346–347 X nematophila, 346–347, 349–350 X particulate toxins (xpt), 349–350 Y Vacuolar-ATPase (V-ATPase), 17–20, 270–271, 280–281 YaxAB cytotoxin, 379–380 YD-repeat proteins, 352–353 Y entomophaga strain MH96, 349–350 Yersinia pestis, 351–352, 362–363 W Z V Wall-associated protein A (WapA), 352–353 Ziconotide/Prialt®, 401 ... idea for this volume on Insect midgut and insecticidal proteins” was conceived from the realization that not a single source of reviews covers the insect midgut and insecticidal proteins isolated... of biological toxins” The insect midgut is the first barrier or a target for ingested toxophores (small-molecule insecticides or insecticidal proteins) For insecticidal proteins from the bacteria,... component of increasing crop yields in an ever-shrinking arable land and continued insect transmission of many human diseases in an increasing world population that is projected to increase to billion
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