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Molecular Mode of Action of Cry6aa1, a New Insecticidal Bacillus Thuringiensis Toxin

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Molecular Mode of Action of Cry6aa1, a New Insecticidal Bacillus Thuringiensis Toxin i ii Université de Montréal Molecular mode of action of Cry6Aa1, a new insecticidal Bacillus thuringiensis toxin par Eva Fortea Verdejo Département de physiologie moléculaire et intégrative Faculté de médecine Mémoire présenté en vue de l’obtention du grade de Maîtrise en physiologie moléculaire, cellulaire et intégrative option physiologie et biophysique moléculaires Membres du jurée Lucie Parent, Réjean Couture et Jean-Louis Schwartz Août 2016 © Eva Fortea Verdejo, 2016 iii ABSTRACT Cry6Aa1 is a new toxin produced by Bacillus thuringiensis (Bt), which displays insecticidal activity against the Western corn rootworm (WCRW). The present work demonstrates that Cry6Aa1 is a pore-forming toxin (PFT) in planar lipid bilayers (PLBs). Contrary to other Bt toxins tested so far, pore formation by Cry6Aa1 does not require protease pretreatment and takes place at doses that are two to three orders of magnitude lower than those required for other Bt toxins under similar conditions. Pore formation by Cry6Aa1 is pH-dependent; the conductances of the pores range between 31 and 689 pS under symmetrical 150 mM KCl conditions; they are cationic and display a complex kinetic behaviour. The treatment of the toxin with midgut juice (Cry6Aa1 WCR1) does not change the biophysical properties of the pores. However, the treatment with trypsin (Cry6Aa1 TT) affects their conductance and selectivity at pH 5.5 (the WCRW gut physiological pH). The incorporation in PLBs of native membrane material from WCRW midgut affects the behaviour of the Cry6Aa1 pores. The molecular determinants of the mode of action of this new PFT appear therefore to differ from those reported before for other Bt toxins. The three-dimensional (3-D) atomic structure of Cry6Aa1 has just been elucidated. It shows that the toxin assumes an α-helix-rich configuration, which is quite similar to that of the ClyA PFT produced by E. coli. Based on the data available for ClyA, we have studied how different changes in the N- and C-terminal regions of Cry6Aa1 affect its pore formation ability in PLBs. Key words: Planar lipid bilayer, bacterial toxin, Bacillus thuringiensis, pore-forming toxin, Western corn rootworm, Cry6Aa1, δ-endotoxin. iv RÉSUMÉ Cry6Aa1, une nouvelle toxine produite par Bacillus thuringiensis (Bt), agit comme insecticide sur la chrysomèle du maïs (WCRW). Dans cette étude, on démontre que Cry6Aa1 est une toxine formeuse de pores (TFP) en bicouches lipidiques planes (BLP). Contrairement aux autres toxines de Bt étudiées jusqu’à présent, la formation de pores par Cry6Aa1 ne requiert pas de prétraitement par protéases et se produit à des doses de toxine deux à trois ordres de grandeur plus faibles que celles nécessaires pour les autres toxines de Bt dans les mêmes conditions. La formation de pores par la forme non traitée de Cry6Aa1 dépend du pH; les pores obtenus ont des conductances comprises entre 31 et 689 pS en conditions symétriques de 150 mM de KCl; ils sont cationiques avec un comportement cinétique complexe. Les propriétés biophysiques des pores ne changent pas lorsque la toxine est traitée avec le suc du mésenthéron de l’insecte (Cry6Aa1 WCR1). Par contre, un traitement à la trypsine (Cry6Aa1 TT) modifie la conductance et la sélectivité des pores à pH 5,5 (le pH physiologique de l’intestin de WCRW). La reconstitution en BLP de fraction de membrane native du mésenthéron de WCRW affecte les propriétés des pores formés par Cy6Aa1. Les déterminants moléculaires du mode d’action de cette nouvelle toxine formeuse de pores semblent donc différer de ceux décrits précédemment pour d’autres toxines de Bt. La structure atomique tridimensionnelle de Cry6Aa1 vient tout juste d’être élucidée. Elle montre que la toxine adopte une conformation riche en hélices α qui ressemble fortement à celle de la TFP ClyA produite par E. coli. En se fondant sur les données disponibles pour ClyA, on a étudié l’effet de divers changements dans les régions N et C terminales de Cry6Aa1 sur sa capacité de former des pores en BLP. Mots-clés: Bicouche lipidique plane, toxine bactérienne, Bacillus thuringiensis, toxine formeuse de pore, Western corn rootworm, Cry6Aa1, δ-endotoxine v CONTENTS ABSTRACT .................................................................................................................................. iii RÉSUMÉ ...................................................................................................................................... iv CONTENTS .................................................................................................................................. v LIST OF FIGURES .................................................................................................................... vii LIST OF TABLES ....................................................................................................................... ix ABBREVIATION TABLE ........................................................................................................... x ACKNOWLEDGEMENTS ....................................................................................................... xii CHAPTER 1. INTRODUCTION ................................................................................................ 1 1.1. Bacillus thuringiensis (Bt) .................................................................................................... 1 1.1.1. Nomenclature ................................................................................................................. 1 1.1.2. Organisms affected by Bt toxins .................................................................................... 2 1.2. Mode of action of Bt toxins .................................................................................................. 3 1.2.1. Ingestion of Bt toxins ..................................................................................................... 4 1.2.2. Solubilization of Bt toxins ............................................................................................. 4 1.2.3. Activation of Bt toxins ................................................................................................... 4 1.2.4. Crossing the peritrophic membrane ............................................................................... 5 1.2.5. Molecular recognition of Bt toxins ................................................................................ 6 1.2.6. Pore formation ............................................................................................................... 9 1.2.7. Bt toxin effect on the membrane potential of lepidopteran insect midgut cells .......... 10 1.2.8. Intracellular effects of Bt toxins .................................................................................. 11 1.2.9. Proposed models of Bt mode of action ........................................................................ 12 1.3. Bt toxins structures and function ........................................................................................ 13 1.3.1. Cry toxins .................................................................................................................... 13 1.3.2. Other toxins ................................................................................................................. 19 1.4. Diabrotica virgifera virgifera (Western corn rootworm, WCRW) .................................... 21 1.4.1. Geographic distribution ............................................................................................... 22 1.4.2. Biological cycle and ecology ....................................................................................... 22 1.4.3. Physiology relevant to Bt studies ................................................................................. 23 1.4.4. Bt toxins currently used to control WCRWs ............................................................... 24 1.5. Cry6Aa1 toxin .................................................................................................................... 25 1.5.1. Target organisms ......................................................................................................... 25 1.5.2. Structure ....................................................................................................................... 26 1.5.3. Similarity of Cry6A to other toxins ............................................................................. 27 1.6. Contribution of co-authors and conferences ...................................................................... 32 vi 1.7. Objectives and hypotheses ................................................................................................. 32 1.7.1. Hypotheses ................................................................................................................... 33 1.7.2. Objectives .................................................................................................................... 33 CHAPTER 2. MATERIALS AND METHODS ....................................................................... 34 2.1. Cry6Aa preparation ............................................................................................................ 34 2.1.1. Toxins used .................................................................................................................. 34 2.1.2. Solubilisation ............................................................................................................... 34 2.1.3. Activation ...................................................................................................................
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