The Structure/Function of New Insecticidal Proteins and Regulatory Challenges for Commercialization
Total Page:16
File Type:pdf, Size:1020Kb
Load more
Recommended publications
-
WO 2019/067496 Al 04 April 2019 (04.04.2019) W 1P O PCT
(12) INTERNATIONAL APPLICATION PUBLISHED UNDER THE PATENT COOPERATION TREATY (PCT) (19) World Intellectual Property Organization I International Bureau (10) International Publication Number (43) International Publication Date WO 2019/067496 Al 04 April 2019 (04.04.2019) W 1P O PCT (51) International Patent Classification: C07K 14/00 (2006.01) A01N 63/00 (2006.01) C12N 15/63 (2006.01) (21) International Application Number: PCT/US20 18/052788 (22) International Filing Date: 26 September 2018 (26.09.2018) (25) Filing Language: English (26) Publication Language: English (30) Priority Data: 62/563,228 26 September 2017 (26.09.2017) US (71) Applicant: DOW AGROSCIENCES LLC [US/US]; 9330 Zionsville Road, Indianapolis, IN 46268 (US). (72) Inventors: ZACK, Marc D.; 9330 Zionsville Road, Indi¬ anapolis, IN 46268 (US). SOPKO, Megan; 9330 Zionsville Road, Indianapolis, IN 46268 (US). HASLER, James M.; 9330 Zionsville Road, Indianapolis, IN 46268 (US). (74) Agent: RIVAS, Marcos; Dow AgroSciences LLC, 9330 Zionsville Road, Indianapolis, Indiana 46268 (US). (81) Designated States (unless otherwise indicated, for every kind of national protection available) : AE, AG, AL, AM, AO, AT, AU, AZ, BA, BB, BG, BH, BN, BR, BW, BY, BZ, CA, CH, CL, CN, CO, CR, CU, CZ, DE, DJ, DK, DM, DO, DZ, EC, EE, EG, ES, FI, GB, GD, GE, GH, GM, GT, HN, HR, HU, ID, IL, IN, IR, IS, JO, JP, KE, KG, KH, KN, KP, KR, KW, KZ, LA, LC, LK, LR, LS, LU, LY, MA, MD, ME, MG, MK, MN, MW, MX, MY, MZ, NA, NG, NI, NO, NZ, OM, PA, PE, PG, PH, PL, PT, QA, RO, RS, RU, RW, SA, SC, SD, SE, SG, SK, SL, SM, ST, SV, SY, TH, TJ, TM, TN, TR, TT, TZ, UA, UG, US, UZ, VC, VN, ZA, ZM, ZW. -
Appendix 5.3 MON 810 Literature Review – List of All Hits (June 2016
Appendix 5.3 MON 810 literature review – List of all hits (June 2016-May 2017) -Web of ScienceTM Core Collection database 12/8/2016 Web of Science [v.5.23] Export Transfer Service Web of Science™ Page 1 (Records 1 50) [ 1 ] Record 1 of 50 Title: Ground beetle acquisition of Cry1Ab from plant and residuebased food webs Author(s): Andow, DA (Andow, D. A.); Zwahlen, C (Zwahlen, C.) Source: BIOLOGICAL CONTROL Volume: 103 Pages: 204209 DOI: 10.1016/j.biocontrol.2016.09.009 Published: DEC 2016 Abstract: Ground beetles are significant predators in agricultural habitats. While many studies have characterized effects of Bt maize on various carabid species, few have examined the potential acquisition of Cry toxins from live plants versus plant residue. In this study, we examined how live Bt maize and Bt maize residue affect acquisition of Cry1Ab in six species. Adult beetles were collected live from fields with either currentyear Bt maize, oneyearold Bt maize residue, twoyearold Bt maize residue, or fields without any Bt crops or residue for the past two years, and specimens were analyzed using ELISA. Observed Cry1Ab concentrations in the beetles were similar to that reported in previously published studies. Only one specimen of Cyclotrachelus iowensis acquired Cry1Ab from twoyearold maize residue. Three species acquired Cry1Ab from fields with either live plants or plant residue (Cyclotrachelus iowensis, Poecilus lucublandus, Poecilus chalcites), implying participation in both liveplant and residuebased food webs. Two species acquired toxin from fields with live plants, but not from fields with residue (Bembidion quadrimaculatum, Elaphropus incurvus), suggesting participation only in live plantbased food webs. -
US Department of Agriculture
Environmental Assessment for Dow/Pioneer Rootworm Resistant Corn APHIS’ Analysis and Response to Comments Received on Petition 03-353-01p and the EA. A total of two comments were submitted during the designated 60-day comment period by a private individual and a national trade association. The comment submitted by the trade association supported deregulation of the Cry34/35 Ab1 corn rootworm resistant corn (CRW). This comment stressed the importance of a different mechanism of control compared to the only CRW resistant corn product on the market while providing a new option for managing insect resistance. The commenter also mentioned that this product would provide a wider range of plant protection. The comment in opposition to deregulation of this product was submitted by a private citizen. This commenter expressed a general disapproval of genetically modified plants and suggested that this product should always be regulated. APHIS disagrees with this comment. The author fails to provide any information to support her assertion that this petition should be denied. The commenter also suggested that APHIS extend the comment period, but failed to provide a reason for the extension. Further, this commenter discussed pesticidal issues related to EPA’s role in the regulation of plant incorporated protectants. APHIS defers to EPA on issues related to EPA’s authority. - 2 - Environmental Assessment for Dow/Pioneer Rootworm Resistant Corn USDA/APHIS Decision on Dow AgroSciences and Pioneer Hi-Bred International Petition 03-353-01P Seeking a Determination of Nonregulated Status for Bt cry34/35Ab1 Insect Resistant Corn Line DAS-59122-7 Environmental Assessment TABLE OF CONTENTS I. -
TECHNISCHE UNIVERSITÄT MÜNCHEN Structural And
TECHNISCHE UNIVERSITÄT MÜNCHEN Fakultät für Chemie Lehrstuhl für Biochemie Structural and biochemical characterization of the YaxAB pore- forming toxin from Yersinia enterocolitica Bastian Loong Wang Yung Shan Bräuning Vollständiger Abdruck der von der Fakultät für Chemie der Technischen Universität München zur Erlangung des akademischen Grades eines Doktors der Naturwissenschaften (Dr. rer. nat.) genehmigten Dissertation. Vorsitzende/-r: Prof. Dr. Matthias Feige Prüfende/-r der Dissertation: 1. Prof. Dr. Michael Groll 2. Prof. Dr. Franz Hagn 3. Prof. Dr. Michal Sharon (schriftliche Begutachtung), 4. Prof. Dr. Tanja Gulder (mündliche Prüfung) Die Dissertation wurde am 09.04.2018 bei der Technischen Universität München eingereicht und durch die Fakultät für Chemie am 23.05.2018 angenommen. Table of contents Chapter 1 ...................................................................................................................................................................... 11 Introduction ............................................................................................................................................................. 11 1.1 The enterobacteriaceae: successful pathogens with a broad host spectrum .................... 11 1.1.1 The human pathogen Yersinia enterocolitica ........................................................................ 12 1.1.2 The insect pathogen Photorhabdus luminescens .................................................................. 12 1.2 Pore-forming toxins (PFT) as virulence -
Nor Hawani Salikin
Characterisation of a novel antinematode agent produced by the marine epiphytic bacterium Pseudoalteromonas tunicata and its impact on Caenorhabditis elegans Nor Hawani Salikin A thesis in fulfilment of the requirements for the degree of Doctor of Philosophy School of Biological, Earth and Environmental Sciences Faculty of Science August 2020 Thesis/Dissertation Sheet Surname/Family Name : Salikin Given Name/s : Nor Hawani Abbreviation for degree as give in the University : Ph.D. calendar Faculty : UNSW Faculty of Science School : School of Biological, Earth and Environmental Sciences Characterisation of a novel antinematode agent produced Thesis Title : by the marine epiphytic bacterium Pseudoalteromonas tunicata and its impact on Caenorhabditis elegans Abstract 350 words maximum: (PLEASE TYPE) Drug resistance among parasitic nematodes has resulted in an urgent need for the development of new therapies. However, the high re-discovery rate of antinematode compounds from terrestrial environments necessitates a new repository for future drug research. Marine epiphytic bacteria are hypothesised to produce nematicidal compounds as a defence against bacterivorous predators, thus representing a promising, yet underexplored source for antinematode drug discovery. The marine epiphytic bacterium Pseudoalteromonas tunicata is known to produce a number of bioactive compounds. Screening genomic libraries of P. tunicata against the nematode Caenorhabditis elegans identified a clone (HG8) showing fast-killing activity. However, the molecular, chemical and biological properties of HG8 remain undetermined. A novel Nematode killing protein-1 (Nkp-1) encoded by an uncharacterised gene of HG8 annotated as hp1 was successfully discovered through this project. The Nkp-1 toxicity appears to be nematode-specific, with the protein being highly toxic to nematode larvae but having no impact on nematode eggs. -
Bacillus Thuringiensis As a Specific, Safe, and Effective Tool for Insect Pest Control
J. Microbiol. Biotechnol. (2007), 17(4), 547–559 Bacillus thuringiensis as a Specific, Safe, and Effective Tool for Insect Pest Control ROH, JONG YUL, JAE YOUNG CHOI, MING SHUN LI, BYUNG RAE JIN1, AND YEON HO JE* Department of Agricultural Biotechnology, College of Agriculture and Life Sciences, Seoul National University, Seoul 151-742, Korea 1College of Natural Resources and Life Science, Dong-A University, Busan 604-714, Korea Received: November 21, 2006 Accepted: January 2, 2007 Bacillus thuringiensis (Bt) was first described by Berliner The insecticidal bacterium Bt is a Gram-positive [10] when he isolated a Bacillus species from the Mediterranean bacterium that produces proteinaceous inclusions during flour moth, Anagasta kuehniella, and named it after the sporulation [53]. These inclusions can be distinguished as province Thuringia in Germany where the infected moth distinctively shaped crystals by phase-contrast microscopy. was found. Although this was the first description under The inclusions are composed of proteins known as crystal the name B. thuringiensis, it was not the first isolation. In proteins, Cry proteins, or δ-endotoxins, which are highly 1901, a Japanese biologist, Ishiwata Shigetane, discovered toxic to a wide variety of important agricultural and a previously undescribed bacterium as the causative health-related insect pests as well as other invertebrates. agent of a disease afflicting silkworms. Bt was originally Because of their high specificity and their safety for the considered a risk for silkworm rearing but it has become environment, crystal proteins are a valuable alternative the heart of microbial insect control. The earliest commercial to chemical pesticides for control of insect pests in production began in France in 1938, under the name agriculture and forestry and in the home. -
The Pesticidal Cry6aa Toxin from Bacillus Thuringiensis Is Structurally
Dementiev et al. BMC Biology (2016) 14:71 DOI 10.1186/s12915-016-0295-9 RESEARCH ARTICLE Open Access The pesticidal Cry6Aa toxin from Bacillus thuringiensis is structurally similar to HlyE- family alpha pore-forming toxins Alexey Dementiev1, Jason Board2, Anand Sitaram3, Timothy Hey4,7, Matthew S. Kelker4,10, Xiaoping Xu4, Yan Hu3, Cristian Vidal-Quist2,8, Vimbai Chikwana4, Samantha Griffin4, David McCaskill4, Nick X. Wang4, Shao-Ching Hung5, Michael K. Chan6, Marianne M. Lee6, Jessica Hughes2,9, Alice Wegener2, Raffi V. Aroian3, Kenneth E. Narva4 and Colin Berry2* Abstract Background: The Cry6 family of proteins from Bacillus thuringiensis represents a group of powerful toxins with great potential for use in the control of coleopteran insects and of nematode parasites of importance to agriculture. These proteins are unrelated to other insecticidal toxins at the level of their primary sequences and the structure and function of these proteins has been poorly studied to date. This has inhibited our understanding of these toxins and their mode of action, along with our ability to manipulate the proteins to alter their activity to our advantage. To increase our understanding of their mode of action and to facilitate further development of these proteins we have determined the structure of Cry6Aa in protoxin and trypsin-activated forms and demonstrated a pore-forming mechanism of action. Results: The two forms of the toxin were resolved to 2.7 Å and 2.0 Å respectively and showed very similar structures. Cry6Aa shows structural homology to a known class of pore-forming toxins including hemolysin E from Escherichia coli and two Bacillus cereus proteins: the hemolytic toxin HblB and the NheA component of the non- hemolytic toxin (pfam05791). -
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. -
Rubina Mushtaq (M.Phil)
Production of Bacillus thuringiensis Recombinant Cry Proteins and Analysis of Mode of Action of their Toxicity Thesis Submitted to University of the Punjab, Lahore for the Award of Degree of Doctor of Philosophy in Biological Sciences By Rubina Mushtaq (M.Phil) Research Supervisor Prof. Dr. A.R. Shakoori Aizaz-i-Kamal, Tamgha-i-Imtiaz, ECO Laureate Distinguished National Professor, Professor Emeritus School of Biological Sciences, University of the Punjab School of Biological Sciences, University of the Punjab, Lahore, Pakistan 2018 i DEDICATION I would like to dedicate this work to my parents, my husband and to my loving children who helped me unconditionally ii SUMMARY The Cry insecticidal proteins of Bacillus thuringiensis (Bt) are produced by transgenic crops for effective and environmentally-safe insect pest control. These transgenic Bt crops are considered to be the most successful agricultural biotechnology for insect control, yet their sustainability is threatened by the evolution of resistance in targeted pests. The evidence suggests that this resistance is probably due to the alterations in recognition of Cry toxin receptors in the insect midgut membrane. Consequently, information is needed on determinants of receptor recognition for designing improved toxins and to adopt effective insect resistance management practices. In this study four Cry proteins, Cry1Ac, Cry2Ac7, Cry1Fa and Cry1Ie2 were expressed either in E. coli expression system or in native Bt strain. Insoluble Cry1Ac and Cry2Ac7 proteins were refolded and purified prior to use. Bioassays of Cry1Ac (C-terminally truncated version) and Cry2Ac7 protoxins were performed with an armyworm, Spodoptera litura Fabricius (Lepidoptera: Noctuidae), a polyphagous cosmopolitan insect which is a serious crop pest of many Asian countries including Pakistan. -
Us 2018 / 0362598 A1
US 20180362598A1 ( 19) United States ( 12) Patent Application Publication (10 ) Pub . No. : US 2018 /0362598 A1 CARLSON et al. ( 43 ) Pub . Date: Dec . 20 , 2018 ( 54 ) CLEAVABLE PEPTIDES AND INSECTICIDAL CO7K 5 / 103 ( 2006 .01 ) AND NEMATICIDAL PROTEINS CO7K 14 /435 (2006 .01 ) COMPRISING SAME CO7K 14 /325 ( 2006 .01 ) (71 ) Applicant: VESTARON CORPORATION , A01N 63 /02 ( 2006 .01 ) KALAMAZOO , MI (US ) C12N 15 /82 (2006 .01 ) (72 ) Inventors : ALVAR R . CARLSON , (52 ) U . S . CI. KALAMAZOO , MI (US ) ; CPC . .. .. CO7K 14 /415 (2013 .01 ) ; CO7K 7 / 06 ALEXANDRA M . HAASE , MARTIN , (2013 .01 ) ; CO7K 5 / 101 ( 2013. 01 ) ; CO7K MI (US ) ; ROBERT M . KENNEDY , 14 / 43518 (2013 .01 ) ; CO7K 14 / 325 (2013 . 01 ) ; DEXTER , MI (US ) CO7K 2319 / 04 ( 2013 .01 ) ; C12N 15 /8285 ( 2013 . 01 ) ; C12N 15 /8286 ( 2013 .01 ) ; COZK ( 73 ) Assignee : VESTARON CORPORATION , 2319 /50 (2013 .01 ) ; CO7K 2319 /55 (2013 .01 ) ; KALAMAZOO , MI (US ) A01N 63 / 02 (2013 .01 ) ( 21 ) Appl. No. : 15 /727 , 277 ( 22 ) Filed : Oct . 6 , 2017 (57 ) ABSTRACT Related U . S . Application Data A peptide comprised of either a binary or a tertiary peptide, (60 ) Provisional application No. 62 /411 , 117 , filed on Oct. the peptide contains at least 4 amino acids and up to a 21 , 2016 . maximum of 16 amino acids, comprised of 2 or 3 different regions, wherein the binary peptides have 2 different regions Publication Classification and the tertiary peptides have 3 different regions; wherein , (51 ) Int . Cl. the peptide can be cleaved by both an animal gut protease CO7K 14 /415 ( 2006 .01 ) and an insect or nematode gut protease . -
Technical Document for Bacillus Thuringiensis Cry34ab1 And
BIOPESTICIDES REGISTRATION ACTION DOCUMENT Bacillus thuringiensis Cry34Ab1 and Cry35Ab1 Proteins and the Genetic Material Necessary for Their Production (PHP17662 T-DNA) in Event DAS-59122-7 Corn (OECD Unique Identifier: DAS-59122-7) PC Code: 006490 U.S. Environmental Protection Agency Office of Pesticide Programs Biopesticides and Pollution Prevention Division Bacillus thuringiensis Cry34/35Ab1 Corn Biopesticides Registration Action Document (BRAD) September 2010 Table of Contents I. OVERVIEW A. Background 4 B. Use Profile 7 C. Regulatory History 8 II. SCIENCE ASSESSMENT A. Product Characterization 14 B. Human Health Assessment 41 C. Environmental Assessment 66 D. Insect Resistance Management 117 E. Benefits 172 III. REGULATORY POSITION FOR EVENT DAS-59122-7 CORN A. Initial Registration (August 31, 2005) 193 B. 2010 Update 195 C. Period of Registration 197 APPENDIX A 199 2 Bacillus thuringiensis Cry34/35Ab1 Corn Biopesticides Registration Action Document (BRAD) September 2010 Bacillus thuringiensis Cry34Ab1 and Cry35Ab1 Proteins and the Genetic Material Necessary for Their Production (PHP17662 T-DNA) in Event DAS-59122-7 Corn Regulatory Action Team Product Characterization and Human Health Rebecca Edelstein, Ph.D. John Kough, Ph.D. Annabel Waggoner Chris Wozniak, Ph.D. Environmental Fate and Effects Joel Gagliardi, Ph.D. Hillary Hill Tessa Milofsky Robyn Rose Zigfridas Vaituzis, Ph.D. Annabel Waggoner Insect Resistance Management Jeannette Martinez Sharlene Matten, Ph.D. Tessa Milofsky Alan Reynolds Benefits Assessment Edward Brandt Sharlene Matten, Ph.D. Tessa Milofsky Registration Support Mike Mendelsohn Sheryl Reilly, Ph.D. Ann Sibold Biopesticides Registration Action Document Team Leaders Jeannine Kausch Mike Mendelsohn Office of General Counsel Angela Huskey, Esq. 3 Bacillus thuringiensis Cry34/35Ab1 Corn Biopesticides Registration Action Document (BRAD) September 2010 I. -
Biopesticides Fact Sheet for Bacillus Thuringiensis Cry34ab1 And
Bacillus thuringiensis Cry34Ab1 and Cry35Ab1 proteins and the genetic material necessary for their production (plasmid insert PHP 17662) in Event DAS-59122-7 corn (006490) Fact Sheet I. Description of the Plant-Incorporated Protectant o Pesticide Name: Bacillus thuringiensis Cry34Ab1 and Cry35Ab1 proteins and the genetic material necessary for their production (plasmid insert PHP 17662) in Event DAS-59122-7 corn o Date Registered: August 31, 2005 o Registration Numbers: 68467-5, 29964-4 o Trade and Other Names: Event DAS-59122-7 corn, Herculex Rootworm, Herculex RW o OPP Chemical Code: 006490 o Basic Manufacturers: Mycogen Seeds c/o Dow AgroSciences LLC 330 Zionsville Road, Indianapolis, IN 46268 Pioneer Hi-Bred International, A Dupont Company 7250 N.W. 62nd Ave., P.O. Box 552, Johnston, IA o Type of Pesticide: Plant-Incorporated Protectant o Uses: Field Corn o Target Pest(s): Corn Rootworm II. Background EPA has conditionally registered Mycogen Seeds c/o Dow AgroSciences LLC and Pioneer Hi-Bred International’s new active ingredient, Bacillus thuringiensis Cry34Ab1 and Cry35Ab1 proteins and the genetic material necessary for their production (plasmid insert PHP 17662) in Event DAS-59122- 7 corn. The Agency has determined that the use of this pesticide is in the public interest and that it will not cause any unreasonable adverse effects on the environment during the time of conditional registration. The new products are the second PIP to offer protection against corn rootworm (CRW), and they are expected to result in a further reduction of chemical insecticide use by growers. The reduced chemical pesticide use will benefit the environment directly and can mean less exposure to people who apply chemical pesticides to corn.