Bacillus Genetic Stock Center Catalog of Strains Seventh Edition Volume 2
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APPENDIX H – Bibliography of ECOTOX Open Literature
APPENDIX H – Bibliography of ECOTOX Open Literature Refresh from 2012 Accepted by ECOTOX and OPP Reference List 1. Abbott, J. D.; Bruton, B. D., and Patterson, C. L. Fungicidal Inhibition of Pollen Germination and Germ-Tube Elongation in Muskmelon. REPSOIL,ENV; 1991; 26, (5): 529-530. Notes: EcoReference No.: 63745 Chemical of Concern: BMY,CTN,CuOH,MZB 2. Abney, M. R.; Ruberson, J. R.; Herzog, G. A.; Kring, T. J.; Steinkraus, D. C., and Roberts, P. M. Rise and Fall of Cotton Aphid (Hemiptera: Aphididae) Populations in Southeastern Cotton Production Systems. GRO,POP. Department of Entomology, North Carolina State University, Raleigh, NC, USA. [email protected]//: SOIL,ENV; 2008; 101, (1): 23-35. Notes: EcoReference No.: 156197 Chemical of Concern: AZX,CTN,IMC 3. Al-Dosari, S. A.; Cranshaw, W. S., and Schweissing, F. C. Effects on Control of Onion Thrips from Co- Application of Onion Pesticides. POPENV; 1996; 21, (1): 49-54. Notes: EcoReference No.: 90255 Chemical of Concern: CTN,CYP,CuOH,LCYT,MLX,MMM,Maneb 4. Arts, G. H. P.; Belgers, J. D. M.; Hoekzema, C. H., and Thissen, J. T. N. M. Sensitivity of Submersed Freshwater Macrophytes and Endpoints in Laboratory Toxicity Tests. GROAQUA; 2008; 153, (1): 199-206. Notes: EcoReference No.: 108008 Chemical of Concern: ASM,CTN,FNZ,PCP 5. Aziz, T.; Habte, M., and Yuen, J. E. Inhibition of Mycorrhizal Symbiosis in Leucaena leucocephala by Chlorothalonil. BCM,GRO,POPSOIL,ENV; 1991; 131, (1): 47-52. Notes: EcoReference No.: 92163 Chemical of Concern: CTN 6. Babu, T. H. Effectiveness of Certain Chemicals and Fungicides on the Feeding Behaviour of House Sparrows. -
The Structure/Function of New Insecticidal Proteins and Regulatory Challenges for Commercialization
This is an Open Access document downloaded from ORCA, Cardiff University's institutional repository: http://orca.cf.ac.uk/100278/ This is the author’s version of a work that was submitted to / accepted for publication. Citation for final published version: Moar, William, Berry, Colin and Narva, Kenneth 2017. The structure/function of new insecticidal proteins and regulatory challenges for commercialization. Journal of Invertebrate Pathology 142 , pp. 1-4. 10.1016/j.jip.2017.02.001 file Publishers page: https://doi.org/10.1016/j.jip.2017.02.001 <https://doi.org/10.1016/j.jip.2017.02.001> Please note: Changes made as a result of publishing processes such as copy-editing, formatting and page numbers may not be reflected in this version. For the definitive version of this publication, please refer to the published source. You are advised to consult the publisher’s version if you wish to cite this paper. This version is being made available in accordance with publisher policies. See http://orca.cf.ac.uk/policies.html for usage policies. Copyright and moral rights for publications made available in ORCA are retained by the copyright holders. The structure/function of new insecticidal proteins and regulatory challenges for commercialization William Moar, Colin Berry and Kenneth Narva Genetically modified crops produced by biotechnology methods have provided grower benefits since 1995 including improved protection of crop yield, reduced input costs, and a reduced reliance on chemical pesticides (Klumper and Qaim, 2014). These benefits have driven annual increases in worldwide adoption of GM crops, with the largest number of hectares being grown in the Americas (ISAAA 2014). -
English-Persian
English-Persian English-Persian A abrachia (= abrachiatism) ﺑﯽ دﺳﺘﯽ ﻣﺎدرزاد abrachiatism ﺑﯽ ﺳﺮو دﺳﺘﯽ ﻣﺎدر زاد abrachiocephalia ﺁ. (A (= adenine ﺑﯽ ﺳﺮ و دﺳﺖ ﻣﺎدر زاد abrachiocephalus ﺁ. (A (= adenovirus ﺑﯽ دﺳﺖ ﻣﺎدر زاد abrachius زﻧﺠﻴﺮﻩ ﺁ. A chain اﺑﺮﯾﻦ abrin دﯼ.ان.اﯼ ﻧﻮع ﺁ. A form DNA اﺑﺴﻴﺰﯾﮏ اﺳﻴﺪ abscisic acid ﺁ.ﯾﮏ، اﯼ.وان. A I (= first meiotic ﭘﻴﮑﺮ anaphase) absolute configuration ﺑﻨﺪﯼ/ﮐﻨﻔﻴﮕﻮراﺳﻴﻮن/ﺁراﯾ ﺁ.دو، اﯼ.ﺗﻮ. A II (= second meiotic ش ﻣﻄﻠﻖ (anaphase ﺟﺬب ﮐﻨﻨﺪﮔﯽ، absorbance ﺟﺎﯾﮕﺎﻩ اﯼ.،ﭘﯽ. A,P site درﺁﺷﺎﻣﻨﺪﮔﯽ، اﺁ (aa (amino acid درﮐﺸﻴﺪﮔﯽ، ﻗﺎﺑﻠﻴﺖ ﺟﺬب اﯼ.اﯼ.ﺟﯽ. AAG (= acid ﺟﺬب، ﺟﺬب ﺳﻄﺤﯽ، alpha-glucosidase) absorption درﺁﺷﺎﻣﯽ، درﮐﺸﯽ، درون اﯼ.اﯼ.ﺗﯽ. (AAT (= alpha-antitrypsin ﺟﺬﺑﯽ اﯼ.اﯼ.وﯼ. AAV (= adeno-associated ﺁﺑﺰﯾﻢ، اﺑﺰاﯾﻢ virus) abzyme ﺁ.ث.، اﯼ.ﺳﯽ. (AC (= adenyl cyclase اﯼ.ﺑﯽ. (ab (= antibody ﺧﺎر ﺳﺮﮎ acanthella ﭘﻴﺸﺒﻴﻨﯽ ژن اب اﯾﻨﻴﺘﻴﻮ ab initio gene prediction ﺧﺎر ﺳﺮان acanthocephala اﻧﺘﻘﺎل دهﻨﺪﻩ اﯼ.ﺑﯽ.ﺳﯽ. ABC transporter =) acanthocephalan ﺟﻮرﻩ/وارﯾﺘﻪ/رﻗﻢ/ﺳﻮﯾﻪ Abelson strain of murine (acanthocephalus (ﻣﺮﺑﻮط ﺑﻪ ﺟﻮﻧﺪﮔﺎن) ﺧﺎر ﺳﺮ acanthocephalus ﺁﺑﻠﺴﻮﻧﯽ ﺧﺎر ﺳﺮﭼﻪ acanthor ﮐﺞ راهﯽ aberration ﺑﯽ ﻗﻠﺒﯽ ﻣﺎدر زاد acardia ﺗﻮﻟﻴﺪ ﺧﻮد ﺑﺨﻮد، ﺗﻮﻟﻴﺪ ﻣﺜﻞ abiogenesis ﺑﯽ ﻗﻠﺐ ﻣﺎدر زاد acardiac ﺧﻮد ﺑﻪ ﺧﻮدﯼ، ﻧﺎزﯾﺴﺖ (acardiacus (=acardiac زاﯾﯽ (acardius (=acardiac ﻏﻴﺮ ﺁﻟﯽ، ﻏﻴﺮ زﻧﺪﻩ، ﻧﺎزﯾﻮا abiotic ﮐﻨﻪ زدﮔﯽ acariasis ﺗﻨﺶ ﻋﻮاﻣﻞ ﻓﻴﺰﯾﮑﯽ ﻣﺤﻴﻂ، abiotic stress ﮐﻨﻪ ﺳﺎﻧﺎن acarina ﺗﻨﺶ اﺑﻴﻮﺗﻴﮏ ﮐﻨﻪ ﺳﺎن acarine اﯼ.ﺑﯽ.ال abl (=Abelson strain of ﮐﻨﻪ زدﮔﯽ (murine) acarinosis (= acariasis ﮐﻨﻪ زدﮔﯽ ﭘﻮﺳﺖ acarodermatitis اﯼ.ﺑﯽ.ال. ABL (=Abelson strain of ﮐﻨﻪ ﺗﺮﺳﯽ murine) acarophobia ﺑﻠﻮغ ﺷﺘﺎﺑﺪار/ﺗﺴﺮﯾﻊ ﺷﺪﻩ accelerated maturation ﻓﺮﺳﺎب، ﺳﺎﯾﺶ، ذوب ﯾﺦ ablation ﮔﻠﻮﺑﻮﻟﻴﻦ ﺷﺘﺎﺑﺪهﻨﺪﻩ/ﺗﺴﺮﯾﻊ accelerator globulin اﯼ.ﺑﯽ.او. -
How Bacillus Thuringiensishas
Review TRENDS in Genetics Vol.17 No.4 April 2001 193 How Bacillus thuringiensis has evolved specific toxins to colonize the insect world Ruud A. de Maagd, Alejandra Bravo and Neil Crickmore Bacillus thuringiensis is a bacterium of great agronomic and scientific interest. between different strains has been observed both in a Together the subspecies of this bacterium colonize and kill a large variety of soil environment and within insects2. host insects and even nematodes, but each strain does so with a high degree of Individual Cry toxins have a defined spectrum of specificity. This is mainly determined by the arsenal of crystal proteins that the insecticidal activity, usually restricted to a few bacterium produces during sporulation. Here we describe the properties of species within one particular order of insects. To date, these toxin proteins and the current knowledge of the basis for their specificity. toxins for insect species in the orders Lepidoptera Assessment of phylogenetic relationships of the three domains of the active (butterflies and moths), Diptera (flies and toxin and experimental results indicate how sequence divergence in mosquitoes), Coleoptera (beetles and weevils) and combination with domain swapping by homologous recombination might Hymenoptera (wasps and bees) have been identified. have caused this extensive range of specificities. A small minority of crystal toxins shows activity against non-insect species such as nematodes3. A few Bacillus thuringiensis (Bt) is an endospore-forming toxins have an activity spectrum that spans two or bacterium characterized by the presence of a protein three insect orders – most notably Cry1Ba, which is crystal within the cytoplasm of the sporulating cell active against larvae of moths, flies and beetles4. -
Role of Toxin Activation on Binding and Pore Formation Activity of the Bacillus Thuringiensis Cry3 Toxins in Membranes of Leptinotarsa Decemlineata (Say)
Biochimica et Biophysica Acta 1660 (2004) 99–105 www.bba-direct.com Role of toxin activation on binding and pore formation activity of the Bacillus thuringiensis Cry3 toxins in membranes of Leptinotarsa decemlineata (Say) C. Rausella,1, I. Garcı´a-Roblesb,1,J.Sa´ncheza, C. Mun˜oz-Garaya, A.C. Martı´nez-Ramı´rezb, M.D. Realb, A. Bravoa,* a Instituto de Biotecnologı´a, Universidad Nacional Auto´noma de Me´xico, Ap. Postal 510-3, Cuernavaca 62250, Morelos, Mexico b Facultad de Ciencias Biolo´gicas, Universidad de Valencia, Dr. Moliner 50, Burjassot 46100, Valencia, Spain Received 29 July 2003; received in revised form 5 November 2003; accepted 7 November 2003 Abstract Binding and pore formation constitute key steps in the mode of action of Bacillus thuringiensis y-endotoxins. In this work, we present a comparative analysis of toxin-binding capacities of proteolytically processed Cry3A, Cry3B and Cry3C toxins to brush border membranes (BBMV) of the Colorado potato beetle Leptinotarsa decemlineata (CPB), a major potato coleopteran-insect pest. Competition experiments showed that the three Cry3 proteolytically activated toxins share a common binding site. Also heterologous competition experiments showed that Cry3Aa and Cry3Ca toxins have an extra binding site that is not shared with Cry3Ba toxin. The pore formation activity of the three different Cry3 toxins is analysed. High pore-formation activities were observed in Cry3 toxins obtained by proteolytical activation with CPB BBMV in contrast to toxins activated with either trypsin or chymotrypsin proteases. The pore-formation activity correlated with the formation of soluble oligomeric structures. Our data support that, similarly to the Cry1A toxins, the Cry3 oligomer is formed after receptor binding and before membrane insertion, forming a pre-pore structure that is insertion-competent. -
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. -
Bt Toxin Modification for Enhanced Efficacy
Toxins 2014, 6, 3005-3027; doi:10.3390/toxins6103005 OPEN ACCESS toxins ISSN 2072-6651 www.mdpi.com/journal/toxins Review Bt Toxin Modification for Enhanced Efficacy Benjamin R. Deist 1, Michael A. Rausch 1, Maria Teresa Fernandez-Luna 1, Michael J. Adang 2,3 and Bryony C. Bonning 1,* 1 Department of Entomology, Iowa State University, Ames, IA 50011, USA; E-Mails: [email protected] (B.R.D.); [email protected] (M.A.R.); [email protected] (M.T.F.-L.) 2 Departments of Entomology, University of Georgia, Athens, GA 30602, USA; E-Mail: [email protected] 3 Department of Biochemistry and Molecular Biology, University of Georgia, Athens, GA 30602, USA * Author to whom correspondence should be addressed; E-Mail: [email protected]; Tel.: +1-515-294-1989; Fax: +1-515-294-2995. External Editor: Anne-Brit Kolstø Received: 2 May 2014; in revised form: 28 September 2014 / Accepted: 29 September 2014 / Published: 22 October 2014 Abstract: Insect-specific toxins derived from Bacillus thuringiensis (Bt) provide a valuable resource for pest suppression. Here we review the different strategies that have been employed to enhance toxicity against specific target species including those that have evolved resistance to Bt, or to modify the host range of Bt crystal (Cry) and cytolytic (Cyt) toxins. These strategies include toxin truncation, modification of protease cleavage sites, domain swapping, site-directed mutagenesis, peptide addition, and phage display screens for mutated toxins with enhanced activity. Toxin optimization provides a useful approach to extend the utility of these proteins for suppression of pests that exhibit low susceptibility to native Bt toxins, and to overcome field resistance. -
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 -
Evolução Do Veneno Em Cnidários Baseada Em Dados De Genomas E Proteomas
Adrian Jose Jaimes Becerra Evolução do veneno em cnidários baseada em dados de genomas e proteomas Venom evolution in cnidarians based on genomes and proteomes data São Paulo 2015 i Adrian Jose Jaimes Becerra Evolução do veneno em cnidários baseada em dados de genomas e proteomas Venom evolution in cnidarians based on genomes and proteomes data Dissertação apresentada ao Instituto de Biociências da Universidade de São Paulo, para a obtenção de Título de Mestre em Ciências, na Área de Zoologia. Orientador: Prof. Dr. Antonio C. Marques São Paulo 2015 ii Jaimes-Becerra, Adrian J. Evolução do veneno em cnidários baseada em dados de genomas e proteomas. 103 + VI páginas Dissertação (Mestrado) - Instituto de Biociências da Universidade de São Paulo. Departamento de Zoologia. 1. Veneno; 2. Evolução; 3. Proteoma. 4. Genoma I. Universidade de São Paulo. Instituto de Biociências. Departamento de Zoologia. Comissão Julgadora Prof(a) Dr(a) Prof(a) Dr(a) Prof. Dr. Antonio Carlos Marques iii Agradecimentos Eu gostaria de agradecer ao meu orientador Antonio C. Marques, pela confiança desde o primeiro dia e pela ajuda tanto pessoal como profissional durantes os dois anos de mestrado. Obrigado por todo. Ao CAPES, pela bolsa de mestrado concedida. Ao FAPESP pelo apoio financeiro durante minha estadia em Londres. Ao Instituto de Biociências da Universidade de São Paulo, pela estrutura oferecida durante a execução desde estudo. Ao Dr. Paul F. Long pelas conversas, por toda sua ajuda, por acreditar no meu trabalho. Aos colegas e amigos de Laboratório de Evolução Marinha (LEM), Jimena Garcia, María Mendoza, Thaís Miranda, Amanda Cunha, Karla Paresque, Marina Fernández, Fernanda Miyamura e Lucília Miranda, pela amizade, dicas e ajuda em tudo e por me fazer sentir em casa, muito obrigado mesmo! Aos meus amigos fora do laboratório, John, Soly, Chucho, Camila, Faride, Cesar, Angela, Camilo, Isa, Nathalia, Susana e Steffania, pelo apoio e por me fazer sentir em casa. -
The First Cry2ac-Type Protein Toxic to Helicoverpa Armigera: Cloning and Overexpression of Cry2ac7 Gene from SBS-BT1 Strain of Bacillus Thuringiensis
toxins Article The First Cry2Ac-Type Protein Toxic to Helicoverpa armigera: Cloning and Overexpression of Cry2ac7 Gene from SBS-BT1 Strain of Bacillus thuringiensis Faiza Saleem 1,2 and Abdul Rauf Shakoori 1,* 1 School of Biological Sciences, University of the Punjab, Quaid-i-Azam Campus, Lahore 54590, Pakistan; [email protected] 2 Department of Biotechnology, Lahore College for Women University, Lahore 54590, Pakistan * Correspondence: [email protected] or [email protected] Academic Editor: Anne-Brit Kolstø Received: 26 August 2017; Accepted: 27 October 2017; Published: 3 November 2017 Abstract: The Cry (crystal) proteins from Bacillus thuringiensis are known to have toxicity against a variety of insects and have been exploited to control insect pests through transgenic plants and biopesticides. B. thuringiensis SBS BT-1 carrying the cry2 genes was isolated from soil samples in Pakistan. The 2-kb full length cry2Ac gene was cloned, sequenced, and submitted to the EMBL DNA database (Accession No. AM292031). For expression analysis, Escherichia coli DH5α was transformed with the fragment sub-cloned in pET22b expression vector using NdeI and HindIII restriction sites, and later confirmed by restriction endonuclease analysis. To assess the toxicity of Cry2Ac7 protein against lepidopteran and dipteran insects, BL21 (codon plus) strain of E. coli was further transformed with the recombinant plasmid. The 65-kDa protein was expressed in the form of inclusion bodies up to 180 OD units per liter of the medium. Inclusions were washed with a buffer containing 1.5% Triton-X 100 and >90% pure Cry2Ac7 was obtained. The inclusion bodies were dissolved in 50 mM K2CO3 (pH 11.5), dialyzed, and freeze-dried. -
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.