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Drosophila nicotinic acetylcholine receptor subunits and their native interactions with insecticidal peptide toxins.
Korona, Dagmara; Dirnberger, Benedict; Giachello, Carlo N G; Queiroz, Rayner M L; Popovic, Rebeka; Müller, Karin H; Minde, David-Paul; Deery, Michael J; Johnson, Glynnis; Firth, Lucy C; Earley, Fergus G; Russell, Steven; Lilley, Kathryn S.
Afiliación
  • Korona D; Department of Genetics, University of Cambridge, Downing Street, Cambridge, United Kingdom.
  • Dirnberger B; Department of Genetics, University of Cambridge, Downing Street, Cambridge, United Kingdom.
  • Giachello CNG; Cambridge Centre for Proteomics, Department of Biochemistry, University of Cambridge, Cambridge, United Kingdom.
  • Queiroz RML; Syngenta, Jealott's Hill International Research Centre, Bracknell, United Kingdom.
  • Popovic R; Syngenta, Jealott's Hill International Research Centre, Bracknell, United Kingdom.
  • Müller KH; Cambridge Centre for Proteomics, Department of Biochemistry, University of Cambridge, Cambridge, United Kingdom.
  • Minde DP; MRC Toxicology Unit, Gleeson Building, University of Cambridge, Tennis Court Road, Cambridge, United Kingdom.
  • Deery MJ; Cambridge Advanced Imaging Centre, Department of Physiology, Development and Neuroscience/Anatomy Building, University of Cambridge, Cambridge, United Kingdom.
  • Johnson G; Cambridge Centre for Proteomics, Department of Biochemistry, University of Cambridge, Cambridge, United Kingdom.
  • Firth LC; Cambridge Centre for Proteomics, Department of Biochemistry, University of Cambridge, Cambridge, United Kingdom.
  • Earley FG; Department of Genetics, University of Cambridge, Downing Street, Cambridge, United Kingdom.
  • Russell S; Syngenta, Jealott's Hill International Research Centre, Bracknell, United Kingdom.
  • Lilley KS; Syngenta, Jealott's Hill International Research Centre, Bracknell, United Kingdom.
Elife ; 112022 05 16.
Article en En | MEDLINE | ID: mdl-35575460
Drosophila nicotinic acetylcholine receptors (nAChRs) are ligand-gated ion channels that represent a target for insecticides. Peptide neurotoxins are known to block nAChRs by binding to their target subunits, however, a better understanding of this mechanism is needed for effective insecticide design. To facilitate the analysis of nAChRs we used a CRISPR/Cas9 strategy to generate null alleles for all ten nAChR subunit genes in a common genetic background. We studied interactions of nAChR subunits with peptide neurotoxins by larval injections and styrene maleic acid lipid particles (SMALPs) pull-down assays. For the null alleles, we determined the effects of α-Bungarotoxin (α-Btx) and ω-Hexatoxin-Hv1a (Hv1a) administration, identifying potential receptor subunits implicated in the binding of these toxins. We employed pull-down assays to confirm α-Btx interactions with the Drosophila α5 (Dα5), Dα6, Dα7 subunits. Finally, we report the localisation of fluorescent tagged endogenous Dα6 during Drosophila CNS development. Taken together, this study elucidates native Drosophila nAChR subunit interactions with insecticidal peptide toxins and provides a resource for the in vivo analysis of insect nAChRs.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Receptores Nicotínicos / Insecticidas Límite: Animals Idioma: En Revista: Elife Año: 2022 Tipo del documento: Article País de afiliación: Reino Unido Pais de publicación: Reino Unido
Texto completo
Añadir a Mi BVS
Imprimir
XML
PubMed Links
Buscar en Google

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Receptores Nicotínicos / Insecticidas Límite: Animals Idioma: En Revista: Elife Año: 2022 Tipo del documento: Article País de afiliación: Reino Unido Pais de publicación: Reino Unido