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Serial femtosecond crystallography on in vivo-grown crystals drives elucidation of mosquitocidal Cyt1Aa bioactivation cascade

Author

Listed:
  • Guillaume Tetreau

    (Univ. Grenoble Alpes, CNRS, CEA, Institut de Biologie Structurale)

  • Anne-Sophie Banneville

    (Univ. Grenoble Alpes, CNRS, CEA, Institut de Biologie Structurale)

  • Elena A. Andreeva

    (Univ. Grenoble Alpes, CNRS, CEA, Institut de Biologie Structurale)

  • Aaron S. Brewster

    (Lawrence Berkeley National Laboratory)

  • Mark S. Hunter

    (Linac Coherent Light Source, SLAC National Accelerator Laboratory)

  • Raymond G. Sierra

    (Linac Coherent Light Source, SLAC National Accelerator Laboratory)

  • Jean-Marie Teulon

    (Univ. Grenoble Alpes, CNRS, CEA, Institut de Biologie Structurale)

  • Iris D. Young

    (Lawrence Berkeley National Laboratory)

  • Niamh Burke

    (Univ. Grenoble Alpes, CNRS, CEA, Institut de Biologie Structurale)

  • Tilman A. Grünewald

    (European Synchrotron Radiation Facility (ESRF), BP 220)

  • Joël Beaudouin

    (Univ. Grenoble Alpes, CNRS, CEA, Institut de Biologie Structurale)

  • Irina Snigireva

    (European Synchrotron Radiation Facility (ESRF), BP 220)

  • Maria Teresa Fernandez-Luna

    (University of California
    Baylor University, One Bear place 97388)

  • Alister Burt

    (Univ. Grenoble Alpes, CNRS, CEA, Institut de Biologie Structurale)

  • Hyun-Woo Park

    (University of California
    California Baptist University)

  • Luca Signor

    (Univ. Grenoble Alpes, CNRS, CEA, Institut de Biologie Structurale)

  • Jayesh A. Bafna

    (Jacobs University)

  • Rabia Sadir

    (Univ. Grenoble Alpes, CNRS, CEA, Institut de Biologie Structurale)

  • Daphna Fenel

    (Univ. Grenoble Alpes, CNRS, CEA, Institut de Biologie Structurale)

  • Elisabetta Boeri-Erba

    (Univ. Grenoble Alpes, CNRS, CEA, Institut de Biologie Structurale)

  • Maria Bacia

    (Univ. Grenoble Alpes, CNRS, CEA, Institut de Biologie Structurale)

  • Ninon Zala

    (Univ. Grenoble Alpes, CNRS, CEA, Institut de Biologie Structurale)

  • Frédéric Laporte

    (Univ. Grenoble Alpes, CNRS, LECA)

  • Laurence Després

    (Univ. Grenoble Alpes, CNRS, LECA)

  • Martin Weik

    (Univ. Grenoble Alpes, CNRS, CEA, Institut de Biologie Structurale)

  • Sébastien Boutet

    (Linac Coherent Light Source, SLAC National Accelerator Laboratory)

  • Martin Rosenthal

    (European Synchrotron Radiation Facility (ESRF), BP 220)

  • Nicolas Coquelle

    (Large-Scale Structures Group, Institut Laue-Langevin)

  • Manfred Burghammer

    (European Synchrotron Radiation Facility (ESRF), BP 220)

  • Duilio Cascio

    (University of California)

  • Michael R. Sawaya

    (University of California)

  • Mathias Winterhalter

    (Univ. Grenoble Alpes, CNRS, LECA)

  • Enrico Gratton

    (The Henry Samueli School of Engineering, University of California)

  • Irina Gutsche

    (Univ. Grenoble Alpes, CNRS, CEA, Institut de Biologie Structurale)

  • Brian Federici

    (University of California)

  • Jean-Luc Pellequer

    (Univ. Grenoble Alpes, CNRS, CEA, Institut de Biologie Structurale)

  • Nicholas K. Sauter

    (Lawrence Berkeley National Laboratory)

  • Jacques-Philippe Colletier

    (Univ. Grenoble Alpes, CNRS, CEA, Institut de Biologie Structurale)

Abstract

Cyt1Aa is the one of four crystalline protoxins produced by mosquitocidal bacterium Bacillus thuringiensis israelensis (Bti) that has been shown to delay the evolution of insect resistance in the field. Limiting our understanding of Bti efficacy and the path to improved toxicity and spectrum has been ignorance of how Cyt1Aa crystallizes in vivo and of its mechanism of toxicity. Here, we use serial femtosecond crystallography to determine the Cyt1Aa protoxin structure from sub-micron-sized crystals produced in Bti. Structures determined under various pH/redox conditions illuminate the role played by previously uncharacterized disulfide-bridge and domain-swapped interfaces from crystal formation in Bti to dissolution in the larval mosquito midgut. Biochemical, toxicological and biophysical methods enable the deconvolution of key steps in the Cyt1Aa bioactivation cascade. We additionally show that the size, shape, production yield, pH sensitivity and toxicity of Cyt1Aa crystals grown in Bti can be controlled by single atom substitution.

Suggested Citation

  • Guillaume Tetreau & Anne-Sophie Banneville & Elena A. Andreeva & Aaron S. Brewster & Mark S. Hunter & Raymond G. Sierra & Jean-Marie Teulon & Iris D. Young & Niamh Burke & Tilman A. Grünewald & Joël B, 2020. "Serial femtosecond crystallography on in vivo-grown crystals drives elucidation of mosquitocidal Cyt1Aa bioactivation cascade," Nature Communications, Nature, vol. 11(1), pages 1-16, December.
    • Handle: RePEc:nat:natcom:v:11:y:2020:i:1:d:10.1038_s41467-020-14894-w
    DOI: 10.1038/s41467-020-14894-w
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    Cited by:

    1. Guillaume Tetreau & Michael R. Sawaya & Elke Zitter & Elena A. Andreeva & Anne-Sophie Banneville & Natalie A. Schibrowsky & Nicolas Coquelle & Aaron S. Brewster & Marie Luise Grünbein & Gabriela Nass , 2022. "De novo determination of mosquitocidal Cry11Aa and Cry11Ba structures from naturally-occurring nanocrystals," Nature Communications, Nature, vol. 13(1), pages 1-18, December.
    2. Izumi Ishigami & Raymond G. Sierra & Zhen Su & Ariana Peck & Cong Wang & Frederic Poitevin & Stella Lisova & Brandon Hayes & Frank R. Moss & Sébastien Boutet & Robert E. Sublett & Chun Hong Yoon & Syu, 2023. "Structural insights into functional properties of the oxidized form of cytochrome c oxidase," Nature Communications, Nature, vol. 14(1), pages 1-10, December.

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