De novo determination of mosquitocidal Cry11Aa and Cry11Ba structures from naturally-occurring nanocrystals

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 Kovacs, Mark S. Hunter, Marco Kloos, Raymond G. Sierra, Giorgio Schiro, Pei Qiao, Myriam Stricker, Dennis Bideshi, Iris D. Young, Ninon Zala, Sylvain Engilberge, Alexander Gorel, Luca Signor, Jean-Marie Teulon, Mario Hilpert, Lutz Foucar, Johan Bielecki, Richard Bean, Raphael Wijn, Tokushi Sato, Henry Kirkwood, Romain Letrun, Alexander Batyuk, Irina Snigireva, Daphna Fenel, Robin Schubert, Ethan J. Canfield, Mario M. Alba, Frédéric Laporte, Laurence Després, Maria Bacia, Amandine Roux, Christian Chapelle, François Riobé, Olivier Maury, Wai Li Ling, Sébastien Boutet, Adrian Mancuso, Irina Gutsche, Eric Girard, Thomas R. M. Barends, Jean-Luc Pellequer, Hyun-Woo Park, Arthur D. Laganowsky, Jose Rodriguez, Manfred Burghammer, Robert L. Shoeman, R. Bruce Doak, Martin Weik, Nicholas K. Sauter, Brian Federici, Duilio Cascio, Ilme Schlichting and Jacques-Philippe Colletier ()
Additional contact information
Guillaume Tetreau: Univ. Grenoble Alpes, CNRS, CEA, Institut de Biologie Structurale
Michael R. Sawaya: University of California
Elke Zitter: Univ. Grenoble Alpes, CNRS, CEA, Institut de Biologie Structurale
Elena A. Andreeva: Univ. Grenoble Alpes, CNRS, CEA, Institut de Biologie Structurale
Anne-Sophie Banneville: Univ. Grenoble Alpes, CNRS, CEA, Institut de Biologie Structurale
Natalie A. Schibrowsky: University of California
Nicolas Coquelle: Institut Laue-Langevin
Aaron S. Brewster: Lawrence Berkeley National Laboratory
Marie Luise Grünbein: Max-Planck-Institut für medizinische Forschung
Gabriela Nass Kovacs: Max-Planck-Institut für medizinische Forschung
Mark S. Hunter: SLAC National Accelerator Laboratory
Marco Kloos: Max-Planck-Institut für medizinische Forschung
Raymond G. Sierra: SLAC National Accelerator Laboratory
Giorgio Schiro: Univ. Grenoble Alpes, CNRS, CEA, Institut de Biologie Structurale
Pei Qiao: Texas A&M University
Myriam Stricker: Max-Planck-Institut für medizinische Forschung
Dennis Bideshi: University of California
Iris D. Young: Lawrence Berkeley National Laboratory
Ninon Zala: Univ. Grenoble Alpes, CNRS, CEA, Institut de Biologie Structurale
Sylvain Engilberge: Univ. Grenoble Alpes, CNRS, CEA, Institut de Biologie Structurale
Alexander Gorel: Max-Planck-Institut für medizinische Forschung
Luca Signor: Univ. Grenoble Alpes, CNRS, CEA, Institut de Biologie Structurale
Jean-Marie Teulon: Univ. Grenoble Alpes, CNRS, CEA, Institut de Biologie Structurale
Mario Hilpert: Max-Planck-Institut für medizinische Forschung
Lutz Foucar: Max-Planck-Institut für medizinische Forschung
Johan Bielecki: European XFEL GmbH
Richard Bean: European XFEL GmbH
Raphael Wijn: European XFEL GmbH
Tokushi Sato: European XFEL GmbH
Henry Kirkwood: European XFEL GmbH
Romain Letrun: European XFEL GmbH
Alexander Batyuk: SLAC National Accelerator Laboratory
Irina Snigireva: European Synchrotron Radiation Facility (ESRF), BP 220
Daphna Fenel: Univ. Grenoble Alpes, CNRS, CEA, Institut de Biologie Structurale
Robin Schubert: European XFEL GmbH
Ethan J. Canfield: University of Southern California
Mario M. Alba: University of Southern California
Frédéric Laporte: Univ. Grenoble Alpes, CNRS, LECA
Laurence Després: Univ. Grenoble Alpes, CNRS, LECA
Maria Bacia: Univ. Grenoble Alpes, CNRS, CEA, Institut de Biologie Structurale
Amandine Roux: Université Claude Bernard Lyon 1, Laboratoire de Chimie
Christian Chapelle: Polyvalan SARL
François Riobé: Université Claude Bernard Lyon 1, Laboratoire de Chimie
Olivier Maury: Université Claude Bernard Lyon 1, Laboratoire de Chimie
Wai Li Ling: Univ. Grenoble Alpes, CNRS, CEA, Institut de Biologie Structurale
Sébastien Boutet: SLAC National Accelerator Laboratory
Adrian Mancuso: European XFEL GmbH
Irina Gutsche: Univ. Grenoble Alpes, CNRS, CEA, Institut de Biologie Structurale
Eric Girard: Univ. Grenoble Alpes, CNRS, CEA, Institut de Biologie Structurale
Thomas R. M. Barends: Max-Planck-Institut für medizinische Forschung
Jean-Luc Pellequer: Univ. Grenoble Alpes, CNRS, CEA, Institut de Biologie Structurale
Hyun-Woo Park: University of California
Arthur D. Laganowsky: Texas A&M University
Jose Rodriguez: University of California
Manfred Burghammer: European Synchrotron Radiation Facility (ESRF), BP 220
Robert L. Shoeman: Max-Planck-Institut für medizinische Forschung
R. Bruce Doak: Max-Planck-Institut für medizinische Forschung
Martin Weik: Univ. Grenoble Alpes, CNRS, CEA, Institut de Biologie Structurale
Nicholas K. Sauter: Lawrence Berkeley National Laboratory
Brian Federici: University of California
Duilio Cascio: University of California
Ilme Schlichting: Max-Planck-Institut für medizinische Forschung
Jacques-Philippe Colletier: Univ. Grenoble Alpes, CNRS, CEA, Institut de Biologie Structurale

Nature Communications, 2022, vol. 13, issue 1, 1-18

Abstract: Abstract Cry11Aa and Cry11Ba are the two most potent toxins produced by mosquitocidal Bacillus thuringiensis subsp. israelensis and jegathesan, respectively. The toxins naturally crystallize within the host; however, the crystals are too small for structure determination at synchrotron sources. Therefore, we applied serial femtosecond crystallography at X-ray free electron lasers to in vivo-grown nanocrystals of these toxins. The structure of Cry11Aa was determined de novo using the single-wavelength anomalous dispersion method, which in turn enabled the determination of the Cry11Ba structure by molecular replacement. The two structures reveal a new pattern for in vivo crystallization of Cry toxins, whereby each of their three domains packs with a symmetrically identical domain, and a cleavable crystal packing motif is located within the protoxin rather than at the termini. The diversity of in vivo crystallization patterns suggests explanations for their varied levels of toxicity and rational approaches to improve these toxins for mosquito control.

Date: 2022
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DOI: 10.1038/s41467-022-31746-x

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