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PreprintCited by 28Enzyme Structure and FunctionInsect Resistance and GeneticsEntomopathogenic Microorganisms in Pest Control

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

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Tetreau, Guillaume, Sawaya, Michael R., De Zitter, Elke, Andreeva, Elena A., Banneville, Anne-Sophie, Schibrowsky, Natalie, Coquelle, Nicolas, Brewster, Aaron S., Grünbein, Marie Luise, Kovacs, Gabriela Nass, Hunter, Mark S., Kloos, Marco, Sierra, Raymond G., Schiro, Giorgio, Qiao, Pei, Stricker, Myriam, Bideshi, Dennis, Young, Iris D., Zala, Ninon, Engilberge, Sylvain, Gorel, Alexander, Signor, Luca, Teulon, Jean-Marie, Hilpert, Mario, Foucar, Lutz, Bielecki, Johan, Bean, Richard, de Wijn, Raphael, Sato, Tokushi, Kirkwood, Henry, Letrun, Romain, Batyuk, Alexander, Snigireva, Irina, Fenel, Daphna, Schubert, Robin, Canfield, Ethan J., Alba, Mario M., Laporte, Frédéric, Després, Laurence, Bacia, Maria, Roux, Amandine, Chapelle, Christian, Riobé, François, Maury, Olivier, Ling, Wai Li, Boutet, Sébastien, Mancuso, Adrian, Gutsche, Irina, Girard, Eric, Barends, Thomas R. M., Pellequer, Jean-Luc, Park, Hyun-Woo, Laganowsky, Arthur D., Rodriguez, Jose, Burghammer, Manfred, Shoeman, Robert L., Doak, R. Bruce, Weik, Martin, Sauter, Nicholas K., Federici, Brian, Cascio, Duilio, Schlichting, Ilme, Colletier, Jacques-Philippe·2021·Nature Communications
DOI 10.1101/2021.12.15.472578PMC PMC9334358

Preprint — published as 10.1038/s41467-022-31746-x · Paper page

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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.

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Metadata

Authors
Tetreau, G., Sawaya, M. R., De Zitter, E., Andreeva, E. A., Banneville, A.-S., Schibrowsky, N., Coquelle, N., Brewster, A. S., Grünbein, M. L., Kovacs, G. N., Hunter, M. S., Kloos, M., Sierra, R. G., Schiro, G., Qiao, P., Stricker, M., Bideshi, D., Young, I. D., Zala, N., Engilberge, S., Gorel, A., Signor, L., Teulon, J.-M., Hilpert, M., Foucar, L., Bielecki, J., Bean, R., de Wijn, R., Sato, T., Kirkwood, H., Letrun, R., Batyuk, A., Snigireva, I., Fenel, D., Schubert, R., Canfield, E. J., Alba, M. M., Laporte, F., Després, L., Bacia, M., Roux, A., Chapelle, C., Riobé, F., Maury, O., Ling, W. L., Boutet, S., Mancuso, A., Gutsche, I., Girard, E., Barends, T. R. M., Pellequer, J.-L., Park, H.-W., Laganowsky, A. D., Rodriguez, J., Burghammer, M., Shoeman, R. L., Doak, R. B., Weik, M., Sauter, N. K., Federici, B., Cascio, D., Schlichting, I., & Colletier, J.-P.
Affiliations
  • Centre National de la Recherche Scientifique (FR)
  • University of California, Los Angeles (US)
  • Institut Laue-Langevin (FR)
  • Lawrence Berkeley National Laboratory (US)
  • Max Planck Institute for Medical Research (DE)
  • SLAC National Accelerator Laboratory (US)
  • Texas A&M University (US)
  • University of California, Riverside (US)
  • European X-Ray Free-Electron Laser (DE)
  • European Synchrotron Radiation Facility (FR)
  • University of Southern California (US)
  • Lyon 1 Université (FR)
Corresponding author
Colletier, Jacques-Philippe
ORCID
Venue
Nature Communications
Publisher
openRxiv
Published
2021-12-16
Volume
13
Issue
1
Pages
4376-4376
ISSN
2041-1723 (ISSN-L)
DOI
10.1101/2021.12.15.472578
PMC
PMC9334358
OpenAlex
W4288096555
Cited by
28
References
1
Citations by year
2026: 4 · 2025: 6 · 2024: 8 · 2023: 9 · 2022: 1
FWCI
1.68
Type
journal article
Language
en
Open access
Licence
cc-by
Locations
  • Nature Communications (publishedVersion, cc-by)
  • bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion)
  • PubMed Central (publishedVersion, cc-by)
  • PubMed (publishedVersion)
  • eScholarship (California Digital Library) (submittedVersion)
  • HAL (submittedVersion, other-oa)
  • HAL (submittedVersion, cc-by-nc)
  • RePEc: Research Papers in Economics (submittedVersion)
  • DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
  • OSTI OAI (U.S. Department of Energy Office of Scientific and Technical Information) (submittedVersion)
  • MPG.PuRe (Max Planck Society) (submittedVersion)
  • European XFEL (submittedVersion)
Funders
  • U.S. Department of Energy (76SF00515, DE–AC02–76SF00515, P41GM103393, AC02‐76SF00515, DE-AC02-)
  • U.S. Department of Health and Human Services (P41RR001209, P41GM103393, 1U01CK000516, GM117126)
  • Infrastructures en Biologie Santé et Agronomie (ANR-17-EURE-0003, ANR-10-INBS-05-02)
  • Agence Nationale de la Recherche (UAR 3518 CNRS-CEA-UGA-EMBL, ANR-17-EURE-0003, ANR-10-INBS-05-02, ANR-10- INBS-05, ANR-17-EURE-, ANR-2018CE11-0005-02, ANR-17-CE11-0018, ANR-15-CE32-0004, DE-AC02-76SF00515, ANR-17, ANR-10, UMS 3518 CNRS-CEA-UGA-EMBL)
  • Centre National de la Recherche Scientifique (DE-AC02-76SF00515, ANR‐10‐INBS‐05‐02, UMS 3518 CNRS‐CEA‐UGA‐EMBL, ANR‐17‐EURE‐0003, UAR 3518 CNRS-CEA-UGA-EMBL)
  • Région Auvergne-Rhône-Alpes (ANR-17-EURE-0003, ANR-10-INBS-05-02)
  • French Infrastructure for Integrated Structural Biology (UAR 3518 CNRS-CEA-UGA-EMBL, ANR-17-EURE-0003, ANR-10-INBS-05–02, UMS 3518, ANR-10-INBS-0.5, UMS 3518 CNRS-CEA-UGA-EMBL, ANR-10-INBS)
  • National Institutes of Health (1U01CK000516, DE-AC02-76SF00515)
  • Centers for Disease Control and Prevention (1U01CK000516, U01CK000516)
  • Office of Science (AC02-76SF00515, P41GM103393, DE-AC02-76SF0051 5, DE-AC02, 76SF00515)
  • National Institute of General Medical Sciences (R01GM117126, T32GM007185, P41GM103393)
  • National Center for Research Resources (P41RR001209)
  • Basic Energy Sciences (DE-AC02, P41GM103393, 76SF00515, AC02-76SF00515, DE-AC-02-76SF00515)
  • SLAC National Accelerator Laboratory (DEAC02−76SF00515, AC02‐76SF00515, P41GM103393)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Enzyme Structure and Function
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Insect Resistance and Genetics
  • Life Sciences › Agricultural and Biological Sciences › Insect Science › Entomopathogenic Microorganisms in Pest Control
Keywords
Cry11Aa, mosquitocidal toxin, Bacillus thuringiensis var. israelensis, nanocrystals, serial femtosecond crystallography, de novo structure determination, single-wavelength anomalous dispersion, protoxin, mosquito control, toxin toxicity
MeSH terms
Animals, Bacillus thuringiensis, Bacterial Proteins, Endotoxins, Hemolysin Proteins, Larva, Mosquito Control, Nanoparticles

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