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Asymmetric peptidoglycan editing generates cell curvature in Bdellovibrio predatory bacteria

Author

Listed:
  • Emma J. Banks

    (University of Nottingham, Queen’s Medical Centre)

  • Mauricio Valdivia-Delgado

    (Institute for Microbiology and Infection, School of Biosciences, University of Birmingham)

  • Jacob Biboy

    (Biosciences Institute, Newcastle University)

  • Amber Wilson

    (Institute for Microbiology and Infection, School of Biosciences, University of Birmingham)

  • Ian T. Cadby

    (Institute for Microbiology and Infection, School of Biosciences, University of Birmingham
    University of Bristol)

  • Waldemar Vollmer

    (Biosciences Institute, Newcastle University)

  • Carey Lambert

    (University of Nottingham, Queen’s Medical Centre)

  • Andrew L. Lovering

    (Institute for Microbiology and Infection, School of Biosciences, University of Birmingham)

  • R. Elizabeth Sockett

    (University of Nottingham, Queen’s Medical Centre)

Abstract

Peptidoglycan hydrolases contribute to the generation of helical cell shape in Campylobacter and Helicobacter bacteria, while cytoskeletal or periskeletal proteins determine the curved, vibrioid cell shape of Caulobacter and Vibrio. Here, we identify a peptidoglycan hydrolase in the vibrioid-shaped predatory bacterium Bdellovibrio bacteriovorus which invades and replicates within the periplasm of Gram-negative prey bacteria. The protein, Bd1075, generates cell curvature in B. bacteriovorus by exerting LD-carboxypeptidase activity upon the predator cell wall as it grows inside spherical prey. Bd1075 localizes to the outer convex face of B. bacteriovorus; this asymmetric localization requires a nuclear transport factor 2-like (NTF2) domain at the protein C-terminus. We solve the crystal structure of Bd1075, which is monomeric with key differences to other LD-carboxypeptidases. Rod-shaped Δbd1075 mutants invade prey more slowly than curved wild-type predators and stretch invaded prey from within. We therefore propose that the vibrioid shape of B. bacteriovorus contributes to predatory fitness.

Suggested Citation

  • Emma J. Banks & Mauricio Valdivia-Delgado & Jacob Biboy & Amber Wilson & Ian T. Cadby & Waldemar Vollmer & Carey Lambert & Andrew L. Lovering & R. Elizabeth Sockett, 2022. "Asymmetric peptidoglycan editing generates cell curvature in Bdellovibrio predatory bacteria," Nature Communications, Nature, vol. 13(1), pages 1-15, December.
  • Handle: RePEc:nat:natcom:v:13:y:2022:i:1:d:10.1038_s41467-022-29007-y
    DOI: 10.1038/s41467-022-29007-y
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    References listed on IDEAS

    as
    1. Pavol Skubák & Navraj S. Pannu, 2013. "Automatic protein structure solution from weak X-ray data," Nature Communications, Nature, vol. 4(1), pages 1-6, December.
    2. Bill Söderström & Alexander Badrutdinov & Helena Chan & Ulf Skoglund, 2018. "Cell shape-independent FtsZ dynamics in synthetically remodeled bacterial cells," Nature Communications, Nature, vol. 9(1), pages 1-10, December.
    3. Kyungjin Min & Doo Ri An & Hye-Jin Yoon & Neha Rana & Ji Su Park & Jinshil Kim & Mijoon Lee & Dusan Hesek & Sangryeol Ryu & B. Moon Kim & Shahriar Mobashery & Se Won Suh & Hyung Ho Lee, 2020. "Peptidoglycan reshaping by a noncanonical peptidase for helical cell shape in Campylobacter jejuni," Nature Communications, Nature, vol. 11(1), pages 1-11, December.
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    Cited by:

    1. Jess Tyson & Paul Radford & Carey Lambert & Rob Till & Simona G. Huwiler & Andrew L. Lovering & R. Elizabeth Sockett, 2024. "Prey killing without invasion by Bdellovibrio bacteriovorus defective for a MIDAS-family adhesin," Nature Communications, Nature, vol. 15(1), pages 1-11, December.
    2. Sebastian Pöhl & Giacomo Giacomelli & Fabian M. Meyer & Volker Kleeberg & Eli J. Cohen & Jacob Biboy & Julia Rosum & Timo Glatter & Waldemar Vollmer & Muriel C. F. Teeseling & Johann Heider & Marc Bra, 2024. "An outer membrane porin-lipoprotein complex modulates elongasome movement to establish cell curvature in Rhodospirillum rubrum," Nature Communications, Nature, vol. 15(1), pages 1-21, December.

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