Asymmetric peptidoglycan editing generates cell curvature in Bdellovibrio predatory bacteria

Banks, Emma J.; Valdivia-Delgado, Mauricio; Biboy, Jacob; Wilson, Amber; Cadby, Ian T.; Vollmer, Waldemar; Lambert, Carey; Lovering, Andrew L.; Sockett, R. Elizabeth

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.

Citation

Banks, E. J., Valdivia-Delgado, M., Biboy, J., Wilson, A., Cadby, I. T., Vollmer, W., Lambert, C., Lovering, A. L., & Sockett, R. E. (2022). Asymmetric peptidoglycan editing generates cell curvature in Bdellovibrio predatory bacteria. Nature Communications, 13(1), Article 1509. https://doi.org/10.1038/s41467-022-29007-y

• Journal Article Type: Article
• Acceptance Date: Feb 22, 2022
• Online Publication Date: Mar 21, 2022
• Publication Date: Mar 21, 2022
• Deposit Date: Feb 14, 2022
• Publicly Available Date: Mar 22, 2022
• Journal: Nature Communications
• Electronic ISSN: 2041-1723
• Publisher: Nature Publishing Group
• Peer Reviewed: Peer Reviewed
• Volume: 13
• Issue: 1
• Article Number: 1509
• DOI: https://doi.org/10.1038/s41467-022-29007-y
• Keywords: General Physics and Astronomy; General Biochemistry, Genetics and Molecular Biology; General Chemistry
• Public URL: https://nottingham-repository.worktribe.com/output/7466387
• Publisher URL: https://www.nature.com/articles/s41467-022-29007-ymmetric