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Peptidoglycan remodeling enables E. coli to survive severe outer membrane assembly defect

Lookup NU author(s): Dr Jacob Biboy, Dr Christian Otten, Matthias Winkle, Lisa Atkinson, Dr Hamish Yau, Professor Waldemar Vollmer

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This work is licensed under a Creative Commons Attribution 4.0 International License (CC BY 4.0).


Abstract

Gram-negative bacteria have a tripartite cell envelope with the cytoplasmic membrane (CM), a stress-bearing peptidoglycan (PG) layer, and the asymmetric outer membrane (OM) containing lipopolysaccharide (LPS) in the outer leaflet. Cells must tightly coordinate the growth of their complex envelope to maintain cellular integrity and OM permeability barrier function. The biogenesis of PG and LPS relies on specialized macromolecular complexes that span the entire envelope. In this work, we show that Escherichia coli cells are capable of avoiding lysis when the transport of LPS to the OM is compromised, by utilizing LD-transpeptidases (LDTs) to generate 3-3 cross-links in the PG. This PG remodeling program relies mainly on the activities of the stress response LDT, LdtD, together with the major PG synthase PBP1B, its cognate activator LpoB, and the carboxypeptidase PBP6a. Our data support a model according to which these proteins cooperate to strengthen the PG in response to defective OM synthesis.


Publication metadata

Author(s): Morè N, Martorana AM, Biboy J, Otten C, Winkle M, Gurnani Serrano CK, Silva AM, Atkinson L, Yau H, Breukink E, den Blaauwen T, Vollmer W, Polissi A

Publication type: Article

Publication status: Published

Journal: mBio

Year: 2019

Volume: 10

Issue: 1

Pages: e02729-18

Print publication date: 01/01/2019

Online publication date: 05/02/2019

Acceptance date: 13/12/2018

Date deposited: 16/12/2018

ISSN (electronic): 2150-7511

Publisher: American Society for Microbiology

URL: https://doi.org/10.1128/mBio.02729-18

DOI: 10.1128/mBio.02729-18


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