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β-Barrel proteins tether the outer membrane in many Gram-negative bacteria
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Journal Article
β-Barrel proteins tether the outer membrane in many Gram-negative bacteria
2021
Overview
Gram-negative bacteria have a cell envelope that comprises an outer membrane (OM), a peptidoglycan (PG) layer and an inner membrane (IM)
1
. The OM and PG are load-bearing, selectively permeable structures that are stabilized by cooperative interactions between IM and OM proteins
2
,
3
. In
Escherichia coli
, Braun’s lipoprotein (Lpp) forms the only covalent tether between the OM and PG and is crucial for cell envelope stability
4
; however, most other Gram-negative bacteria lack Lpp so it has been assumed that alternative mechanisms of OM stabilization are present
5
. We used a glycoproteomic analysis of PG to show that β-barrel OM proteins are covalently attached to PG in several Gram-negative species, including
Coxiella burnetii
,
Agrobacterium tumefaciens
and
Legionella pneumophila
. In
C. burnetii
, we found that four different types of covalent attachments occur between OM proteins and PG, with tethering of the β-barrel OM protein BbpA becoming most abundant in the stationary phase and tethering of the lipoprotein LimB similar throughout the cell cycle. Using a genetic approach, we demonstrate that the cell cycle-dependent tethering of BbpA is partly dependent on a developmentally regulated L,D-transpeptidase (Ldt). We use our findings to propose a model of Gram-negative cell envelope stabilization that includes cell cycle control and an expanded role for Ldts in covalently attaching surface proteins to PG.
β-barrel outer-membrane proteins are covalently attached to peptidoglycan in Gram-negative bacteria including
Coxiella burnetii
,
Agrobacterium tumefaciens
and
Legionella pneumophila
.
Publisher
Nature Publishing Group UK,Nature Publishing Group
Subject
/ 101/58
/ 13/1
/ 38/23
/ 38/39
/ 45/29
/ 45/70
/ 82/80
/ Agrobacterium tumefaciens - metabolism
/ Bacteria
/ Bacterial Outer Membrane Proteins - metabolism
/ Bacterial structural biology
/ Biomedical and Life Sciences
/ Coxiella burnetii - metabolism
/ Escherichia coli - metabolism
/ Legionella pneumophila - metabolism
/ Letter
/ Molecular Dynamics Simulation
/ Peptidyl Transferases - metabolism
/ Protein Binding - physiology
/ Proteins
/ Virology
