PhoPQ regulates acidic glycerophospholipid content of the
            <i>Salmonella</i>
            Typhimurium outer membrane

Dalebroux, Zachary D.; Matamouros, Susana; Whittington, Dale; Bishop, Russell E.; Miller, Samuel I.

doi:10.1073/pnas.1316901111

Cited by 141 publications

(178 citation statements)

References 41 publications

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“…To prevent damage resulting from surface-exposed PLs in wild-type E. coli cells, several mechanisms destroy or remove these PLs from the outer leaflet. The OM β-barrel protein PagP is a palmitoyltransferase that removes a palmitate from the sn-1 position of a surface-exposed PL and transfers it to lipid A or phosphatidylglycerol (12,13). Another OM β-barrel phospholipase, PldA, removes both sn-1 and sn-2 palmitate moieties from PLs and lyso-PLs (14).…”

mentioning

confidence: 99%

Disruption of lipid homeostasis in the Gram-negative cell envelope activates a novel cell death pathway

Sutterlin

Shi

May

et al. 2016

Proc. Natl. Acad. Sci. U.S.A.

160

197

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Gram-negative bacteria balance synthesis of the outer membrane (OM), cell wall, and cytoplasmic contents during growth via unknown mechanisms. Here, we show that a dominant mutation (designated mlaA*, maintenance of lipid asymmetry) that alters MlaA, a lipoprotein that removes phospholipids from the outer leaflet of the OM of Escherichia coli, increases OM permeability, lipopolysaccharide levels, drug sensitivity, and cell death in stationary phase. Surprisingly, single-cell imaging revealed that death occurs after protracted loss of OM material through vesiculation and blebbing at celldivision sites and compensatory shrinkage of the inner membrane, eventually resulting in rupture and slow leakage of cytoplasmic contents. The death of mlaA* cells was linked to fatty acid depletion and was not affected by membrane depolarization, suggesting that lipids flow from the inner membrane to the OM in an energy-independent manner. Suppressor analysis suggested that the dominant mlaA* mutation activates phospholipase A, resulting in increased levels of lipopolysaccharide and OM vesiculation that ultimately undermine the integrity of the cell envelope by depleting the inner membrane of phospholipids. This novel cell-death pathway suggests that balanced synthesis across both membranes is key to the mechanical integrity of the Gram-negative cell envelope.

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mentioning

confidence: 99%

Disruption of lipid homeostasis in the Gram-negative cell envelope activates a novel cell death pathway

Sutterlin

Shi

May

et al. 2016

Proc. Natl. Acad. Sci. U.S.A.

160

197

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“…In some bacteria like Salmonella, this lipid has also been found in the outer membrane (10,11). Cardiolipin has been described for its predisposition to be organized into clusters (12).…”

mentioning

confidence: 99%

Negatively Charged Lipids as a Potential Target for New Amphiphilic Aminoglycoside Antibiotics

Sautrey¹,

Khoury²,

Santos³

et al. 2016

Journal of Biological Chemistry

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Bacterial membranes are highly organized, containing specific microdomains that facilitate distinct protein and lipid assemblies. Evidence suggests that cardiolipin molecules segregate into such microdomains, probably conferring a negative curvature to the inner plasma membrane during membrane fission upon cell division. 3,6-Dinonyl neamine is an amphiphilic aminoglycoside derivative active against Pseudomonas aeruginosa, including strains resistant to colistin. The mechanisms involved at the molecular level were identified using lipid models (large unilamellar vesicles, giant unilamelllar vesicles, and lipid monolayers) that mimic the inner membrane of P. aeruginosa. The study demonstrated the interaction of 3,6-dinonyl neamine with cardiolipin and phosphatidylglycerol, two negatively charged lipids from inner bacterial membranes. This interaction induced membrane permeabilization and depolarization. Lateral segregation of cardiolipin and membrane hemifusion would be critical for explaining the effects induced on lipid membranes by amphiphilic aminoglycoside antibiotics. The findings contribute to an improved understanding of how amphiphilic aminoglycoside antibiotics that bind to negatively charged lipids like cardiolipin could be promising antibacterial compounds.

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“…Together these changes lead to a reduction of the negative charge of the outer membrane and of the electrostatic interactions with antimicrobial peptides Herrera et al, 2010;Jones et al, 2008a;Lee et al, 2004;Zhou et al, 2001b). 3 Decrease in the fluidity of the outer membrane by the incorporation, catalysed by PagP, of an additional palmitate to lipid A and to phosphatidylglycerol (Bishop et al, 2000;Dalebroux et al, 2014;Guo et al, 1998).…”

Section: Antimicrobial Peptidesmentioning

confidence: 99%

Molecular Mechanisms Used by Salmonella to Evade the Immune System

Bernal-Bayard¹,

Ramos‐Morales²

2018

Current Issues in Molecular Biology

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PhoPQ regulates acidic glycerophospholipid content of the Salmonella Typhimurium outer membrane

Cited by 141 publications

References 41 publications

Disruption of lipid homeostasis in the Gram-negative cell envelope activates a novel cell death pathway

Disruption of lipid homeostasis in the Gram-negative cell envelope activates a novel cell death pathway

Negatively Charged Lipids as a Potential Target for New Amphiphilic Aminoglycoside Antibiotics

Molecular Mechanisms Used by Salmonella to Evade the Immune System

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