A periplasmic phospholipase that maintains outer membrane lipid asymmetry in


Journal

Proceedings of the National Academy of Sciences of the United States of America
ISSN: 1091-6490
Titre abrégé: Proc Natl Acad Sci U S A
Pays: United States
ID NLM: 7505876

Informations de publication

Date de publication:
25 07 2023
Historique:
pmc-release: 18 01 2024
medline: 21 7 2023
pubmed: 18 7 2023
entrez: 18 7 2023
Statut: ppublish

Résumé

The outer membrane of Gram-negative bacteria is unique in both structure and function. The surface-exposed outer leaflet is composed of lipopolysaccharide, while the inner leaflet is composed of glycerophospholipids. This lipid asymmetry creates mechanical strength, lowers membrane permeability, and is necessary for virulence in many pathogens. Glycerophospholipids that mislocalize to the outer leaflet are removed by the Mla pathway, which consists of the outer membrane channel MlaA, the periplasmic lipid carrier MlaC, and the inner membrane transporter MlaBDEF. The opportunistic pathogen

Identifiants

pubmed: 37463202
doi: 10.1073/pnas.2302546120
pmc: PMC10374164
doi:

Substances chimiques

Membrane Lipids 0
Phospholipases EC 3.1.-
Bacterial Outer Membrane Proteins 0
Glycerophospholipids 0

Types de publication

Journal Article Research Support, N.I.H., Extramural

Langues

eng

Sous-ensembles de citation

IM

Pagination

e2302546120

Subventions

Organisme : NIGMS NIH HHS
ID : R35 GM118024
Pays : United States

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Auteurs

Randi L Guest (RL)

Department of Molecular Biology, Princeton University, Princeton, NJ 08544.

Michael J Lee (MJ)

Department of Molecular Biology, Princeton University, Princeton, NJ 08544.

Wei Wang (W)

Lewis-Sigler Institute for Integrative Genomics, Princeton University, Princeton, NJ 08544.

Thomas J Silhavy (TJ)

Department of Molecular Biology, Princeton University, Princeton, NJ 08544.

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