Accéder directement au contenu Accéder directement à la navigation
Article dans une revue

A functional msbB acyltransferase of Photorhabdus luminescens, required for secondary lipid a acylation in gram-negative bacteria, confers resistance to anti-microbial peptides

Abstract : Lipid A is a potent endotoxin, and its fatty acids (lauric, myristic, and sometimes palmitic acid) anchors lipopolysaccharide (LPS) into the outer leaflet of the outer membrane of most Gram-negative bacteria. The highly anionic charge of the glucosamine lipid A moiety makes the LPS a powerful attractant for cationic antimicrobial peptides (AMPs). AMPs are major component of innate immunity that kill bacteria by permeabilization of lipid bilayers. Secondary lipid A acylation of Klebsiella pneumoniae, involving the acyltransferase LpxM (formally, msbB or WaaN) that acylates (KDO)2-(lauroyl)-lipid IV-A with myristate during lipid A biosynthesis, has been associated with bacterial resistance to AMPs contributing to virulence in animal models. We investigated here the role of the msbB gene of the entomopathogenic bacterium Photorhabdus luminescens in AMP resistance, by functional complementation of the AMP susceptible K. pneumoniae lpxM mutant with the P. luminescens msbB gene. We showed that msbB (lpxM) gene of P. luminescens is able to enhance polymyxin B, colistin and cecropin A resistance of K. pneumoniae lpxM mutant, compared to the non-complemented mutant. However, we could not obtain any msbB mutant of Photorhabdus by performing allelic exchange experiments based on positive selection of sucrose highly resistant mutants. We thus suggest that msbB-mediated Photorhabdus lipid A acylation is essential for outer membrane low-permeability and that modification of lipid A composition, fluidity and osmosis-resistance have an important role in the ability of Photorhabdus to grow in sucrose at high concentrations.
Type de document :
Article dans une revue
Liste complète des métadonnées

Littérature citée [40 références]  Voir  Masquer  Télécharger

https://hal.archives-ouvertes.fr/hal-01512210
Déposant : Archive Ouverte Prodinra <>
Soumis le : vendredi 21 avril 2017 - 21:40:03
Dernière modification le : mardi 2 février 2021 - 11:26:03
Archivage à long terme le : : samedi 22 juillet 2017 - 15:32:29

Fichier

Abi Khattar 2016 Lebanese Scie...
Accord explicite pour ce dépôt

Identifiants

  • HAL Id : hal-01512210, version 1
  • PRODINRA : 368282

Collections

Citation

Z. Abi Khattar, Sophie Gaudriault, Alain Givaudan. A functional msbB acyltransferase of Photorhabdus luminescens, required for secondary lipid a acylation in gram-negative bacteria, confers resistance to anti-microbial peptides. Lebanese Science Journal, National Council for Scientific Research in Lebanon, 2016, 17 (1), pp.45-56. ⟨hal-01512210⟩

Partager

Métriques

Consultations de la notice

850

Téléchargements de fichiers

377