A functional msbb acyltransferase of Photorhabdus luminescens, required for secondary lipid a acylation in gram-negative bacteria, confers resistance to anti-microbial peptides
Joint Authors
Abi Khattar, Z.
Gaudriault, S.
Givaudan, A.
Source
Issue
Vol. 17, Issue 1 (30 Jun. 2016), pp.45-56, 12 p.
Publisher
National Council for Scientific Research
Publication Date
2016-06-30
Country of Publication
Lebanon
No. of Pages
12
Main Subjects
Abstract EN
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.
American Psychological Association (APA)
Abi Khattar, Z.& Gaudriault, S.& Givaudan, A.. 2016. 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،Vol. 17, no. 1, pp.45-56.
https://search.emarefa.net/detail/BIM-763242
Modern Language Association (MLA)
Abi Khattar, Z.…[et al.]. 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 Vol. 17, no. 1 (2016), pp.45-56.
https://search.emarefa.net/detail/BIM-763242
American Medical Association (AMA)
Abi Khattar, Z.& Gaudriault, S.& Givaudan, A.. 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. 2016. Vol. 17, no. 1, pp.45-56.
https://search.emarefa.net/detail/BIM-763242
Data Type
Journal Articles
Language
English
Notes
Includes bibliographical references : p. 54-56
Record ID
BIM-763242