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Francisella FlmX broadly affects lipopolysaccharide modification and virulence
Emory Antibiotic Resistance Center, Emory University School of Medicine, GA, Atlanta, United States; Emory Vaccine Center, Emory University School of Medicine, GA, Atlanta, United States; Yerkes National Primate Research Center, Emory University School of Medicine, GA, Atlanta, United States; Division of Infectious Diseases, Department of Medicine, Emory University School of Medicine, GA, Atlanta, United States.
Department of Biochemistry, Duke University School of Medicine, NC, Durham, United States.
Emory Vaccine Center, Emory University School of Medicine, GA, Atlanta, United States; Yerkes National Primate Research Center, Emory University School of Medicine, GA, Atlanta, United States; Division of Infectious Diseases, Department of Medicine, Emory University School of Medicine, GA, Atlanta, United States.
Umeå universitet, Medicinska fakulteten, Molekylär Infektionsmedicin, Sverige (MIMS). Umeå universitet, Medicinska fakulteten, Institutionen för klinisk mikrobiologi, Klinisk bakteriologi.
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2021 (Engelska)Ingår i: Cell Reports, E-ISSN 2211-1247, Vol. 35, nr 11, artikel-id 109247Artikel i tidskrift (Refereegranskat) Published
Abstract [en]

The outer membrane protects Gram-negative bacteria from the host environment. Lipopolysaccharide (LPS), a major outer membrane constituent, has distinct components (lipid A, core, O-antigen) generated by specialized pathways. In this study, we describe the surprising convergence of these pathways through FlmX, an uncharacterized protein in the intracellular pathogen Francisella. FlmX is in the flippase family, which includes proteins that traffic lipid-linked envelope components across membranes. flmX deficiency causes defects in lipid A modification, core remodeling, and O-antigen addition. We find that an F. tularensis mutant lacking flmX is >1,000,000-fold attenuated. Furthermore, FlmX is required to resist the innate antimicrobial LL-37 and the antibiotic polymyxin. Given FlmX's central role in LPS modification and its conservation in intracellular pathogens Brucella, Coxiella, and Legionella, FlmX may represent a novel drug target whose inhibition could cripple bacterial virulence and sensitize bacteria to innate antimicrobials and antibiotics.

Ort, förlag, år, upplaga, sidor
Elsevier, 2021. Vol. 35, nr 11, artikel-id 109247
Nyckelord [en]
cationic antimicrobial peptide, flippase, lipid A, lipopolysaccharide, polymyxin resistance
Nationell ämneskategori
Mikrobiologi inom det medicinska området Medicinsk bioteknologi (med inriktning mot cellbiologi (inklusive stamcellsbiologi), molekylärbiologi, mikrobiologi, biokemi eller biofarmaci)
Identifikatorer
URN: urn:nbn:se:umu:diva-186362DOI: 10.1016/j.celrep.2021.109247ISI: 000661869600009PubMedID: 34133919Scopus ID: 2-s2.0-85107905377OAI: oai:DiVA.org:umu-186362DiVA, id: diva2:1581682
Forskningsfinansiär
NIH (National Institute of Health), AI098800, I01 BX002788Vetenskapsrådet, 2013-4581, 2013-8621Tillgänglig från: 2021-07-23 Skapad: 2021-07-23 Senast uppdaterad: 2024-01-17Bibliografiskt granskad

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Golovliov, IgorSjöstedt, Anders

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Molekylär Infektionsmedicin, Sverige (MIMS)Klinisk bakteriologi
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Cell Reports
Mikrobiologi inom det medicinska områdetMedicinsk bioteknologi (med inriktning mot cellbiologi (inklusive stamcellsbiologi), molekylärbiologi, mikrobiologi, biokemi eller biofarmaci)

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