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Heterologous Expression of 3-O-Deacylase in Acinetobacter Baumannii Modulates the Endotoxicity of Lipopolysaccharide Publisher Pubmed



Badmasti F1 ; Shahcheraghi F1 ; Siadat SD1 ; Bouzari S2 ; Ajdary S3 ; Amin M5 ; Halabian R4 ; Imani Fooladi AA4
Authors
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Authors Affiliations
  1. 1. Department of Bacteriology, Pasteur Institute of Iran, Tehran University of Medical Sciences, Tehran, Iran
  2. 2. Department of Molecular Biology, Pasteur Institute of Iran, Tehran University of Medical Sciences, Tehran, Iran
  3. 3. Department of Immunology, Pasteur Institute of Iran, Tehran University of Medical Sciences, Tehran, Iran
  4. 4. Applied Microbiology Research Center, Baqiyatallah University of Medical Sciences, Tehran University of Medical Sciences, Tehran, Iran
  5. 5. Department of Drug and Food Control, Faculty of Pharmacy, Tehran University of Medical Sciences, Tehran, Iran

Source: Journal of Molecular Microbiology and Biotechnology Published:2015


Abstract

The lipopolysaccharide (LPS) of Acinetobacter baumannii is a potent stimulator of proinflammatory cytokines, such as interleukin-6 (IL-6). The 3-O-deacylase (PagL)-modifying enzyme that removes the 3-O-linked acyl chain from the disaccharide backbone of lipid A provides the opportunity to develop a new therapeutic compound that could reduce detrimental inflammatory responses. The plasmid pMMB66EH-PagL obtained by recombinant DNA technology was electroporated into A. baumannii ATCC 19606. Compared with wild-type LPS, outer membrane vesicles and inactivated whole cells of engineered bacteria had a statistically significant decreased ability to produce IL-6. Structural analysis of lipid A by negative-ion matrix-assisted laser desorption/ionization time-of-ight mass spectrometry revealed that the profile of lipid A fractions under PagL expression was changed. Taken together, our data showed that recombinant penta-acylated lipid A had less immunoreactivity and that the tetra-acylated version of lipid A with TLR4 antagonist activity decreased the induction of IL-6 production in the murine macrophage cell line J774 A.1. © 2015 S. Karger AG, Basel.
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