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The Deep-Sea Polyextremophile Halobacteroides lacunaris TB21 Rough-Type LPS: Structure and Inhibitory Activity towards Toxic LPS
The structural characterization of the lipopolysaccharide (LPS) from extremophiles has important implications in several biomedical and therapeutic applications. The polyextremophile Gram-negative bacterium Halobacteroides lacunaris TB21, isolated from one of the most extreme habitats on our planet,...
Autores principales: | , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2017
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5532643/ https://www.ncbi.nlm.nih.gov/pubmed/28653982 http://dx.doi.org/10.3390/md15070201 |
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author | Di Lorenzo, Flaviana Palmigiano, Angelo Paciello, Ida Pallach, Mateusz Garozzo, Domenico Bernardini, Maria-Lina La Cono, Violetta Yakimov, Michail M. Molinaro, Antonio Silipo, Alba |
author_facet | Di Lorenzo, Flaviana Palmigiano, Angelo Paciello, Ida Pallach, Mateusz Garozzo, Domenico Bernardini, Maria-Lina La Cono, Violetta Yakimov, Michail M. Molinaro, Antonio Silipo, Alba |
author_sort | Di Lorenzo, Flaviana |
collection | PubMed |
description | The structural characterization of the lipopolysaccharide (LPS) from extremophiles has important implications in several biomedical and therapeutic applications. The polyextremophile Gram-negative bacterium Halobacteroides lacunaris TB21, isolated from one of the most extreme habitats on our planet, the deep-sea hypersaline anoxic basin Thetis, represents a fascinating microorganism to investigate in terms of its LPS component. Here we report the elucidation of the full structure of the R-type LPS isolated from H. lacunaris TB21 that was attained through a multi-technique approach comprising chemical analyses, NMR spectroscopy, and Matrix-Assisted Laser Desorption Ionization (MALDI) mass spectrometry. Furthermore, cellular immunology studies were executed on the pure R-LPS revealing a very interesting effect on human innate immunity as an inhibitor of the toxic Escherichia coli LPS. |
format | Online Article Text |
id | pubmed-5532643 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2017 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-55326432017-08-09 The Deep-Sea Polyextremophile Halobacteroides lacunaris TB21 Rough-Type LPS: Structure and Inhibitory Activity towards Toxic LPS Di Lorenzo, Flaviana Palmigiano, Angelo Paciello, Ida Pallach, Mateusz Garozzo, Domenico Bernardini, Maria-Lina La Cono, Violetta Yakimov, Michail M. Molinaro, Antonio Silipo, Alba Mar Drugs Article The structural characterization of the lipopolysaccharide (LPS) from extremophiles has important implications in several biomedical and therapeutic applications. The polyextremophile Gram-negative bacterium Halobacteroides lacunaris TB21, isolated from one of the most extreme habitats on our planet, the deep-sea hypersaline anoxic basin Thetis, represents a fascinating microorganism to investigate in terms of its LPS component. Here we report the elucidation of the full structure of the R-type LPS isolated from H. lacunaris TB21 that was attained through a multi-technique approach comprising chemical analyses, NMR spectroscopy, and Matrix-Assisted Laser Desorption Ionization (MALDI) mass spectrometry. Furthermore, cellular immunology studies were executed on the pure R-LPS revealing a very interesting effect on human innate immunity as an inhibitor of the toxic Escherichia coli LPS. MDPI 2017-06-27 /pmc/articles/PMC5532643/ /pubmed/28653982 http://dx.doi.org/10.3390/md15070201 Text en © 2017 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Article Di Lorenzo, Flaviana Palmigiano, Angelo Paciello, Ida Pallach, Mateusz Garozzo, Domenico Bernardini, Maria-Lina La Cono, Violetta Yakimov, Michail M. Molinaro, Antonio Silipo, Alba The Deep-Sea Polyextremophile Halobacteroides lacunaris TB21 Rough-Type LPS: Structure and Inhibitory Activity towards Toxic LPS |
title | The Deep-Sea Polyextremophile Halobacteroides
lacunaris TB21 Rough-Type LPS: Structure and Inhibitory Activity towards Toxic LPS |
title_full | The Deep-Sea Polyextremophile Halobacteroides
lacunaris TB21 Rough-Type LPS: Structure and Inhibitory Activity towards Toxic LPS |
title_fullStr | The Deep-Sea Polyextremophile Halobacteroides
lacunaris TB21 Rough-Type LPS: Structure and Inhibitory Activity towards Toxic LPS |
title_full_unstemmed | The Deep-Sea Polyextremophile Halobacteroides
lacunaris TB21 Rough-Type LPS: Structure and Inhibitory Activity towards Toxic LPS |
title_short | The Deep-Sea Polyextremophile Halobacteroides
lacunaris TB21 Rough-Type LPS: Structure and Inhibitory Activity towards Toxic LPS |
title_sort | deep-sea polyextremophile halobacteroides
lacunaris tb21 rough-type lps: structure and inhibitory activity towards toxic lps |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5532643/ https://www.ncbi.nlm.nih.gov/pubmed/28653982 http://dx.doi.org/10.3390/md15070201 |
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