Role of a fluid-phase PRR in fighting an intracellular pathogen: PTX3 in Shigella infection.

Autor: Valeria Ciancarella, Luigi Lembo-Fazio, Ida Paciello, Anna-Karin Bruno, Sébastien Jaillon, Sara Berardi, Marialuisa Barbagallo, Shiri Meron-Sudai, Dani Cohen, Antonio Molinaro, Giacomo Rossi, Cecilia Garlanda, Maria Lina Bernardini

Publikováno v: PLoS Pathogens, Vol 14, Iss 12, p e1007469 (2018)

Shigella spp. are pathogenic bacteria that cause bacillary dysentery in humans by invading the colonic and rectal mucosa where they induce dramatic inflammation. Here, we have analyzed the role of the soluble PRR Pentraxin 3 (PTX3), a key component o

Externí odkaz: https://doaj.org/article/661b305eb3de4e29a3341dbe3a0dd2ca

Authors need to be prudent when assigning names to microbial isolates

Autor: Mike S. M. Jetten, Juan A. Mondotte, Luigi Lembo Fazio, Erko Stackebrandt

Publikováno v: Antonie van Leeuwenhoek International Journal of General and Molecular Microbiology, 115, 1, pp. 1-5
Archives of Microbiology, 203, 5845-5848
Antonie van Leeuwenhoek International Journal of General and Molecular Microbiology, 115, 1-5
Archives of Microbiology, 203, pp. 5845-5848

Contains fulltext : 240191.pdf (Publisher’s version ) (Closed access)

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3e340444686c1b88d3b3cecb270fc8d0
https://doi.org/10.1007/s10482-021-01675-8

Determination of the structure of the O-antigen and the lipid A from the entomopathogenic bacterium Pseudomonas entomophila lipopolysaccharide along with its immunological properties

Autor: Michelangelo Parrilli, Ida Paciello, Rosa Lanzetta, Domenico Garozzo, Immacolata Speciale, Maria Lina Bernardini, Luisa Sturiale, Luigi Lembo Fazio, Cristina De Castro, Bruno Lemaitre, Antonio Molinaro, Angelo Palmigiano

Publikováno v: Carbohydrate research
412 (2015): 20–27. doi:10.1016/j.carres.2015.04.017
info:cnr-pdr/source/autori:Speciale I.; Paciello I.; Fazio L.L.; Sturiale L.; Palmigiano A.; Lanzetta R.; Parrilli M.; Garozzo D.; Lemaitre B.; Bernardini M.L.; Molinaro A.; De Castro C./titolo:Determination of the structure of the O-antigen and the lipid A from the entomopathogenic bacterium Pseudomonas entomophila lipopolysaccharide along with its immunological properties/doi:10.1016%2Fj.carres.2015.04.017/rivista:Carbohydrate research (Print)/anno:2015/pagina_da:20/pagina_a:27/intervallo_pagine:20–27/volume:412

The structure and the immunology of the lipopolysaccharide (LPS) of Pseudomonas entomophila, an entomopathogenic bacterium isolated from the fruit fly Drosophila melanogaster, was characterized. The O-antigen portion was established and resulted to b

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4aa31f5ffcd5596965aa3ba4d1c2255c
https://pubmed.ncbi.nlm.nih.gov/25996527

Thermophiles as potential source of novel endotoxin antagonists: the full structure and bioactivity of the lipo-oligosaccharide from Thermomonas hydrothermalis

Autor: Luisa Sturiale, Luciana Albuquerque, Flaviana Di Lorenzo, Ida Paciello, Maria Lina Bernardini, Antonio Molinaro, Luigi Lembo Fazio, Milton S. da Costa, Rosa Lanzetta, Domenico Garozzo, Michelangelo Parrilli, Dott. Alba Silipo

Publikováno v: ChemBioChem (Internet) 15 (2014): 2146–2155. doi:10.1002/cbic.201402233
info:cnr-pdr/source/autori:Di Lorenzo F.; Paciello I.; Fazio L.L.; Albuquerque L.; Sturiale L.; da Costa M.S.; Lanzetta R.; Parrilli M.; Garozzo D.; Bernardini M.L.; Silipo D.A.; Molinaro A./titolo:Thermophiles as potential source of novel endotoxin antagonists: The full structure and bioactivity of thelipo-oligosaccharide from thermomonas hydrothermalis/doi:10.1002%2Fcbic.201402233/rivista:ChemBioChem (Internet)/anno:2014/pagina_da:2146/pagina_a:2155/intervallo_pagine:2146–2155/volume:15

Thermomonas hydrothermalis is a Gram-negative thermophilic bacterium that is able to live at 50°C. This ability is attributed to chemical modifications, involving those to bacterial cell-wall components, such as proteins and (glyco)lipids. As the ma

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ffd7d1bf7d57f2cab8932fe37fa344a1
https://pubmed.ncbi.nlm.nih.gov/25171597

Intracellular Shigella remodels its LPS to dampen the innate immune recognition and evade inflammasome activation

Autor: Luisa Sturiale, Gaëlle Noël, Antonio Molinaro, Valeria Ciancarella, Maria Lina Bernardini, Anna Brotcke Zumsteg, Laura Curcurù, Ida Paciello, Alba Silipo, Luigi Lembo-Fazio

Publikováno v: Proceedings of the National Academy of Sciences of the United States of America
Proceedings of the National Academy of Sciences of the United States of America, 2013, 110 (46), pp.E4345-54. ⟨10.1073/pnas.1303641110⟩
Proceedings of the National Academy of Sciences of the United States of America, National Academy of Sciences, 2013, 110 (46), pp.E4345-54. ⟨10.1073/pnas.1303641110⟩
Proceedings of the National Academy of Sciences of the United States of America 110 (2013): E4345–E4354. doi:10.1073/pnas.1303641110
info:cnr-pdr/source/autori:Paciello, I; Silipo, A; Lembo-Fazio, L; Curcuru, L; Zumsteg, A; Noel, G; Ciancarella, V; Sturiale, L; Molinaro, A; Bernardini, ML./titolo:Intracellular Shigella remodels its LPS to dampen the innate immune recognition and evade inflammasome activation/doi:10.1073%2Fpnas.1303641110/rivista:Proceedings of the National Academy of Sciences of the United States of America/anno:2013/pagina_da:E4345/pagina_a:E4354/intervallo_pagine:E4345–E4354/volume:110
Proceedings of the National Academy of Sciences; Vol 110

International audience; LPS is a potent bacterial effector triggering the activation of the innate immune system following binding with the complex CD14, myeloid differentiation protein 2, and Toll-like receptor 4. The LPS of the enteropathogen Shige

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2f4459ea70e0e3b8ca3eacdf8a7498e6
https://hal-riip.archives-ouvertes.fr/pasteur-01044866/document