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Contributo in rivista
Tipo: Articolo in rivista
Titolo: Proteomic analysis of human U937 cell line activation mediated by Haemophilus influenzae type b P2 porin and its surface-exposed loop 7
Anno di pubblicazione: 2010
Autori: Severino V, Chambery A, Vitiello M, Cantisani M, Galdiero S, Galdiero M, Malorni L, Di Maro A, Parente A.
Affiliazioni autori: Department of Life Science, Second University of Naples, Via Vivaldi 43, I-81100 Caserta, Italy, Department of Experimental Medicine, Second University of Naples, Via De Crecchio 7, I-80138 Napoli, Italy, Department of Biological Sciences, University of Naples "Federico II", Via Mezzocannone 16, I-80134, Napoli, Italy, Institute of Biostructure and Bioimaging, C.N.R., Via Mezzocannone 16, I-80134, Napoli, Italy, and Proteomic and Biomolecular Mass Spectrometry Center, Institute of Food Science and Technology, C.N.R., Via Roma 52 A-C, I-83100 Avellino, Italy.
Abstract: The virulence of Haemophilus influenzae type b (Hib) has been attributed to a variety of potential factors associated with its cell surface, including lipopolysaccharides (LPS) and major outer membrane proteins (OMPs). P2 porin, one of the best-characterized porins in terms of its functional characteristics, is the most abundant OMP in Hib and has also been shown to possess proinflammatory activity. To characterize the role played by bacterial surface components in disease onset and development, the proteomic profiling of human U937 cell line activated by H. influenzae type b P2 porin and its most active surface-exposed loop (L7) was performed by means of two-dimensional electrophoresis and mass spectrometry. The study provided a list of candidate proteins with potential relevance in the host immune and inflammatory response. Most of the differentially expressed proteins are involved in metabolic processes, remodelling of cytoskeleton, stress response and signal transduction pathways. The results constitute the basis for dissecting signal transduction cascades activated by P2 stimulation and gain insights into the molecular events involved in the modulation of pathogen-host cell interactions.
Pagine da: 1050
Pagine a: 1062
Journal of proteome research
American Chemical Society,
Numero volume: 9
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