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4 results on '"Finamore,Emiliana"'

1. Activation of monocytic cells by immunostimulatory lipids conjugated to peptide antigens.

Author

Galdiero S, Vitiello M, Finamore E, Mansi R, Galdiero M, Morelli G, and Tesauro D

Subjects
Animals, Antigens, Bacterial chemistry, Antigens, Bacterial immunology, Calcium-Calmodulin-Dependent Protein Kinases antagonists & inhibitors, Cell Line, Tumor, Cytokines biosynthesis, Cytokines immunology, Enzyme Inhibitors pharmacology, Epitopes, B-Lymphocyte immunology, Epitopes, T-Lymphocyte immunology, Flavonoids pharmacology, Herpesvirus 1, Human immunology, Humans, Imidazoles pharmacology, Lipid Metabolism, Macrophage Activation, Mice, Mitogen-Activated Protein Kinases antagonists & inhibitors, Mitogen-Activated Protein Kinases immunology, Peptides metabolism, Peptides pharmacology, Pyridines pharmacology, Viral Envelope Proteins immunology, Viral Envelope Proteins metabolism, Immunization, Lipids immunology, Macrophages immunology, Monocytes immunology, Peptides immunology
Abstract

Bacterial derived lipoproteins constitute potent macrophage activators in vivo and are effective stimuli, enhancing the immune response especially with respect to low or non-immunogenic compounds. In the present study we have prepared branched lipopeptide constructs in which different (B- and T-cell) epitopes of Herpes simplex virus type 1, derived from glycoproteins B (gB) and D (gD), are linked to a synthetic lipid core. The ability of the lipid core peptide (LCP) constructs (LCP-gB and LCP-gD) to induce cytokine expression and activate the mitogen-activated protein kinase cascade has been evaluated and compared with the behaviour of the isolated epitopes and the lipid core. In this respect, the use of LCP technology coupled with the use of three different gB or gD peptide epitopes in the same branched constructs could represent an interesting approach in order to obtain efficient delivery systems in the development of a synthetic multiepitopic vaccine for the prevention of viral infections.

Published
2012
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2. Haemophilus influenzae porin induces Toll-like receptor 2-mediated cytokine production in human monocytes and mouse macrophages.

Author

Galdiero M, Galdiero M, Finamore E, Rossano F, Gambuzza M, Catania MR, Teti G, Midiri A, and Mancuso G

Subjects
Adaptor Proteins, Signal Transducing, Animals, Antibodies, Monoclonal immunology, Antigens, Differentiation physiology, Cell Line, Humans, Interleukin-6 biosynthesis, Interleukin-8 biosynthesis, Lipopolysaccharide Receptors physiology, Mice, Myeloid Differentiation Factor 88, Receptors, Immunologic physiology, Toll-Like Receptor 2, Toll-Like Receptor 4, Toll-Like Receptors, Tumor Necrosis Factor-alpha biosynthesis, Cytokines biosynthesis, Haemophilus influenzae physiology, Macrophages immunology, Membrane Glycoproteins physiology, Monocytes immunology, Porins physiology, Receptors, Cell Surface physiology
Abstract

The production of proinflammatory cytokines is likely to play a major pathophysiological role in meningitis and other infections caused by Haemophilus influenzae type b (Hib). Previous studies have shown that Hib porin contributes to signaling of the inflammatory cascade. We examined here the role of Toll-like receptors (TLRs) and the TLR-associated adaptor protein MyD88 in Hib porin-induced production of tumor necrosis factor alpha (TNF-alpha) and interleukin-6 (IL-6). Hib porin-induced TNF-alpha and IL-6 production was virtually eliminated in macrophages from TLR2- or MyD88-deficient mice. In contrast, macrophages from lipopolysaccharide (LPS)-hyporesponsive C3H/HeJ mice, which are defective in TLR4 function, responded normally to Hib porin. Moreover anti-TLR2 antibodies but not anti-TLR4 antibodies significantly reduced Hib porin-stimulated TNF-alpha and IL-6 release from the human monocytic cell line THP-1. These data indicate that the TLR2/MyD88 pathway plays an essential role in Hib porin-mediated cytokine production. These findings may be useful in the development of alternative therapies aimed at reducing excessive inflammatory responses during Hib infections.

Published
2004
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3. Activation of monocytic cells by immunostimulatory lipids conjugated to peptide antigens

Author

Mariateresa Vitiello, Emiliana Finamore, Marilena Galdiero, Rosalba Mansi, Diego Tesauro, Stefania Galdiero, Giancarlo Morelli, Galdiero, Stefania, Vitiello, Mariateresa, Finamore, Emiliana, Mansi, Rosalba, Galdiero, Marilena, Morelli, Giancarlo, Tesauro, Diego, Vitiello, M., Finamore, E., Mansi, R., and Galdiero, M.

Subjects
Pyridines, Macrophage, Pyridine, Epitopes, T-Lymphocyte, Peptide, Herpesvirus 1, Human, medicine.disease_cause, Mitogen-Activated Protein Kinase, Monocyte, Monocytes, Epitope, chemistry.chemical_compound, Mice, Viral Envelope Proteins, Enzyme Inhibitor, Enzyme Inhibitors, chemistry.chemical_classification, Imidazoles, Lipopeptide, Viral Envelope Protein, Lipid, Lipids, Biochemistry, Cytokines, Epitopes, B-Lymphocyte, Mitogen-Activated Protein Kinases, Biotechnology, Human, Calcium-Calmodulin-Dependent Protein Kinase, Biology, antigen, Immune system, Antigen, In vivo, Cell Line, Tumor, medicine, Animals, Humans, Molecular Biology, Cytokine, Imidazole, Flavonoids, Antigens, Bacterial, Animal, Macrophages, Macrophage Activation, Lipid Metabolism, Herpes simplex virus, chemistry, Calcium-Calmodulin-Dependent Protein Kinases, Flavonoid, Immunization, Peptides, Glycoprotein
Abstract

Bacterial derived lipoproteins constitute potent macrophage activators in vivo and are effective stimuli, enhancing the immune response especially with respect to low or non-immunogenic compounds. In the present study we have prepared branched lipopeptide constructs in which different (B- and T-cell) epitopes of Herpes simplex virus type 1, derived from glycoproteins B (gB) and D (gD), are linked to a synthetic lipid core. The ability of the lipid core peptide (LCP) constructs (LCP-gB and LCP-gD) to induce cytokine expression and activate the mitogen-activated protein kinase cascade has been evaluated and compared with the behaviour of the isolated epitopes and the lipid core. In this respect, the use of LCP technology coupled with the use of three different gB or gD peptide epitopes in the same branched constructs could represent an interesting approach in order to obtain efficient delivery systems in the development of a synthetic multiepitopic vaccine for the prevention of viral infections.

Published
2012

4. Viral fusion peptides induce several signal transduction pathway activations that are essential for interleukin-10 and beta-interferon production

Author

Marilena Galdiero, Katia Raieta, Francesco Galdiero, Emiliana Finamore, Stefania Galdiero, Mariateresa Vitiello, Marco Cantisani, Carlo Pedone, Annarita Falanga, Vitiello, M, Finamore, E, Falanga, A, Raieta, K, Cantisani, M, Galdiero, F, Pedone, C, Galdiero, Marilena, Galdiero, S., Vitiello, Mariateresa, Finamore, Emiliana, Falanga, Annarita, Raieta, Katia, Cantisani, Marco, Galdiero, Francesco, Pedone, Carlo, and Galdiero, Stefania

Subjects
Transcriptional Activation, Blotting, Western, Enzyme-Linked Immunosorbent Assay, Biology, Monocyte, Monocytes, Cell Line, Intracellular signaling pathways, Virology, Humans, Immunoprecipitation, Beta (finance), Viral Fusion Protein, Original Paper, Fusion, Interferon-beta, Interleukin-10, Cell biology, Host-Pathogen Interaction, Interleukin 10, Interferon production, Infectious Diseases, Hes3 signaling axis, Host-Pathogen Interactions, Viral peptides-transduction pathways, Signal transduction, Viral Fusion Proteins, Human, Signal Transduction
Abstract

Objectives: The deciphering of intracellular signaling pathways that are activated by the interaction between viral fusion peptides and cellular membranes are important for the understanding of both viral replication strategies and host defense mechanisms. Methods: Fusion peptides of several enveloped viruses belonging to different virus families were prepared by standard 9-fluorenylmethoxycarbonyl polyamine solid-phase synthesis and used to stimulate U937 cells in vitro to analyze the phosphorylation patterns of the signaling pathways (PKC, Src, Akt, and MAPK pathways). Immunoprecipitation and Western blotting were carried out by using phosphospecific antibodies. All samples were also assayed for the presence of IL-10 and IFN-β by ELISA and activation of nuclear factors (AP-1 and NF-ĸB). Results: We have demonstrated that hydrophobic domains of fusion proteins are able to induce several transduction pathways that lead to cytokine (IFN-β and IL-10) production, an event that appears to be dependent on early activation of AP-1 and NF-ĸB. Conclusions: The results obtained on the signaling activity of fusion peptides from different viruses enabled us to shed some light on the complex mechanism of viral entry and more precisely we focused on the exact signaling event induced by hydrophobic domains characteristic of fusion peptides interacting with the cell membrane.

Published
2010

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