The Experts below are selected from a list of 326715 Experts worldwide ranked by ideXlab platform
Martin Rottman - One of the best experts on this subject based on the ideXlab platform.
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In-Host Adaptation of Salmonella enterica Serotype Dublin during Prosthetic Hip Joint Infection
Emerging Infectious Diseases, 2018Co-Authors: Faten El Sayed, Guillaume Sapriel, Nizar Fawal, Aurelia Gruber, Thomas Bauer, Beate Heym, Caroline Dupont, Henri-jean Garchon, Jean-louis Gaillard, Martin RottmanAbstract:Genome degradation has been central to the adaptation of Salmonella enterica serotypes to their Hosts throughout evolution. We witnessed the patho-adaptation of a strain of Salmonella Dublin (a cattle-adapted serotype) to a Human Host during the course of a recurrent prosthetic hip joint infection evolving over several years.
Jonpaul S Powers - One of the best experts on this subject based on the ideXlab platform.
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modulation of the tlr mediated inflammatory response by the endogenous Human Host defense peptide ll 37
Journal of Immunology, 2006Co-Authors: Neeloffer Mookherjee, Reza Falsafi, Jelena Pistolic, Kelly L Brown, Dawn M E Bowdish, Silvana Doria, Karsten Hokamp, Fiona M Roche, Gregory H Doho, Jonpaul S PowersAbstract:The sole Human cathelicidin peptide, LL-37, has been demonstrated to protect animals against endotoxemia/sepsis. Low, physiological concentrations of LL-37 ( or =50% in the presence of LL-37, demonstrating that the peptide altered gene expression in part by acting directly on the TLR-to-NF-kappaB pathway. LL-37 almost completely prevented the release of TNF-alpha and other cytokines by Human PBMC following stimulation with LPS and other TLR2/4 and TLR9 agonists, but not with cytokines TNF-alpha or IL-1beta. Biochemical and inhibitor studies were consistent with a model whereby LL-37 modulated the inflammatory response to LPS/endotoxin and other agonists of TLR by a complex mechanism involving multiple points of intervention. We propose that the natural Human Host defense peptide LL-37 plays roles in the delicate balancing of inflammatory responses in homeostasis as well as in combating sepsis induced by certain TLR agonists.
Robert E W Hancock - One of the best experts on this subject based on the ideXlab platform.
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Human Host defense peptide ll 37 prevents bacterial biofilm formation
Infection and Immunity, 2008Co-Authors: Joerg Overhage, Andrea Campisano, Manjeet Bains, Ellen C W Torfs, Bernd H A Rehm, Robert E W HancockAbstract:The ability to form biofilms is a critical factor in chronic infections by Pseudomonas aeruginosa and has made this bacterium a model organism with respect to biofilm formation. This study describes a new, previously unrecognized role for the Human cationic Host defense peptide LL-37. In addition to its key role in modulating the innate immune response and weak antimicrobial activity, LL-37 potently inhibited the formation of bacterial biofilms in vitro. This occurred at the very low and physiologically meaningful concentration of 0.5 μg/ml, far below that required to kill or inhibit growth (MIC = 64 μg/ml). LL-37 also affected existing, pregrown P. aeruginosa biofilms. Similar results were obtained using the bovine neutrophil peptide indolicidin, but no inhibitory effect on biofilm formation was detected using subinhibitory concentrations of the mouse peptide CRAMP, which shares 67% identity with LL-37, polymyxin B, or the bovine bactenecin homolog Bac2A. Using microarrays and follow-up studies, we were able to demonstrate that LL-37 affected biofilm formation by decreasing the attachment of bacterial cells, stimulating twitching motility, and influencing two major quorum sensing systems (Las and Rhl), leading to the downregulation of genes essential for biofilm development.
Neeloffer Mookherjee - One of the best experts on this subject based on the ideXlab platform.
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Intracellular Receptor for Human Host Defense Peptide LL-37 in Monocytes
Journal of immunology (Baltimore Md. : 1950), 2009Co-Authors: Neeloffer Mookherjee, Dustin N D Lippert, Pamela Hamill, Reza Falsafi, Anastasia Nijnik, Jason Kindrachuk, Jelena Pistolic, Jennifer L. Gardy, Pegah Miri, Misbah NaseerAbstract:The Human cationic Host defense peptide LL-37 has a broad range of immunomodulatory, anti-infective functions. A synthetic innate defense regulator peptide, innate defense regulator 1 (IDR-1), based conceptually on LL-37, was recently shown to selectively modulate innate immunity to protect against a wide range of bacterial infections. Using advanced proteomic techniques, ELISA, and Western blotting procedures, GAPDH was identified as a direct binding partner for LL-37 in monocytes. Enzyme kinetics and mobility shift studies also indicated LL-37 and IDR-1 binding to GAPDH. The functional relevance of GAPDH in peptide-induced responses was demonstrated by using gene silencing of GAPDH with small interfering RNA (siRNA). Previous studies have established that the induction of chemokines and the anti-inflammatory cytokine IL-10 are critical immunomodulatory functions in the anti-infective properties of LL-37 and IDR-1, and these functions are modulated by the MAPK p38 pathway. Consistent with that, this study demonstrated the importance of the GAPDH interactions with these peptides since gene silencing of GAPDH resulted in impaired p38 MAPK signaling, downstream chemokine and cytokine transcriptional responses induced by LL-37 and IDR-1, and LL-37-induced cytokine production. Bioinformatic analysis, using InnateDB, of the major interacting partners of GAPDH indicated the likelihood that this protein can impact on innate immune pathways including p38 MAPK. Thus, this study has demonstrated a novel function for GAPDH as a mononuclear cell receptor for Human cathelicidin LL-37 and immunomodulatory IDR-1 and conclusively demonstrated its relevance in the functioning of cationic Host defense peptides.
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modulation of the tlr mediated inflammatory response by the endogenous Human Host defense peptide ll 37
Journal of Immunology, 2006Co-Authors: Neeloffer Mookherjee, Reza Falsafi, Jelena Pistolic, Kelly L Brown, Dawn M E Bowdish, Silvana Doria, Karsten Hokamp, Fiona M Roche, Gregory H Doho, Jonpaul S PowersAbstract:The sole Human cathelicidin peptide, LL-37, has been demonstrated to protect animals against endotoxemia/sepsis. Low, physiological concentrations of LL-37 ( or =50% in the presence of LL-37, demonstrating that the peptide altered gene expression in part by acting directly on the TLR-to-NF-kappaB pathway. LL-37 almost completely prevented the release of TNF-alpha and other cytokines by Human PBMC following stimulation with LPS and other TLR2/4 and TLR9 agonists, but not with cytokines TNF-alpha or IL-1beta. Biochemical and inhibitor studies were consistent with a model whereby LL-37 modulated the inflammatory response to LPS/endotoxin and other agonists of TLR by a complex mechanism involving multiple points of intervention. We propose that the natural Human Host defense peptide LL-37 plays roles in the delicate balancing of inflammatory responses in homeostasis as well as in combating sepsis induced by certain TLR agonists.
Faten El Sayed - One of the best experts on this subject based on the ideXlab platform.
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In-Host Adaptation of Salmonella enterica Serotype Dublin during Prosthetic Hip Joint Infection
Emerging Infectious Diseases, 2018Co-Authors: Faten El Sayed, Guillaume Sapriel, Nizar Fawal, Aurelia Gruber, Thomas Bauer, Beate Heym, Caroline Dupont, Henri-jean Garchon, Jean-louis Gaillard, Martin RottmanAbstract:Genome degradation has been central to the adaptation of Salmonella enterica serotypes to their Hosts throughout evolution. We witnessed the patho-adaptation of a strain of Salmonella Dublin (a cattle-adapted serotype) to a Human Host during the course of a recurrent prosthetic hip joint infection evolving over several years.