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  • 1
    Online Resource
    Online Resource
    Basel :S. Karger AG,
    Keywords: Electronic books.
    Type of Medium: Online Resource
    Pages: 1 online resource (203 pages)
    Edition: 1st ed.
    ISBN: 9783318011746
    Series Statement: Chemical Immunology and Allergy Series ; v.86
    Language: English
    Note: Cover -- Contents -- Preface -- Antimicrobial Peptides: Basic Features and Clinical Relevance -- Antimicrobial Peptides in Drosophila: Structures, Activities and Gene Regulation -- Abstract -- Introduction -- Drosophila Defensin, An Anti-Gram-Positive Peptide -- The Antifungal Drosomycin -- Antifungal Peptide -- Metchnikowin, A Cysteine-Free Drosophila Antifungal Peptide -- Cecropins, alpha-Helical Peptides Largely Distributed in Higher Insect Orders -- Drosocin, An Anti-Gram-Negative O-Glycopeptide -- Diptericin, An Anti-Gram-Negative O-Glycopeptide -- Attacins, Large Polypeptides with Antibacterial Properties -- MPAC, the Drosophila Attacin C Pro-Domain with Antibacterial Properties -- Rel Proteins Control Expression of Antimicrobial Peptide Genes -- The Toll and IMD Pathways Control Inducible Expression of AMP Genes -- Other Signaling Pathways Activated during the Drosophila Immune Response -- Hemocytes in the Drosophila Immune Response -- Epithelial Responses in Drosophila -- Concluding Remarks -- Acknowledgements -- References -- Antimicrobial Peptides in Human Skin -- Abstract -- Introduction -- beta-Defensins -- Human beta-Defensin-2 -- Human beta-Defensin-3 -- Human beta-Defensin-1 -- Human beta-Defensin-4 -- Cathelicidin LL-37 -- Serine Protease Inhibitors Antileukoprotease and Elafin -- Dermcidin -- Adrenomedullin -- Neutrophil Gelatinase-Associated Lipocalin -- RNase 7 -- Skin Disease Implications -- Conclusion -- References -- Human Defensins in Crohn's Disease -- Abstract -- Introduction -- Epidemiology: The Role of Hygiene -- Pathophysiology: The Role of Luminal and Mucosal Bacteria -- Defensin Expression and Regulation in the Healthy Intestinal Tract -- Defensins and Inflammatory Bowel Diseases -- NOD2, A Peptidoglycan Receptor and Defensin Expression -- Toll-Like Receptors and Their Expression in Inflammatory Bowel Diseases. , Therapy: The Role of Antibiotics and Probiotics -- Concluding Remarks -- Acknowledgements -- References -- Antimicrobial Peptides in Lung Inflammation -- Abstract -- Introduction -- AMPs Are Expressed in the Respiratory Tract -- Host Defense in the Airways -- AMPs in the Human Lung -- Regulation of the AMPs in the Lung -- Functions of AMPs in the Respiratory Tract -- Antimicrobial Activity -- Inflammation, Angiogenesis, and Cell Function -- Role of AMPs in Pulmonary Disease -- Pneumonia and Tuberculosis -- Cystic Fibrosis and Diffuse Panbronchiolitis -- Asthma and Chronic Obstructive Pulmonary Disease -- Adult Respiratory Distress Syndrome -- Pulmonary Fibrosis and Sarcoidosis -- Conclusions -- Acknowledgement -- References -- Reciprocal Interactions of Host Cells and Microbes -- Bacterial Evasion of Innate Defense at Epithelial Linings -- Abstract -- How to Circumvent Physical Removal from Body Surfaces -- Overcome Space and Nutrient Deprivation -- Resisting the Low-pH Defense Barrier -- Avoid Protease Mediated Destruction and Opsonization -- Evade Recognition and Cell Activation -- Withstand Targeted Destruction -- Active Penetration of the Epithelial Cell Barrier -- Acknowledgements -- References -- Recognition of Bacterial Products by Toll-Like Receptors -- Abstract -- Mammalian Toll-Like Receptors and Their Ligands -- Extracellular Recognition of TLR Ligands -- TLR4 -- TLR2, TLR2/TLR1, and TLR2/TLR6 -- TLR10 -- TLR5 -- TLR11 -- Intracellular Recognition of TLR Ligands -- TLR3 -- TLR7/TLR8 -- TLR9 -- Conclusion -- References -- TLR Signalling and the Function of Dendritic Cells -- Abstract -- Introduction -- What Are Toll-Like Receptors? -- Toll-Like Receptors Recognize Various Molecules -- Signalling Pathway of TLRs -- MyD88-Dependent Pathway -- MyD88-Independent Pathway -- TIRAP/Mal -- TRIF -- TRAM -- The Role of TLR Family in the Host Defence. , TLRs Stimulate DCs to Induce T Cell Activation -- LPS-Stimulated MyD88-Deficient DCs -- DC Subset-Dependent Cytokine Production -- Conclusion -- References -- Contribution of T Cells to Epithelial Defense -- Immunosurveillance by gama/deltaT Cells: Focus on the Murine System -- Abstract -- TCRgamadelta+ Intraepithelial Lymphocytes -- Immunoprotective Roles of gamadelta T Cells in the Tissues -- Immunoregulatory Roles of Local gamadelta T Cells -- gamadelta+ T Cells and Tumor Surveillance -- gamadelta+ T Cell Regulation of Epithelial Malignancy -- From gamadelta Cell Biology in Mice to Immunosurveillance in Humans -- Immunological Mechanisms Highlighted by gamadelta Cells - Towards the Clinic -- References -- gamadelta T Cells Link Innate and Adaptive Immune Responses -- Abstract -- Introduction -- Vgama9/Vdelta2 T Cells -- Vgama9/Vdelta2 T Cells Are Expanded by Various Microbes -- Vgama9/Vdelta2 T Cells Are Activated by Non-Peptide Antigens -- Non-Mevalonate Pathway Intermediates Are the Most Potent Vgama9/Vdelta2 Activators -- Alkylamines Activate Vgama9/Vdelta2 T Cells -- N-Bisphosphonates Stimulate Vgama9/Vdelta2 T Cells -- Vgama9/Vdelta2 T Cells Can Kill Bacteria within Hours after Activation -- The Vgama9/Vdelta2 TCR Repertoire Is Shaped by Non-Peptide Antigens -- Vgama9/Vdelta2 T Cells and Tumor Surveillance -- Activation of Vgama9/Vdelta2 T Cells as a Therapeutic Approach in Tumor Treatment: From Bench to Bedside -- Vdelta1 Cells -- Vdelta1 T Cells Are the Dominant gamma/delta T Cell Population at Mucosal Surfaces -- Vdelta1 T Cells Are Activated by MICA/B -- Vdelta1 T Cells Are Activated by Glycolipids Presented by CD1 -- Lipid Extracts from Gram-Negative Bacteria Indirectly Stimulate Vdelta1T Cells -- TCR Repertoire of Vdelta1 T Cells -- The Role of Vdelta1 T Cells in Microbial Infections -- The Role of Vdelta1 T Cells in Tumor Recognition. , Migration and Homing of gamma/delta T cells -- Chemokine Expression of Peripheral gamma/delta T cells -- gamma/delta T Cells Can Be Polarized into TH1/TH2 Cells -- Chemokine Expression of Mucosal gamma/delta T Cells -- gamma/delta T Cells Can Have Immunosuppressive and Anti-Inflammatory Activities -- Expression of Toll-Like Receptors -- Concluding Remarks -- References -- Author Index -- Subject Index -- A -- B -- C -- D -- E -- F -- G -- H -- I -- L -- M -- N -- P -- R -- S -- T -- Y.
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  • 2
    Publication Date: 2013-02-21
    Description: Bacillus cereus strains harboring a pXO1-like virulence plasmid cause respiratory anthrax-like disease in humans, particularly in welders. We developed mouse models for intraperitoneal as well as aerosol challenge with spores of B. cereus G9241, harboring pBCXO1 and pBC218 virulence plasmids. Compared to wild-type B. cereus G9241, spores with a deletion of the pBCXO1-carried protective antigen gene ( pagA1 ) were severely attenuated, whereas spores with a deletion of the pBC218-carried protective antigen homologue ( pagA2 ) were not. Anthrax vaccine adsorbed (AVA) immunization raised antibodies that bound and neutralized the pagA1 -encoded protective antigen (PA1) but not the PA2 orthologue encoded by pagA2 . AVA immunization protected mice against a lethal challenge with spores from B. cereus G9241 or B. cereus Elc4, a strain that had been isolated from a fatal case of anthrax-like disease. As the pathogenesis of B. cereus anthrax-like disease in mice is dependent on pagA1 and PA-neutralizing antibodies provide protection, AVA immunization may also protect humans from respiratory anthrax-like death.
    Print ISSN: 0019-9567
    Electronic ISSN: 1098-5522
    Topics: Medicine
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  • 3
    Publication Date: 2015-11-11
    Description: Many pathogens usurp the host hemostatic system during infection to promote pathogenesis. Yersinia pestis , the causative agent of plague, expresses the plasminogen activator protease Pla, which has been shown in vitro to target and cleave multiple proteins within the fibrinolytic pathway, including the plasmin inhibitor α2-antiplasmin (A2AP). It is not known, however, if Pla inactivates A2AP in vivo ; the role of A2AP during respiratory Y. pestis infection is not known either. Here, we show that Y. pestis does not appreciably cleave A2AP in a Pla-dependent manner in the lungs during experimental pneumonic plague. Furthermore, following intranasal infection with Y. pestis , A2AP-deficient mice exhibit no difference in survival time, bacterial burden in the lungs, or dissemination from wild-type mice. Instead, we found that in the absence of Pla, A2AP contributes to the control of the pulmonary inflammatory response during infection by reducing neutrophil recruitment and cytokine production, resulting in altered immunopathology of the lungs compared to A2AP-deficient mice. Thus, our data demonstrate that A2AP is not significantly affected by the Pla protease during pneumonic plague, and although A2AP participates in immune modulation in the lungs, it has limited impact on the course or ultimate outcome of the infection.
    Print ISSN: 0019-9567
    Electronic ISSN: 1098-5522
    Topics: Medicine
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  • 4
    Publication Date: 2015-12-29
    Description: Pneumonic plague represents the most severe form of disease caused by Yersinia pestis due to its ease of transmission, rapid progression, and high mortality rate. The Y. pestis outer membrane Pla protease is essential for the development of pneumonic plague; however, the complete repertoire of substrates cleaved by Pla in the lungs is not known. In this study, we describe a proteomic screen to identify host proteins contained within the bronchoalveolar lavage fluid of mice that are cleaved and/or processed by Y. pestis in a Pla-dependent manner. We identified peroxiredoxin 6 (Prdx6), a host factor that contributes to pulmonary surfactant metabolism and lung defense against oxidative stress, as a previously unknown substrate of Pla. Pla cleaves Prdx6 at three distinct sites, and these cleavages disrupt both the peroxidase and phospholipase A 2 activities of Prdx6. In addition, we found that infection with wild-type Y. pestis reduces the abundance of extracellular Prdx6 in the lungs compared to that after infection with pla Y. pestis , suggesting that Pla cleaves Prdx6 in the pulmonary compartment. However, following infection with either wild-type or pla Y. pestis , Prdx6-deficient mice exhibit no differences in bacterial burden, host immune response, or lung damage from wild-type mice. Thus, while Pla is able to disrupt Prdx6 function in vitro and reduce Prdx6 levels in vivo , the cleavage of Prdx6 has little detectable impact on the progression or outcome of pneumonic plague.
    Print ISSN: 0019-9567
    Electronic ISSN: 1098-5522
    Topics: Medicine
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