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  • 1
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    Regulation of intestinal alpha-defensin activation by the metalloproteinase matrilysin in innate host defense (1999)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1999-10-03
    Description: Precursors of alpha-defensin peptides require activation for bactericidal activity. In mouse small intestine, matrilysin colocalized with alpha-defensins (cryptdins) in Paneth cell granules, and in vitro it cleaved the pro segment from cryptdin precursors. Matrilysin-deficient (MAT-/-) mice lacked mature cryptdins and accumulated precursor molecules. Intestinal peptide preparations from MAT-/- mice had decreased antimicrobial activity. Orally administered bacteria survived in greater numbers and were more virulent in MAT-/- mice than in MAT+/+ mice. Thus, matrilysin functions in intestinal mucosal defense by regulating the activity of defensins, which may be a common role for this metalloproteinase in its numerous epithelial sites of expression.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wilson, C L -- Ouellette, A J -- Satchell, D P -- Ayabe, T -- Lopez-Boado, Y S -- Stratman, J L -- Hultgren, S J -- Matrisian, L M -- Parks, W C -- New York, N.Y. -- Science. 1999 Oct 1;286(5437):113-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pediatrics, Division of Allergy and Pulmonary Medicine, Washington University School of Medicine, St. Louis, MO 63110, USA. wilson_c@kids.wustl.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10506557" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Catalysis ; Cytoplasmic Granules/enzymology ; Escherichia coli/growth & development ; Escherichia coli Infections/immunology/microbiology ; Female ; Humans ; *Immunity, Innate ; *Immunity, Mucosal ; Intestinal Mucosa/enzymology/immunology/microbiology ; Intestine, Small/enzymology/*immunology/microbiology ; Male ; Matrix Metalloproteinase 7 ; Metalloendopeptidases/genetics/*metabolism ; Mice ; Molecular Sequence Data ; Paneth Cells/enzymology ; Protein Precursors/genetics/*metabolism ; Recombinant Fusion Proteins/metabolism ; Salmonella typhimurium/growth & development/pathogenicity ; Tissue Extracts/pharmacology
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 2
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    Prevention of mucosal Escherichia coli infection by FimH-adhesin-based systemic vaccination (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-04-25
    Description: Virtually all uropathogenic strains of Escherichia coli, the primary cause of cystitis, assemble adhesive surface organelles called type 1 pili that contain the FimH adhesin. Sera from animals vaccinated with candidate FimH vaccines inhibited uropathogenic E. coli from binding to human bladder cells in vitro. Immunization with FimH reduced in vivo colonization of the bladder mucosa by more than 99 percent in a murine cystitis model, and immunoglobulin G to FimH was detected in urinary samples from protected mice. Furthermore, passive systemic administration of immune sera to FimH also resulted in reduced bladder colonization by uropathogenic E. coli. This approach may represent a means of preventing recurrent and acute infections of the urogenital mucosa.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Langermann, S -- Palaszynski, S -- Barnhart, M -- Auguste, G -- Pinkner, J S -- Burlein, J -- Barren, P -- Koenig, S -- Leath, S -- Jones, C H -- Hultgren, S J -- R01DK51406/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 1997 Apr 25;276(5312):607-11.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉MedImmune, Inc., Gaithersburg, MD 20878, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9110982" target="_blank"〉PubMed〈/a〉
    Keywords: Adhesins, Bacterial/*immunology/metabolism ; *Adhesins, Escherichia coli ; Animals ; Antibodies, Bacterial/analysis/immunology ; Bacterial Adhesion ; *Bacterial Vaccines/administration & dosage/immunology ; Child ; Cystitis/immunology/*prevention & control ; Epithelium/microbiology ; Escherichia coli/immunology/metabolism/pathogenicity ; Escherichia coli Infections/immunology/*prevention & control ; Female ; *Fimbriae Proteins ; Fimbriae, Bacterial/immunology ; Humans ; Immunity, Mucosal ; Mice ; Mice, Inbred C3H ; Neutrophils/immunology ; Rabbits ; Urinary Bladder/microbiology ; Vaccination ; *Vaccines, Synthetic/administration & dosage/immunology
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 3
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    Intracellular bacterial biofilm-like pods in urinary tract infections (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2003-07-05
    Description: Escherichia coli entry into the bladder is met with potent innate defenses, including neutrophil influx and epithelial exfoliation. Bacterial subversion of innate responses involves invasion into bladder superficial cells. We discovered that the intracellular bacteria matured into biofilms, creating pod-like bulges on the bladder surface. Pods contained bacteria encased in a polysaccharide-rich matrix surrounded by a protective shell of uroplakin. Within the biofilm, bacterial structures interacted extensively with the surrounding matrix, and biofilm associated factors had regional variation in expression. The discovery of intracellular biofilm-like pods explains how bladder infections can persist in the face of robust host defenses.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Anderson, Gregory G -- Palermo, Joseph J -- Schilling, Joel D -- Roth, Robyn -- Heuser, John -- Hultgren, Scott J -- AI29549/AI/NIAID NIH HHS/ -- AI48689/AI/NIAID NIH HHS/ -- DK51406/DK/NIDDK NIH HHS/ -- DK64540/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 2003 Jul 4;301(5629):105-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Microbiology, Washington University School of Medicine, 660 South Euclid Avenue, St. Louis, MO 63110, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12843396" target="_blank"〉PubMed〈/a〉
    Keywords: *Adhesins, Bacterial ; Adhesins, Escherichia coli ; Animals ; *Antigens, Bacterial ; Bacterial Outer Membrane Proteins/analysis ; *Biofilms ; Colony Count, Microbial ; Epithelial Cells/microbiology/ultrastructure ; Escherichia coli/growth & development/immunology/*pathogenicity/ultrastructure ; Escherichia coli Infections/immunology/*microbiology/pathology ; *Escherichia coli Proteins ; Female ; Fimbriae, Bacterial/physiology/ultrastructure ; Freeze Fracturing ; Immunity, Innate ; Membrane Glycoproteins/analysis ; Mice ; Mice, Inbred C3H ; Microscopy, Electron ; Microscopy, Electron, Scanning ; Polysaccharides, Bacterial/analysis ; Urinary Bladder/immunology/*microbiology/ultrastructure ; Urinary Bladder Diseases/immunology/*microbiology/pathology ; Urinary Tract Infections/immunology/*microbiology/pathology ; Urothelium/microbiology/ultrastructure
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 4
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    Induction and evasion of host defenses by type 1-piliated uropathogenic Escherichia coli (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-11-20
    Description: Virtually all uropathogenic strains of Escherichia coli encode filamentous surface adhesive organelles called type 1 pili. High-resolution electron microscopy of infected mouse bladders revealed that type 1 pilus tips interacted directly with the lumenal surface of the bladder, which is embedded with hexagonal arrays of integral membrane glycoproteins known as uroplakins. Attached pili were shortened and facilitated intimate contact of the bacteria with the uroplakin-coated host cells. Bacterial attachment resulted in exfoliation of host bladder epithelial cells as part of an innate host defense system. Exfoliation occurred through a rapid apoptosis-like mechanism involving caspase activation and host DNA fragmentation. Bacteria resisted clearance in the face of host defenses within the bladder by invading into the epithelium.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mulvey, M A -- Lopez-Boado, Y S -- Wilson, C L -- Roth, R -- Parks, W C -- Heuser, J -- Hultgren, S J -- AI09787/AI/NIAID NIH HHS/ -- R01AI29549/AI/NIAID NIH HHS/ -- R01DK51406/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 1998 Nov 20;282(5393):1494-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Microbiology and Microbial Pathogenesis, Box 8230, Washington University School of Medicine, 660 S. Euclid Avenue, St. Louis, MO 63110, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9822381" target="_blank"〉PubMed〈/a〉
    Keywords: Adhesins, Bacterial/metabolism ; *Adhesins, Escherichia coli ; Amino Acid Chloromethyl Ketones/pharmacology ; Animals ; Apoptosis ; Bacterial Adhesion ; Caspase Inhibitors ; Caspases/metabolism ; Cysteine Proteinase Inhibitors/pharmacology ; Cystitis/*microbiology/pathology ; DNA Fragmentation ; Escherichia coli/genetics/*pathogenicity ; Escherichia coli Infections/*microbiology/pathology ; Female ; *Fimbriae Proteins ; Fimbriae, Bacterial/physiology/ultrastructure ; In Situ Nick-End Labeling ; Membrane Glycoproteins/analysis/metabolism ; Mice ; Mice, Inbred C57BL ; Microscopy, Electron ; Microscopy, Electron, Scanning ; Tetraspanins ; Urinary Bladder/chemistry/*microbiology/pathology ; Uroplakin Ib ; Urothelium/microbiology/pathology
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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