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  • 1
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    Manipulation of small Rho GTPases is a pathogen-induced process detected by NOD1 (2013)
    Nature Publishing Group (NPG)
    Details
    Publication Date: 2013-04-02
    Description: Our innate immune system distinguishes microbes from self by detecting conserved pathogen-associated molecular patterns. However, these are produced by all microbes, regardless of their pathogenic potential. To distinguish virulent microbes from those with lower disease-causing potential the innate immune system detects conserved pathogen-induced processes, such as the presence of microbial products in the host cytosol, by mechanisms that are not fully resolved. Here we show that NOD1 senses cytosolic microbial products by monitoring the activation state of small Rho GTPases. Activation of RAC1 and CDC42 by bacterial delivery or ectopic expression of SopE, a virulence factor of the enteric pathogen Salmonella, triggered the NOD1 signalling pathway, with consequent RIP2 (also known as RIPK2)-mediated induction of NF-kappaB-dependent inflammatory responses. Similarly, activation of the NOD1 signalling pathway by peptidoglycan required RAC1 activity. Furthermore, constitutively active forms of RAC1, CDC42 and RHOA activated the NOD1 signalling pathway. Our data identify the activation of small Rho GTPases as a pathogen-induced process sensed through the NOD1 signalling pathway.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3625479/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3625479/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Keestra, A Marijke -- Winter, Maria G -- Auburger, Josef J -- Frassle, Simon P -- Xavier, Mariana N -- Winter, Sebastian E -- Kim, Anita -- Poon, Victor -- Ravesloot, Marietta M -- Waldenmaier, Julian F T -- Tsolis, Renee M -- Eigenheer, Richard A -- Baumler, Andreas J -- AI044170/AI/NIAID NIH HHS/ -- AI076246/AI/NIAID NIH HHS/ -- R01 AI044170/AI/NIAID NIH HHS/ -- R01 AI076246/AI/NIAID NIH HHS/ -- England -- Nature. 2013 Apr 11;496(7444):233-7. doi: 10.1038/nature12025. Epub 2013 Mar 31.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Medical Microbiology and Immunology, School of Medicine, University of California at Davis, One Shields Avenue, Davis, California 95616, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/23542589" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Bacterial Proteins/metabolism ; Cytosol/metabolism ; Female ; HEK293 Cells ; HSP90 Heat-Shock Proteins/metabolism ; Humans ; Male ; Mice ; Mice, Inbred C57BL ; NF-kappa B/metabolism ; Nod1 Signaling Adaptor Protein/*metabolism ; Nod2 Signaling Adaptor Protein/metabolism ; Peptidoglycan/metabolism ; Receptor-Interacting Protein Serine-Threonine Kinase 2/metabolism ; Salmonella typhimurium/genetics/*metabolism/*pathogenicity ; Signal Transduction ; Virulence Factors/metabolism ; cdc42 GTP-Binding Protein/metabolism ; rac1 GTP-Binding Protein/metabolism ; rho GTP-Binding Proteins/*metabolism ; rhoA GTP-Binding Protein/metabolism
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Published by Nature Publishing Group (NPG)
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  • 2
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    Human alpha-defensin 6 promotes mucosal innate immunity through self-assembled peptide nanonets (2012)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2012-06-23
    Description: Defensins are antimicrobial peptides that contribute broadly to innate immunity, including protection of mucosal tissues. Human alpha-defensin (HD) 6 is highly expressed by secretory Paneth cells of the small intestine. However, in contrast to the other defensins, it lacks appreciable bactericidal activity. Nevertheless, we report here that HD6 affords protection against invasion by enteric bacterial pathogens in vitro and in vivo. After stochastic binding to bacterial surface proteins, HD6 undergoes ordered self-assembly to form fibrils and nanonets that surround and entangle bacteria. This self-assembly mechanism occurs in vivo, requires histidine-27, and is consistent with x-ray crystallography data. These findings support a key role for HD6 in protecting the small intestine against invasion by diverse enteric pathogens and may explain the conservation of HD6 throughout Hominidae evolution.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4332406/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4332406/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chu, Hiutung -- Pazgier, Marzena -- Jung, Grace -- Nuccio, Sean-Paul -- Castillo, Patricia A -- de Jong, Maarten F -- Winter, Maria G -- Winter, Sebastian E -- Wehkamp, Jan -- Shen, Bo -- Salzman, Nita H -- Underwood, Mark A -- Tsolis, Renee M -- Young, Glenn M -- Lu, Wuyuan -- Lehrer, Robert I -- Baumler, Andreas J -- Bevins, Charles L -- AI032738/AI/NIAID NIH HHS/ -- AI040124/AI/NIAID NIH HHS/ -- AI044170/AI/NIAID NIH HHS/ -- AI050843/AI/NIAID NIH HHS/ -- AI057757/AI/NIAID NIH HHS/ -- AI070726/AI/NIAID NIH HHS/ -- AI072732/AI/NIAID NIH HHS/ -- AI073120/AI/NIAID NIH HHS/ -- AI076246/AI/NIAID NIH HHS/ -- AI082320/AI/NIAID NIH HHS/ -- AI088122/AI/NIAID NIH HHS/ -- HD059127/HD/NICHD NIH HHS/ -- R01 AI032738/AI/NIAID NIH HHS/ -- R01 AI050843/AI/NIAID NIH HHS/ -- R01 AI057757/AI/NIAID NIH HHS/ -- R01 AI076246/AI/NIAID NIH HHS/ -- R01 GM099526/GM/NIGMS NIH HHS/ -- T32AI060555/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 2012 Jul 27;337(6093):477-81. doi: 10.1126/science.1218831. Epub 2012 Jun 21.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Microbiology and Immunology, School of Medicine, University of California, Davis, CA 95616, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/22722251" target="_blank"〉PubMed〈/a〉
    Keywords: Adhesins, Bacterial/metabolism ; Animals ; Bacterial Proteins/metabolism ; Cell Line ; Humans ; *Immunity, Innate ; *Immunity, Mucosal ; Intestinal Mucosa/immunology/microbiology/ultrastructure ; Intestine, Small/*immunology/microbiology/ultrastructure ; Macromolecular Substances/chemistry/immunology/metabolism ; Mice ; Mice, Transgenic ; Microscopy, Electron, Scanning ; Models, Molecular ; Nanostructures ; Paneth Cells/immunology/metabolism ; Peptides/chemistry/metabolism ; Protein Binding ; Protein Multimerization ; Protein Structure, Quaternary ; Salmonella Infections, Animal/immunology/microbiology ; Salmonella typhimurium/immunology/pathogenicity/ultrastructure ; Yersinia enterocolitica/immunology/pathogenicity ; alpha-Defensins/*chemistry/immunology/*metabolism ; env Gene Products, Human Immunodeficiency Virus/metabolism
    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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