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  • 1
    Publication Date: 2011-01-29
    Description: The human gut is colonized with a wide variety of microorganisms, including species, such as those belonging to the bacterial genus Bifidobacterium, that have beneficial effects on human physiology and pathology. Among the most distinctive benefits of bifidobacteria are modulation of host defence responses and protection against infectious diseases. Nevertheless, the molecular mechanisms underlying these effects have barely been elucidated. To investigate these mechanisms, we used mice associated with certain bifidobacterial strains and a simplified model of lethal infection with enterohaemorrhagic Escherichia coli O157:H7, together with an integrated 'omics' approach. Here we show that genes encoding an ATP-binding-cassette-type carbohydrate transporter present in certain bifidobacteria contribute to protecting mice against death induced by E. coli O157:H7. We found that this effect can be attributed, at least in part, to increased production of acetate and that translocation of the E. coli O157:H7 Shiga toxin from the gut lumen to the blood was inhibited. We propose that acetate produced by protective bifidobacteria improves intestinal defence mediated by epithelial cells and thereby protects the host against lethal infection.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Fukuda, Shinji -- Toh, Hidehiro -- Hase, Koji -- Oshima, Kenshiro -- Nakanishi, Yumiko -- Yoshimura, Kazutoshi -- Tobe, Toru -- Clarke, Julie M -- Topping, David L -- Suzuki, Tohru -- Taylor, Todd D -- Itoh, Kikuji -- Kikuchi, Jun -- Morita, Hidetoshi -- Hattori, Masahira -- Ohno, Hiroshi -- England -- Nature. 2011 Jan 27;469(7331):543-7. doi: 10.1038/nature09646.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory for Epithelial Immunobiology, RIKEN Research Center for Allergy and Immunology, 1-7-22 Suehiro-cho, Tsurumi-ku, Yokohama, Kanagawa 230-0045, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/21270894" target="_blank"〉PubMed〈/a〉
    Keywords: Acetates/*metabolism ; Animals ; Bifidobacterium/genetics/*metabolism ; Cercopithecus aethiops ; Escherichia coli Infections/microbiology/*prevention & control ; Escherichia coli O157/*physiology ; Gene Expression Profiling ; Genome, Bacterial ; Mice ; Molecular Sequence Data ; Vero Cells
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
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  • 2
    Publication Date: 1995-09-29
    Description: Tyrosine-based signals within the cytoplasmic domain of integral membrane proteins mediate clathrin-dependent protein sorting in the endocytic and secretory pathways. A yeast two-hybrid system was used to identify proteins that bind to tyrosine-based signals. The medium chains (mu 1 and mu 2) of two clathrin-associated protein complexes (AP-1 and AP-2, respectively) specifically interacted with tyrosine-based signals of several integral membrane proteins. The interaction was confirmed by in vitro binding assays. Thus, it is likely that the medium chains serve as signal-binding components of the clathrin-dependent sorting machinery.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ohno, H -- Stewart, J -- Fournier, M C -- Bosshart, H -- Rhee, I -- Miyatake, S -- Saito, T -- Gallusser, A -- Kirchhausen, T -- Bonifacino, J S -- New York, N.Y. -- Science. 1995 Sep 29;269(5232):1872-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Cell Biology and Metabolism Branch, National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, MD 20892, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7569928" target="_blank"〉PubMed〈/a〉
    Keywords: Adaptor Proteins, Vesicular Transport ; Amino Acid Sequence ; Cell Membrane/metabolism ; Clathrin/*metabolism ; Cloning, Molecular ; Glutathione Transferase/metabolism ; Golgi Apparatus/metabolism ; Lysosomes/metabolism ; Membrane Proteins/chemistry/*metabolism ; Molecular Sequence Data ; Nerve Tissue Proteins/chemistry/*metabolism ; Phosphoproteins/chemistry/*metabolism ; Protein Sorting Signals/chemistry/*metabolism ; Recombinant Fusion Proteins/metabolism ; Saccharomyces cerevisiae/genetics/metabolism ; Transformation, Genetic ; Tyrosine/*metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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