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  • Journal article
    Clarke TB, 2014,

    Early innate immunity to bacterial infection in the lung is regulated systemically by the commensal microbiota via nod-like receptor ligands

    , Infection and Immunity, Vol: 82, Pages: 4596-4606, ISSN: 0019-9567

    The commensal microbiota is a major regulator of the immune system. The majority of commensal bacteria inhabit the gastrointestinal tract and are known to regulate local mucosal defenses against intestinal pathogens. There is growing appreciation that the commensal microbiota also regulates immune responses at extraintestinal sites. Currently, however, it is unclear how this influences host defenses against bacterial infection outside the intestine. Microbiota depletion caused significant defects in the early innate response to lung infection by the major human pathogen Klebsiella pneumoniae. After microbiota depletion, early clearance of K. pneumoniae was impaired, and this could be rescued by administration of bacterial Nod-like receptor (NLR) ligands (the NOD1 ligand MurNAcTriDAP and NOD2 ligand muramyl dipeptide [MDP]) but not bacterial Toll-like receptor (TLR) ligands. Importantly, NLR ligands from the gastrointestinal, but not upper respiratory, tract rescued host defenses in the lung. Defects in early innate immunity were found to be due to reduced reactive oxygen species-mediated killing of bacteria by alveolar macrophages. These data show that bacterial signals from the intestine have a profound influence on establishing the levels of antibacterial defenses in distal tissues.
  • Journal article
    Clements A, Stoneham CA, Furniss RCD, Frankel Get al., 2014,

    Enterohaemorrhagic <i>Escherichia coli</i> inhibits recycling endosome function and trafficking of surface receptors

    , CELLULAR MICROBIOLOGY, Vol: 16, Pages: 1693-1705, ISSN: 1462-5814
  • Journal article
    Fajardo A, Hernando-Amado S, Oliver A, Ball G, Filloux A, Martinez JLet al., 2014,

    Characterization of a novel Zn<SUP>2+</SUP>-dependent intrinsic imipenemase from <i>Pseudomonas aeruginosa</i>

    , JOURNAL OF ANTIMICROBIAL CHEMOTHERAPY, Vol: 69, Pages: 2972-2978, ISSN: 0305-7453
  • Journal article
    Pallett MA, Berger CN, Pearson JS, Hartland EL, Frankel Get al., 2014,

    The Type III Secretion Effector NleF of Enteropathogenic <i>Escherichia coli</i> Activates NF-κB Early during Infection

    , INFECTION AND IMMUNITY, Vol: 82, Pages: 4878-4888, ISSN: 0019-9567
  • Journal article
    Nicod SS, Weinzierl RO, Burchell L, Escalera-Maurer A, James EH, Wigneshweraraj Set al., 2014,

    Systematic mutational analysis of the LytTR DNA binding domain of Staphylococcus aureus virulence gene transcription factor AgrA

    , Nucleic Acids Research, Vol: 42, Pages: 12523-12536, ISSN: 1362-4962

    Most DNA-binding bacterial transcription factors contact DNA through a recognition α-helix in their DNA-binding domains. An emerging class of DNA-binding transcription factors, predominantly found in pathogenic bacteria interact with the DNA via a relatively novel type of DNA-binding domain, called the LytTR domain, which mainly comprises β strands. Even though the crystal structure of the LytTR domain of the virulence gene transcription factor AgrA from Staphylococcus aureus bound to its cognate DNA sequence is available, the contribution of specific amino acid residues in the LytTR domain of AgrA to transcription activation remains elusive. Here, for the first time, we have systematically investigated the role of amino acid residues in transcription activation in a LytTR domain-containing transcription factor. Our analysis, which involves in vivo and in vitro analyses and molecular dynamics simulations of S. aureus AgrA identifies a highly conserved tyrosine residue, Y229, as a major amino acid determinant for maximal activation of transcription by AgrA and provides novel insights into structure-function relationships in S. aureus AgrA.
  • Journal article
    Campeotto I, Percy MG, MacDonald JT, Foerster A, Freemont PS, Gruendling Aet al., 2014,

    Structural and Mechanistic Insight into the Listeria monocytogenes Two-enzyme Lipoteichoic Acid Synthesis System

    , Journal of Biological Chemistry, Vol: 289, Pages: 28054-28069, ISSN: 0021-9258

    Lipoteichoic acid (LTA) is an important cell wall componentrequired for proper cell growth in many Gram-positive bacteria.In Listeria monocytogenes, two enzymes are required for the synthesisof this polyglycerolphosphate polymer. The LTA primaseLtaPLm initiates LTA synthesis by transferring the first glycerolphosphate(GroP) subunit onto the glycolipid anchor and theLTA synthase LtaSLm extends the polymer by the repeated additionof GroP subunits to the tip of the growing chain. Here, wepresent the crystal structures of the enzymatic domains ofLtaPLm and LtaSLm. Although the enzymes share the same fold,substantial differences in the cavity of the catalytic site andsurface charge distribution contribute to enzyme specialization.The eLtaSLm structure was also determined in complexwith GroP revealing a second GroP binding site. Mutationalanalysis confirmed an essential function for this binding siteand allowed us to propose a model for the binding of thegrowing chain.
  • Journal article
    Painter KL, Krishna A, Wigneshweraraj S, Edwards AMet al., 2014,

    What role does the quorum-sensing accessory gene regulator system play during Staphylococcus aureus bacteremia?

    , Trends in Microbiology, Vol: In Press, ISSN: 0966-842X
  • Journal article
    Belardinelli JM, Larrouy-Maumus G, Jones V, de Carvalho LPS, McNeil MR, Jackson Met al., 2014,

    Biosynthesis and Translocation of Unsulfated Acyltrehaloses in Mycobacterium tuberculosis

    , Journal of Biological Chemistry, Vol: 289, Pages: 27952-27965, ISSN: 1083-351X
  • Journal article
    Collins JW, Chervaux C, Raymond B, Derrien M, Brazeilles R, Kosta A, Chambaud I, Crepin VF, Frankel Get al., 2014,

    Fermented Dairy Products Modulate <i>Citrobacter rodentium</i>-Induced Colonic Hyperplasia

    , JOURNAL OF INFECTIOUS DISEASES, Vol: 210, Pages: 1029-1041, ISSN: 0022-1899
  • Journal article
    Colas C, Menezes S, Gutierrez-Martinez E, Pean CB, Dionne MS, Guermonprez Pet al., 2014,

    An improved flow cytometry assay to monitor phagosome acidification

    , JOURNAL OF IMMUNOLOGICAL METHODS, Vol: 412, Pages: 1-13, ISSN: 0022-1759

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