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• Journal article
  James EH, Edwards AM, Wigneshweraraj S, 2013,

  Transcriptional downregulation of agr expression in Staphylococcus aureus during growth in human serum can be overcome by constitutively active mutant forms of the sensor kinase AgrC

  , FEMS Microbiology Letters, Vol: 349, Pages: 153-162, ISSN: 0378-1097

  The temporal and cell density-dependent regulation of expression of virtually all the Staphylococcus aureus virulon is under the control of the agr (accessory gene regulatory) operon. The expression of the agr operon is subject to transcriptional regulation by the AgrA/C two-component response regulator/sensor kinase pair. During bacteraemia, a frequent syndrome caused by methicillin-resistant S. aureus (MRSA), the transcriptional downregulation of agr expression has been attributed to the sequestration of the quorum-signalling molecule auto-inducing peptide (AIP) by the human serum component apolipoprotein B as part of an innate immune response to infection. However, it is not known whether transcriptional downregulation of agr expression during growth in human serum is additionally subjected to regulation by transcription regulatory proteins that either directly or indirectly affect transcription from the agr operon promoters. Here, using chromosomal fluorescence reporters of agr expression in S. aureus, we show that the transcriptional downregulation of agr expression in human serum can be overcome using constitutive active mutant forms of AgrC. Therefore, it seems that the sequestration of the AIP is likely to be the only mechanism by which the host innate immune response limits agr expression at the transcriptional level to maintain the host–pathogen balance towards a noninvasive outcome.

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• Conference paper
  Al Shammari B, Shiomi T, Tezera L, Workman V, Jayasinghe S, Sathyamoorthy T, Mauri F, Robertson BD, Friedland JS, D'Armiento J, Elkington PTet al., 2013,

  Cell-matrix interactions regulate the immune response to Mycobacterium tuberculosis

  , Annual Congress of the British-Society-for-Immunology, Publisher: WILEY-BLACKWELL, Pages: 104-104, ISSN: 0019-2805
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• Journal article
  Muniz-Feliciano L, Van Grol J, Portillo J-AC, Liew L, Liu B, Carlin CR, Carruthers VB, Matthews S, Subauste CSet al., 2013,

  <i>Toxoplasma gondii</i>-Induced Activation of EGFR Prevents Autophagy Protein-Mediated Killing of the Parasite

  , PLOS PATHOGENS, Vol: 9, ISSN: 1553-7366
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  • Citations: 86
• Journal article
  Schumacher J, Behrends V, Pan Z, Brown DR, Heydenreich F, Lewis MR, Bennett MH, Razzaghi B, Komorowski M, Barahona M, Stumpf MPH, Wigneshweraraj S, Bundy JG, Buck Met al., 2013,

  Nitrogen and Carbon Status Are Integrated at the Transcriptional Level by the Nitrogen Regulator NtrC <i>In Vivo</i>

  , MBIO, Vol: 4, ISSN: 2150-7511
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  • Citations: 45
• Journal article
  Lu Z, Bergeron JRC, Atkinson RA, Schaller T, Veselkov DA, Oregioni A, Yang Y, Matthews SJ, Malim MH, Sanderson MRet al., 2013,

  Insight into the HIV-1 Vif SOCS-box-ElonginBC interaction

  , Open Biology, Vol: 3, Pages: 1-11, ISSN: 2046-2441

  The HIV-1 viral infectivity factor (Vif) neutralizes cell-encoded antiviral APOBEC3 proteins by recruiting a cellular ElonginB (EloB)/ElonginC (EloC)/Cullin5-containing ubiquitin ligase complex, resulting in APOBEC3 ubiquitination and proteolysis. The suppressors-of-cytokine-signalling-like domain (SOCS-box) of HIV-1 Vif is essential for E3 ligase engagement, and contains a BC box as well as an unusual proline-rich motif. Here, we report the NMR solution structure of the Vif SOCS–ElonginBC (EloBC) complex. In contrast to SOCS-boxes described in other proteins, the HIV-1 Vif SOCS-box contains only one α-helical domain followed by a β-sheet fold. The SOCS-box of Vif binds primarily to EloC by hydrophobic interactions. The functionally essential proline-rich motif mediates a direct but weak interaction with residues 101–104 of EloB, inducing a conformational change from an unstructured state to a structured state. The structure of the complex and biophysical studies provide detailed insight into the function of Vif's proline-rich motif and reveal novel dynamic information on the Vif–EloBC interaction.

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• Journal article
  Gouzy A, Larrouy-Maumus G, Wu T-D, Peixoto A, Levillain F, Lugo-Villarino G, Guerquin-Kern J-L, de Carvalho LPS, Poquet Y, Neyrolles Oet al., 2013,

  <i>Mycobacterium tuberculosis</i> nitrogen assimilation and host colonization require aspartate

  , NATURE CHEMICAL BIOLOGY, Vol: 9, Pages: 674-+, ISSN: 1552-4450
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  • Citations: 74
• Journal article
  Lai Y, Rosenshine I, Leong JM, Frankel Get al., 2013,

  Intimate host attachment: enteropathogenic and enterohaemorrhagic <i>Escherichia coli</i>

  , CELLULAR MICROBIOLOGY, Vol: 15, Pages: 1796-1808, ISSN: 1462-5814
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  • Citations: 81
• Journal article
  Mercedes Palomino M, Allievi MC, Gruendling A, Sanchez-Rivas C, Ruzal SMet al., 2013,

  Osmotic stress adaptation in <i>Lactobacillus casei</i> BL23 leads to structural changes in the cell wall polymer lipoteichoic acid

  , MICROBIOLOGY-SGM, Vol: 159, Pages: 2416-2426, ISSN: 1350-0872
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  • Citations: 34
• Journal article
  Harding CR, Mattheis C, Mousnier A, Oates CV, Hartland EL, Frankel G, Schroeder GNet al., 2013,

  LtpD Is a Novel <i>Legionella pneumophila</i> Effector That Binds Phosphatidylinositol 3-Phosphate and Inositol Monophosphatase IMPA1

  , INFECTION AND IMMUNITY, Vol: 81, Pages: 4261-4270, ISSN: 0019-9567
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  • Citations: 28
• Journal article
  Clark RI, Tan SWS, Pean CB, Roostalu U, Vivancos V, Bronda K, Pilatova M, Fu J, Walker DW, Berdeaux R, Geissmann F, Dionne MSet al., 2013,

  MEF2 Is an In Vivo Immune-Metabolic Switch

  , CELL, Vol: 155, Pages: 435-447, ISSN: 0092-8674
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  • Citations: 114

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