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23 results on '"Hawes, Pippa"'

12. Chicken Interferon-induced Protein with Tetratricopeptide Repeats 5 Antagonizes Replication of RNA Viruses

Author

Santhakumar, Diwakar, Rohaim, Mohammed Abdel Mohsen Shahaat, Hussein, Hussein A., Hawes, Pippa, Ferreira, Helena Lage, Behboudi, Shahriar, Iqbal, Munir, Nair, Venugopal, Arns, Clarice W., Munir, Muhammad, Santhakumar, Diwakar, Rohaim, Mohammed Abdel Mohsen Shahaat, Hussein, Hussein A., Hawes, Pippa, Ferreira, Helena Lage, Behboudi, Shahriar, Iqbal, Munir, Nair, Venugopal, Arns, Clarice W., and Munir, Muhammad

Abstract

The intracellular actions of interferon (IFN)-regulated proteins, including IFN-induced proteins with tetratricopeptide repeats (IFITs), attribute a major component of the protective antiviral host defense. Here we applied genomics approaches to annotate the chicken IFIT locus and identified a single IFIT (chIFIT5) gene. The profound transcriptional level of this effector of innate immunity was mapped within its unique cis-acting elements. This highly virus- and IFN-responsive chIFIT5 protein interacted with negative sense viral RNA structures that carried a triphosphate group on its 5’ terminus (ppp-RNA). This interaction reduced the replication of RNA viruses in lentivirus-mediated IFIT5-stable chicken fibroblasts whereas CRISPR/Cas9-edited chIFIT5 gene knockout fibroblasts supported the replication of RNA viruses. Finally, we generated mosaic transgenic chicken embryos stably expressing chIFIT5 protein or knocked-down for endogenous chIFIT5 gene. Replication kinetics of RNA viruses in these transgenic chicken embryos demonstrated the antiviral potential of chIFIT5 in ovo. Taken together, these findings propose that IFIT5 specifically antagonize RNA viruses by sequestering viral nucleic acids in chickens, which are unique in innate immune sensing and responses to viruses of both poultry and human health significance.

Published
2018

18. Role of Intimin-Tir Interactions and the Tir-Cytoskeleton Coupling Protein in the Colonization of Calves and Lambs by Escherichia coli O157:H7

Author

Vlisidou, Isabella, primary, Dziva, Francis, additional, La Ragione, Roberto M., additional, Best, Angus, additional, Garmendia, Junkal, additional, Hawes, Pippa, additional, Monaghan, Paul, additional, Cawthraw, Shaun A., additional, Frankel, Gad, additional, Woodward, Martin J., additional, and Stevens, Mark P., additional

Published
2006
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20. Identification of a bacterial factor required for actin-based motility ofBurkholderia pseudomallei.

Author

Stevens, Mark P., Stevens, Joanne M., Jeng, Robert L., Taylor, Lowrie A., Wood, Michael W., Hawes, Pippa, Monaghan, Paul, Welch, Matthew D., and Galyov, Edouard E.

Subjects
GRAM-negative bacteria, EUKARYOTIC cells, ACTIN, MOTILITY of microorganisms, MICROFILAMENT proteins, MICROBIAL proteins, PATHOGENIC microorganisms
Abstract

Burkholderia pseudomalleiis a Gram-negative facultative intracellular pathogen that enters and escapes from eukaryotic cells using the power of actin polymerization. We have identified a bacterial protein (BimA) that is required for the ability ofB. pseudomalleito induce the formation of actin tails. BimA contains proline-rich motifs and WH2-like domains and shares limited homology at the C-terminus with theYersiniaautosecreted adhesin YadA. BimA is located at the pole of the bacterial cell at which actin polymerization occurs and mutation ofbimAabolished actin-based motility of the pathogen in J774.2 cells. Transient expression of BimA in HeLa cells resulted in F-actin clustering reminiscent of that seen on WASP overexpression. Antibody-mediated clustering of a CD32 chimera in which the cytoplasmic domain was replaced with BimA resulted in localization of the chimera to the tips of F-actin enriched membrane protrusions. We report that purified truncated BimA protein binds monomeric actin in a concentration-dependent manner in cosedimentation assays and that BimA stimulates actin polymerizationin vitroin a manner independent of the cellular Arp2/3 complex. [ABSTRACT FROM AUTHOR]

Published
2005
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21. The Neuroendocrine Stress Hormone Norepinephrine Augments Escherichia coliO157:H7-Induced Enteritis and Adherence in a Bovine Ligated Ileal Loop Model of Infection

Author

Vlisidou, Isabella, Lyte, Mark, van Diemen, Pauline M., Hawes, Pippa, Monaghan, Paul, Wallis, Timothy S., and Stevens, Mark P.

Abstract

ABSTRACTThe role of the neuroendocrine environment in the pathogenesis of enteric bacterial infections is increasingly being recognized. Here we report that norepinephrine augments Escherichia coliO157:H7-induced intestinal inflammatory and secretory responses as well as bacterial adherence to intestinal mucosa in a bovine ligated ileal loop model of infection. Norepinephrine modulation of enteritis and adherence was dependent on the ability of E. coliO157:H7 to form attaching and effacing lesions.

Published
2004
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22. 1st EM-UK Meeting.

Author

Hawes, Pippa

Subjects
*ELECTRON microscopy, *MICROSCOPY, *SOCIETIES
Abstract

The article offers information on the Royal Microscopical Society's Electron Microscopy section's 50th Anniversary celebration, held at January 13, 2016.

Published
2016

23. Electron Microscopy.

Author

Hawes, Pippa

Subjects
*MICROSCOPY, *ELECTRON microscopy, *ANNUAL meetings, *ADULT education workshops, *BACKSCATTERING, *DIFFRACTIVE scattering, *SOCIETIES
Abstract

The article discusses a report by the Royal Microscopical Society's Electron Microscopy (EM) Section which was presented at the Annual General Meetings in July 2014 in Manchester, England about the courses and meetings it organized in 2013-2014. The courses associated with the EM section include the Cryo Workshop in October 2013, and the Spectral Imaging Course and the Electron Bank Scattered Diffraction in April 2014.

Published
2015

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