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  • Journal article
    Koutsakos M, Thi HN, Barclay WS, Kedzierska Ket al., 2015,

    Knowns and unknowns of influenza B viruses

    , Future Microbiology, Vol: 11, Pages: 119-135, ISSN: 1746-0913

    Influenza B viruses (IBVs) circulate annually along with influenza A (IAV) strains during seasonal epidemics. IBV can dominate influenza seasons and cause severe disease, particularly in children and adolescents. Research has revealed interesting aspects of IBV and highlighted the importance of these viruses in clinical settings. Yet, many important questions remain unanswered. In this review, the clinical relevance of IBV is emphasized, unique features in epidemiology, host range and virology are highlighted and gaps in knowledge pinpointed. Multiple aspects of IBV epidemiology, evolution, virology and immunology are discussed. Future research into IBV is needed to understand how we can prevent severe disease in high-risk groups, especially children and elderly.
  • Journal article
    Hardin JW, Warnasooriya C, Kondo Y, Nagai K, Rueda DSet al., 2015,

    Assembly and dynamics of the U4/U6 di-snRNP by single-molecule FRET

    , Nucleic Acids Research, Vol: 43, Pages: 10963-10974, ISSN: 1362-4962

    In large ribonucleoprotein machines, such as ribosomes and spliceosomes, RNA functions as an assembly scaffold as well as a critical catalytic component. Protein binding to the RNA scaffold can induce structural changes, which in turn modulate subsequent binding of other components. The spliceosomal U4/U6 di-snRNP contains extensively base paired U4 and U6 snRNAs, Snu13, Prp31, Prp3 and Prp4, seven Sm and seven LSm proteins. We have studied successive binding of all protein components to the snRNA duplex during di-snRNP assembly by electrophoretic mobility shift assay and accompanying conformational changes in the U4/U6 RNA 3-way junction by single-molecule FRET. Stems I and II of the duplex were found to co-axially stack in free RNA and function as a rigid scaffold during the entire assembly, but the U4 snRNA 5′ stem-loop adopts alternative orientations each stabilized by Prp31 and Prp3/4 binding accounting for altered Prp3/4 binding affinities in presence of Prp31.
  • Journal article
    Brenlla A, Rueda D, Romano LJ, 2015,

    Mechanism of aromatic amine carcinogen bypass by the Y-family polymerase, Dpo4

    , Nucleic Acids Research, Vol: 43, Pages: 9918-9927, ISSN: 1362-4962
  • Journal article
    Matos-Patron A, Byrd-Leotis L, Steinhauer DA, Barclay WS, Ayora-Talavera Get al., 2015,

    Amino acid substitution D222N from fatal influenza infection affects receptor-binding properties of the influenza A(H1N1)pdm09 virus

    , VIROLOGY, Vol: 484, Pages: 15-21, ISSN: 0042-6822
  • Journal article
    Liu M, Lam MK-H, Zhang Q, Elderfield R, Barclay WS, Shaw P-Cet al., 2015,

    The Functional Study of the N-Terminal Region of Influenza B Virus Nucleoprotein

    , PLOS One, Vol: 10, ISSN: 1932-6203

    Influenza nucleoprotein (NP) is a major component of the ribonucleoprotein (vRNP) in influenzavirus, which functions for the transcription and replication of viral genome. Comparedto the nucleoprotein of influenza A (ANP), the N-terminal region of influenza B nucleoprotein(BNP) is much extended. By virus reconstitution, we found that the first 38 residues areessential for viral growth. We further illustrated the function of BNP by mini-genome reconstitution,fluorescence microscopy, electron microscopy, light scattering and gel shift.Results show that the N terminus is involved in the formation of both higher homo-oligomersof BNP and BNP-RNA complex.
  • Journal article
    Gregorovic G, Boulden EA, Bosshard R, Karstegl CE, Skalsky R, Cullen BR, Gujer C, Rämer P, Münz C, Farrell PJet al., 2015,

    Epstein-Barr viruses deficient in EBER RNAs give higher LMP2 RNA expression in lymphoblastoid cell lines and efficiently establish persistent infection in humanized mice.

    , Journal of Virology, Vol: 89, Pages: 1171-11714, ISSN: 1098-5514

    Functions of EBER RNAs were tested in lymphoblastoid cell lines containing EBER mutants of Epstein-Barr Virus (EBV). Binding of EBER1 to RPL22 was confirmed. Deletion of EBER1 or EBER2 correlated with increased cytoplasmic EBV LMP2 RNA and with small effects on specific cellular miRNA levels but protein levels of LMP1 and LMP2A were not affected. Wild type and EBER deletion EBV had approximately equal ability to infect immunodeficient mice reconstituted with a human haematopoietic system.
  • Journal article
    McCallin AJ, Maertens GN, Bangham CRM, 2015,

    Host determinants of HTLV-1 integration site preference

    , RETROVIROLOGY, Vol: 12, ISSN: 1742-4690
  • Journal article
    Serwa R, Krause E, Abaitua F, Tate EW, O'Hare PFet al., 2015,

    Systems analysis of protein fatty acylation in herpes simplex virus infected cells using chemical proteomics.

    , Chemistry & Biology, Vol: 22, Pages: 1008-1017, ISSN: 1074-5521

    Protein fatty acylation regulates diverse aspects of cellular function and organization and plays a key role in host immune responses to infection. Acylation also modulates the function and localization of virus-encoded proteins. Here, we employ chemical proteomics tools, bio-orthogonal probes, and capture reagents to study myristoylation and palmitoylation during infection with herpes simplex virus (HSV). Using in-gel fluorescence imaging and quantitative mass spectrometry, we demonstrate a generalized reduction in myristoylation of host proteins, whereas palmitoylation of host proteins, including regulators of interferon and tetraspanin family proteins, was selectively repressed. Furthermore, we found that a significant fraction of the viral proteome undergoes palmitoylation; we identified a number of virus membrane glycoproteins, structural proteins, and kinases. Taken together, our results provide broad oversight of protein acylation during HSV infection, a roadmap for similar analysis in other systems, and a resource with which to pursue specific analysis of systems and functions.
  • Journal article
    Brady G, Haas DA, Farrell PJ, Pichlmair A, Bowie AGet al., 2015,

    Poxvirus Protein MC132 from Molluscum Contagiosum Virus Inhibits NF-kappa B Activation by Targeting p65 for Degradation

    , JOURNAL OF VIROLOGY, Vol: 89, Pages: 8406-8415, ISSN: 0022-538X
  • Journal article
    Elderfield RA, Parker L, Stilwell P, Roberts KL, Schepelmann S, Barclay WSet al., 2015,

    Ferret airway epithelial cell cultures support efficient replication of influenza B virus but not mumps virus

    , JOURNAL OF GENERAL VIROLOGY, Vol: 96, Pages: 2092-2098, ISSN: 0022-1317

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