490 research outputs found

    Comparative genomics among members of the Streptococcus bovis/Streptococcus equinus complex

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    Background: Today, only one streptococcal species, i.e. Streptococcus thermophilus is recognized as food-grade. Interestingly, other streptococci like Streptococcus macedonicus and Streptococcus infantarius belonging to the Streptococcus bovis/Streptococcus equinus complex (SBSEC) are also found in food matrices. However, these species are phylogenetically related to Streptococcus gallolyticus and Streptococcus pasteurianus that have been linked to endocarditis, bacteremia and colon cancer. Objectives: To compare the available genomes of the members of the SBSEC in order to shed light onto their evolution and phylogenetic relation and to assess in silico their pathogenic potential. Methods: Comparative genomics analysis including full chromosome and CDS alignments, whole genome phylogeny and evaluation of gene content (e.g. core genome, singletons, etc.) was performed with appropriate bioinformatics tools. Conclusions: Despite the fact that the four species of the SBSEC were found tightly related based on whole genome phylogeny, there were two different patterns of evolution among them. Streptococcus pasteurianus, S. macedonicus and S. infantarius seem to have undergone a reductive evolution process that resulted in significantly diminished genome sizes and increased percentages of potential pseudogenes when compared to S. gallolyticus. In addition, S. pasteurianus, S. macedonicus and S. infantarius seem to have lost several genes previously linked to the ability of S. gallolyticus to survive in the gastrointestinal tract of herbivores and to its pathogenicity. Our findings indicate differences in the ecological niche and the pathogenic potential among the four species

    Cosmology with a long range repulsive force

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    We consider a class of cosmological models in which the universe is filled with a (non-electric) charge density that repels itself by means of a force carried by a vector boson with a tiny mass. When the vector's mass depends upon other fields, the repulsive interaction gives rise to an electromagnetic barrier which prevents these fields from driving the mass to zero. This can modify the cosmology dramatically. We present a very simple realization of this idea in which the vector's mass arises from a scalar field. The electromagnetic barrier prevents this field from rolling down its potential and thereby leads to accelerated expansion.Comment: 15 pages, 8 figures, LaTeX (version accepted for publication in PRD). 3 new figures, extended discussion of observational consequence

    Electronic excitation of furfural as probed by high-resolution vacuum ultraviolet spectroscopy, electron energy loss spectroscopy, and ab initio calculations

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    13 págs.; 7 figs.; 8 tabs.© 2015 AIP Publishing LLC. The electronic spectroscopy of isolated furfural (2-furaldehyde) in the gas phase has been investigated using high-resolution photoabsorption spectroscopy in the 3.5-10.8 eV energy-range, with absolute cross section measurements derived. Electron energy loss spectra are also measured over a range of kinematical conditions. Those energy loss spectra are used to derive differential cross sections and in turn generalised oscillator strengths. These experiments are supported by ab initio calculations in order to assign the excited states of the neutral molecule. The good agreement between the theoretical results and the measurements allows us to provide the first quantitative assignment of the electronic state spectroscopy of furfural over an extended energy range.F.F.S. and P.L.V. acknowledge the Portuguese Foundation for Science and Technology (FCT-MEC) through Grant Nos. SFRH/BPD/68979/2010 and SFRH/BSAB/105792/2014, respectively, the research Grant Nos. PTDC/FIS-ATO/1832/ 2012 and UID/FIS/00068/2013. P.L.V. also acknowledges his Visiting Research Fellow position at Flinders University, Adelaide, South Australia. The Patrimoine of the University of Liège, the Fonds National de la Recherche Scientifique, and the Fonds de la Recherche Fondamentale Collective of Belgium have also supported this research. E.L. and R.F.C.N. thank CNPq (Brazil) and the Science Without Borders Programme for opportunities to study abroad. The authors wish to acknowledge the beam time at the ISA synchrotron at Aarhus University, Denmark. The research leading to these results has received funding from the European Community’s Seventh Framework Programme (Grant No. FP7/2007-2013) CALIPSO under Grant Agreement No. 312284. D.B.J. thanks the Australian Research Council for financial support provided through a Discovery Early Career Research Award. M.J.B. also thanks the Australian Research Council for some financial support, while M.J.B. and M.C.A.L. acknowledge the Brazilian agencies CNPq and FAPEMIG for financial support. F.B. and G.G. acknowledge partial financial support from the Spanish Ministry MINECO (Project No. FIS2012-31230) and the EU COST Action No. CM1301 (CELINA). Finally, R.F.C., M.T.do N.V., M.H.F.B., and M.A.P.L. acknowledge support from the Brazilian agency CNPq.Peer Reviewe

    Ticks produce highly selective chemokine binding proteins with antiinflammatory activity

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    Bloodsucking parasites such as ticks have evolved a wide variety of immunomodulatory proteins that are secreted in their saliva, allowing them to feed for long periods of time without being detected by the host immune system. One possible strategy used by ticks to evade the host immune response is to produce proteins that selectively bind and neutralize the chemokines that normally recruit cells of the innate immune system that protect the host from parasites. We have identified distinct cDNAs encoding novel chemokine binding proteins (CHPBs), which we have termed Evasins, using an expression cloning approach. These CHBPs have unusually stringent chemokine selectivity, differentiating them from broader spectrum viral CHBPs. Evasin-1 binds to CCL3, CCL4, and CCL18; Evasin-3 binds to CXCL8 and CXCL1; and Evasin-4 binds to CCL5 and CCL11. We report the characterization of Evasin-1 and -3, which are unrelated in primary sequence and tertiary structure, and reveal novel folds. Administration of recombinant Evasin-1 and -3 in animal models of disease demonstrates that they have potent antiinflammatory properties. These novel CHBPs designed by nature are even smaller than the recently described single-domain antibodies (Hollinger, P., and P.J. Hudson. 2005. Nat. Biotechnol. 23:1126–1136), and may be therapeutically useful as novel antiinflammatory agents in the future
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