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  • 1
    Online Resource
    Online Resource
    Livestock and the promise of genomics
    Canadian Science Publishing ; 2013
    In:  Genome Vol. 56, No. 10 ( 2013-10), p. 556-566
    Details
    In: Genome, Canadian Science Publishing, Vol. 56, No. 10 ( 2013-10), p. 556-566
    Abstract: The emergence of the middle class in countries such as Brazil, Russia, India, and China is resulting in increasing global demand for animal-based food products. This increase represents a unique opportunity for Canadian livestock producers to export their products to new markets and expand Canada’s reputation as a global provider of safe and highest quality food items. This article has two major themes. First, current Canadian contributions to livestock genomics in the cattle and swine industries are outlined. Second, important future opportunities are discussed, including the high throughput collection of phenotypic data, development of environmentally friendly livestock, emergence of decision support software, and the use of Web 2.0. Through the use of genomic technologies, livestock producers can not only ensure that the nutritional demands of Canada are secured, but also play a pivotal role in ensuring the rest of the world is fed as well. Furthermore, investment through initiatives led by Genome Canada has ensured that Canada is favorably positioned to contribute cutting-edge solutions to meet this global challenge. Ultimately, genomic-based innovations will enable producers to increase efficiency, lower production costs, decrease the use of prophylactics, and limit the expenditure of resources.
    Type of Medium: Online Resource
    ISSN: 0831-2796 , 1480-3321
    URL: Article
    DOI: 10.1139/gen-2013-0080
    Language: English
    Publisher: Canadian Science Publishing
    Publication Date: 2013
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  • 2
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    A Francisella tularensis Pathogenicity Island Required for Intramacrophage Growth
    American Society for Microbiology ; 2004
    In:  Journal of Bacteriology Vol. 186, No. 19 ( 2004-10), p. 6430-6436
    Details
    In: Journal of Bacteriology, American Society for Microbiology, Vol. 186, No. 19 ( 2004-10), p. 6430-6436
    Abstract: Francisella tularensis is a gram-negative, facultative intracellular pathogen that causes the highly infectious zoonotic disease tularemia. We have discovered a ca. 30-kb pathogenicity island of F. tularensis (FPI) that includes four large open reading frames (ORFs) of 2.5 to 3.9 kb and 13 ORFs of 1.5 kb or smaller. Previously, two small genes located near the center of the FPI were shown to be needed for intramacrophage growth. In this work we show that two of the large ORFs, located toward the ends of the FPI, are needed for virulence. Although most genes in the FPI encode proteins with amino acid sequences that are highly conserved between high- and low-virulence strains, one of the FPI genes is present in highly virulent type A F. tularensis , absent in moderately virulent type B F. tularensis , and altered in F. tularensis subsp. novicida , which is highly virulent for mice but avirulent for humans. The G+C content of a 17.7-kb stretch of the FPI is 26.6%, which is 6.6% below the average G+C content of the F. tularensis genome. This extremely low G+C content suggests that the DNA was imported from a microbe with a very low G+C-containing chromosome.
    Type of Medium: Online Resource
    ISSN: 0021-9193 , 1098-5530
    URL: Article
    DOI: 10.1128/JB.186.19.6430-6436.2004
    Language: English
    Publisher: American Society for Microbiology
    Publication Date: 2004
    detail.hit.zdb_id: 1481988-0
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  • 3
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    The biochemical properties of the Francisella pathogenicity island (FPI)-encoded proteins IglA, IglB, IglC, PdpB and DotU suggest roles in type VI secretion
    Microbiology Society ; 2011
    In:  Microbiology Vol. 157, No. 12 ( 2011-12-01), p. 3483-3491
    Details
    In: Microbiology, Microbiology Society, Vol. 157, No. 12 ( 2011-12-01), p. 3483-3491
    Abstract: The Francisella pathogenicity island (FPI) encodes proteins thought to compose a type VI secretion system (T6SS) that is required for the intracellular growth of Francisella novicida . In this work we used deletion mutagenesis and genetic complementation to determine that the intracellular growth of F. novicida was dependent on 14 of the 18 genes in the FPI. The products of the iglABCD operon were localized by the biochemical fractionation of F. novicida, and Francisella tularensis LVS. Sucrose gradient separation of water-insoluble material showed that the FPI-encoded proteins IglA, IglB and IglC were found in multiple fractions, especially in a fraction that did not correspond to a known membrane fraction. We interpreted these data to suggest that IglA, IglB and IglC are part of a macromolecular structure. Analysis of published structural data suggested that IglC is an analogue of Hcp, which is thought to form long nano-tubes. Thus the fractionation properties of IglA, IglB and IglC are consistent with the current model of the T6SS apparatus, which supposes that IglA and IglB homologues form an outer tube structure that surrounds an inner tube composed of Hcp (IglC) subunits. Fractionation of F. novicida expressing FLAG-tagged DotU (IcmH homologue) and PdpB (IcmF homologue) showed that these proteins localize to the inner membrane. Deletion of dotU led to the cleavage of PdpB, suggesting an interaction of these two proteins that is consistent with results obtained with other T6SSs. Our results may provide a mechanistic basis for many of the studies that have examined the virulence properties of Francisella mutants in FPI genes, namely that the observed phenotypes of the mutants are the result of the disruption of the FPI-encoded T6SS structure.
    Type of Medium: Online Resource
    ISSN: 1350-0872 , 1465-2080
    URL: Article
    DOI: 10.1099/mic.0.052308-0
    Language: English
    Publisher: Microbiology Society
    Publication Date: 2011
    detail.hit.zdb_id: 2008736-6
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  • 4
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    Genetic elements for selection, deletion mutagenesis and complementation in Francisella spp.
    Oxford University Press (OUP) ; 2008
    In:  FEMS Microbiology Letters Vol. 278, No. 1 ( 2008-01), p. 86-93
    Details
    In: FEMS Microbiology Letters, Oxford University Press (OUP), Vol. 278, No. 1 ( 2008-01), p. 86-93
    Type of Medium: Online Resource
    ISSN: 0378-1097 , 1574-6968
    URL: Issue
    URL: Article
    DOI: 10.1111/fml.2008.278.issue-1
    DOI: 10.1111/j.1574-6968.2007.00979.x
    RVK:
    WA 15000
    Language: English
    Publisher: Oxford University Press (OUP)
    Publication Date: 2008
    detail.hit.zdb_id: 1501716-3
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  • 5
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    The Francisella pathogenicity island protein IglA localizes to the bacterial cytoplasm and is needed for intracellular growth
    Springer Science and Business Media LLC ; 2007
    In:  BMC Microbiology Vol. 7, No. 1 ( 2007-12)
    Details
    In: BMC Microbiology, Springer Science and Business Media LLC, Vol. 7, No. 1 ( 2007-12)
    Abstract: Francisella tularensis is a gram negative, facultative intracellular bacterium that is the etiological agent of tularemia. F. novicida is closely related to F. tularensis but has low virulence for humans while being highly virulent in mice. IglA is a 21 kDa protein encoded by a gene that is part of an iglABCD operon located on the Francisella pathogenicity island (FPI). Results Bioinformatics analysis of the FPI suggests that IglA and IglB are components of a newly described type VI secretion system. In this study, we showed that IglA regulation is controlled by the global regulators MglA and MglB. During intracellular growth IglA production reaches a maximum at about 10 hours post infection. Biochemical fractionation showed that IglA is a soluble cytoplasmic protein and immunoprecipitation experiments demonstrate that it interacts with the downstream-encoded IglB. When the iglB gene was disrupted IglA could not be detected in cell extracts of F. novicida , although IglC could be detected. We further demonstrated that IglA is needed for intracellular growth of F. novicida . A non-polar iglA deletion mutant was defective for growth in mouse macrophage-like cells, and in cis complementation largely restored the wild type macrophage growth phenotype. Conclusion The results of this study demonstrate that IglA and IglB are interacting cytoplasmic proteins that are required for intramacrophage growth. The significance of the interaction may be to secrete effector molecules that affect host cell processes.
    Type of Medium: Online Resource
    ISSN: 1471-2180
    URL: Article
    DOI: 10.1186/1471-2180-7-1
    Language: English
    Publisher: Springer Science and Business Media LLC
    Publication Date: 2007
    detail.hit.zdb_id: 2041505-9
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  • 6
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    The Francisella Pathogenicity Island Protein PdpD Is Required for Full Virulence and Associates with Homologues of the Type VI Secretion System
    American Society for Microbiology ; 2008
    In:  Journal of Bacteriology Vol. 190, No. 13 ( 2008-07), p. 4584-4595
    Details
    In: Journal of Bacteriology, American Society for Microbiology, Vol. 190, No. 13 ( 2008-07), p. 4584-4595
    Abstract: Francisella tularensis is a highly infectious, facultative intracellular bacterial pathogen that is the causative agent of tularemia. Nearly a century ago, researchers observed that tularemia was often fatal in North America but almost never fatal in Europe and Asia. The chromosomes of F. tularensis strains carry two identical copies of the Francisella pathogenicity island (FPI), and the FPIs of North America-specific biotypes contain two genes, anmK and pdpD , that are not found in biotypes that are distributed over the entire Northern Hemisphere. In this work, we studied the contribution of anmK and pdpD to virulence by using F. novicida , which is very closely related to F. tularensis but which carries only one copy of the FPI. We showed that anmK and pdpD are necessary for full virulence but not for intracellular growth. This is in sharp contrast to most other FPI genes that have been studied to date, which are required for intracellular growth. We also showed that PdpD is localized to the outer membrane. Further, overexpression of PdpD affects the cellular distribution of FPI-encoded proteins IglA, IglB, and IglC. Finally, deletions of FPI genes encoding proteins that are homologues of known components of type VI secretion systems abolished the altered distribution of IglC and the outer membrane localization of PdpD.
    Type of Medium: Online Resource
    ISSN: 0021-9193 , 1098-5530
    URL: Article
    DOI: 10.1128/JB.00198-08
    Language: English
    Publisher: American Society for Microbiology
    Publication Date: 2008
    detail.hit.zdb_id: 1481988-0
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  • 7
    Online Resource
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    Characterization of the pathogenicity island protein PdpA and its role in the virulence of Francisella novicida
    Microbiology Society ; 2009
    In:  Microbiology Vol. 155, No. 5 ( 2009-05-01), p. 1489-1497
    Details
    In: Microbiology, Microbiology Society, Vol. 155, No. 5 ( 2009-05-01), p. 1489-1497
    Abstract: Francisella tularensis is a highly virulent, intracellular pathogen that causes the disease tularaemia. A research surrogate for F. tularensis is Francisella novicida , which causes a tularaemia-like disease in mice, grows similarly in macrophages, and yet is unable to cause disease in humans. Both Francisella species contain a cluster of genes referred to as the Francisella pathogenicity island (FPI). Pathogenicity determinant protein A (PdpA), encoded by the pdpA gene, is located within the FPI and has been associated with the virulence of Francisella species. In this work we examined the properties of PdpA protein expression and localization as well as the phenotype of a F. novicida pdpA deletion mutant. Monoclonal antibody detection of PdpA showed that it is a soluble protein that is upregulated in iron-limiting conditions and undetectable in an mglA or mglB mutant background. Deletion of pdpA resulted in a strain that was highly attenuated for virulence in chicken embryos and mice.
    Type of Medium: Online Resource
    ISSN: 1350-0872 , 1465-2080
    URL: Article
    DOI: 10.1099/mic.0.025379-0
    Language: English
    Publisher: Microbiology Society
    Publication Date: 2009
    detail.hit.zdb_id: 2008736-6
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