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Dietetics, Nutrition and Biological Sciences

Permanent URI for this collectionhttps://eresearch.qmu.ac.uk/handle/20.500.12289/23

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Author: search.filters.author.Barron, RonaHas files: No

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Now showing 1 - 10 of 29
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    A gene-targeted mouse model of P102L Gerstmann-Sträussler-Scheinker syndrome
    (Elsevier, 2003-03) Barron, Rona; Manson, Jean C.
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    The 101L mutation in murine PrP can alter transmission across three species barriers
    (2002) Barron, Rona; Jamieson, Elizabeth; Thomson, Val; Melton, David W.; Will, Robert; Ironside, James; Manson, Jean C.
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    Gene Targeting the PrP Gene
    (Horizon Bioscience, 2004) Barron, Rona; Manson, Jean C.
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    Knockouts, Knockins, Transgenics and Transplants in Prion Research
    (Cold Spring Harbor Laboratory Press, 2004) Weissman, C; Fleschig, E; Barron, Rona; Aguzzi, A; Manson, Jean C.
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    The transmissible spongiform encephalopathies.
    (Cambridge University Press, 2005-04) Manson, Jean C.; Barron, Rona; Diggard, P.; Nash, A.A.; Randall, R.E.
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    The role of host PrP in control of incubation time
    (Springer Verlag, 2005) Manson, Jean C.; Barron, Rona; Hart, Patricia; Tuzi, Nadia L.; Bishop, Matthew T.
    PrP is central to TSE disease and has been hypothesised to be the infectious agent. Polymorphisms in the PrP gene are associated with different incubation times of disease following exposure to an infectious agent and mutations in the human PrP gene can apparently lead to spontaneous genetic disease. Strains of TSE agent are proposed to be generated and maintained through differences in glycosylation or conformation of PrP and the barrier to infection between species is thought to be due to the differences in the sequence of PrP between different species. To test these hypotheses, we have introduced specific modifications into the endogenous mouse Prnp gene by gene targeting. The mutated PrP gene is in the correct location under the control of the endogenous Prnp regulatory sequences and thus expressed in the same tissues and amounts as the wild type Prnp gene. By altering the murine PrP coding region to that of another species we have established that increasing overall identity between host and donor PrP can lead to either an increase or a decrease in incubation time of disease in a strain dependent manner. We have introduced a point mutation (101L) into the N-terminus of the host PrP and shown that it dramatically changes the susceptibility of the host to infection from different species. We have in addition demonstrated that polymorphisms in the N terminus (L108T) and C-terminus (F189V) of host PrP both alter the incubation time of disease. We have in addition introduced mutations into the Prnp gene which prevent glycosylation at each or both of the two N-linked glycosylation sites of PrP. Inoculation of these mice with infectivity has established that glycosylation of host PrP can influence incubation time of disease, vacuolar pathology and strain determination.
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    The transmissible spongiform encephalopathies: emerging and declining epidemics
    (Portland Press, 2006-10-25) Manson, Jean C.; Cancellotti, Enrico; Bishop, Matthew T.; Hart, Patricia; Barron, Rona
    TSEs (transmissible spongiform encephalopathies) are neurodegenerative diseases of various mammalian species, the best known of which include BSE (bovine spongiform encephalopathies) in cattle, CJD (Creutzfeldt–Jakob disease) in humans, scrapie in sheep and CWD (chronic wasting disease) in deer. This review examines the emergence of various TSE strains and their transmission, and discusses disease surveillance and control.
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    The nature of the prion
    (2009) Barron, Rona
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    The relationship between PrPSc and TSE infectivity
    (Research Signpost, 2011) Barron, Rona
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    Identification and characterization of a putative serine protease expressed in vivo by Mycobacterium avium subsp. paratuberculosis
    (Microbiology Society, 1994-08-01) Barron, Rona; Stevenson, Karen; Inglis, Neil F.; Klausen, Joan; Sharp, J. Michael
    A putative serine protease expressed in vivo by Mycobacterium avium subsp. paratuberculosis was isolated from a lambda gt11 genomic expression library by screening with serum from a naturally infected sheep. The gene was contained in two overlapping clones, which were shown by antibody elution to encode a protein of 34 kDa in M. a. paratuberculosis. The clones were sequenced and database searches detected a motif identical to the active serine site in trypsin, and 30% homology to the putative serine proteases (HtrA proteins) of Escherichia coli, Salmonella typhimurium, Brucella abortus and Rochalimaea henselae.