Food Safety
Online ISSN : 2187-8404
ISSN-L : 2187-8404
Volume 4 , Issue 4
Showing 1-10 articles out of 10 articles from the selected issue
Editorial
Reviews
  • Juan Maria Torres, Alba Marin-Moreno, Olivier Andreoletti, Juan-Carlos ...
    Type: Review
    2016 Volume 4 Issue 4 Pages 105-109
    Published: 2016
    Released: December 22, 2016
    [Advance publication] Released: December 07, 2016
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    Dietary exposure to Bovine Spongiform Encephalopathy (BSE) contaminated bovine tissues is considered as the origin of variant Creutzfeldt-Jakob disease (vCJD) in humans. To date, BSE agent is the only recognized zoonotic prion. Despite the variety of transmissible spongiform encephalopathy (TSE) agents that have been circulating for centuries in farmed ruminants, there is no apparent epidemiological link between exposure to ruminant products and the occurrence of other form of TSE in human like sporadic Creutzfeldt-Jakob disease (sCJD). However, the zoonotic potential of the diversity of circulating TSE agents has never been systematically assessed. The major issue in experimental assessment of TSEs zoonotic potential lies in the modelling of the “species barrier,” the biological phenomenon that limits TSE agents’ propagation from one species to another. In the past decade, mice genetically engineered to express normal forms of the human prion protein have proven to be essential in studying human prions pathogenesis and modelling the capacity of TSEs to cross the human species barrier.

    To assess the zoonotic potential of prions circulating in farmed ruminants, we study their transmission ability in transgenic mice expressing human PrPC (HuPrP-Tg). Two lines of mice expressing different forms of the human PrPC (129Met or 129Val) are used to determine the role of the Met129Val dimorphism in susceptibility/resistance to the different agents.

    These transmission experiments confirm the ability of BSE prions to propagate in 129M-HuPrP-Tg mice and demonstrate that Met129 homozygotes may be susceptible to BSE in sheep or goats to a greater degree than the BSE agent in cattle, and that these agents can convey molecular properties and be neuropathologically indistinguishable from vCJD. However, homozygous 129V mice are resistant to all tested BSE derived prions independently of the originating species, suggesting a higher transmission barrier for 129V-PrP variant.

    Transmission data also revealed that several scrapie prions propagate in HuPrP-Tg mice with efficiency comparable to that of cattle BSE. While the efficiency of transmission at primary passage was low, subsequent passages resulted in a highly virulent prion disease in both Met129 and Val129 mice. Transmission of the different scrapie isolates in these mice leads to the emergence of prion strain phenotypes that showed similar characteristics to those displayed by MM1 or VV2 sCJD prion. These results demonstrate that scrapie prions have a zoonotic potential and raise new questions about the possible link between animal and human prions.

  • Justin J. Greenlee, Robert A. Kunkle, Jodi D. Smith, M. Heather West G ...
    Type: Review
    2016 Volume 4 Issue 4 Pages 110-114
    Published: 2016
    Released: December 22, 2016
    [Advance publication] Released: December 07, 2016
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    A naturally occurring prion disease has not been recognized in swine, but the agent of bovine spongiform encephalopathy does transmit to swine by experimental routes. Swine are thought to have a robust species barrier when exposed to the naturally occurring prion diseases of other species, but the susceptibility of swine to the agent of sheep scrapie has not been thoroughly tested. We conducted this experiment to test the susceptibility of swine to U.S. scrapie isolates by intracranial and oral inoculation. Scrapie inoculum was a pooled 10% (w/v) homogenate derived from the brains of clinically ill sheep from the 4th passage of a serial passage study of the U.S scrapie agent (No. 13–7) through susceptible sheep (homozygous ARQ at prion protein residues 136, 154, and 171, respectively). Pigs were inoculated intracranially (n=19) with a single 0.75 mL dose or orally (n=24) with 15 mL repeated on 4 consecutive days. Necropsies were done on a subset of animals at approximately six months post inoculation (PI): the time the pigs were expected to reach market weight. Remaining pigs were maintained and monitored for clinical signs of transmissible spongiform encephalopathies (TSE) until study termination at 80 months PI or when removed due to intercurrent disease (primarily lameness). Brain samples were examined by immunohistochemistry (IHC), western blot (WB), enzyme immunoassay (EIA), and for a subset of pigs in each inoculation group, bioassay in mice expressing porcine prion protein. At six-months PI, no evidence of scrapie infection was noted by any diagnostic method. However, at 51 months of incubation or greater, 5 animals were positive by one or more methods: IHC (n=4), WB (n=3), or EIA (n=4). Furthermore, positive bioassay results were obtained from all inoculated groups (oral and intracranial; market weight and end of study) suggesting that swine are potential hosts for the agent of scrapie.

  • Steven Collins, Shannon Sarros
    Type: Review
    2016 Volume 4 Issue 4 Pages 115-120
    Published: 2016
    Released: December 22, 2016
    [Advance publication] Released: December 07, 2016
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    Prion diseases are neurodegenerative diseases affecting both humans and animal species. The phenotypic spectrum is broad and includes Creutzfeldt-Jakob disease (CJD) and its variant zoonotic form (vCJD) in humans, while in animals, scrapie of sheep and goats, bovine spongiform encephalopathy and chronic wasting disease of deer, elk and moose are naturally occurring forms. Transmission and pathogenesis appear causally linked to the misfolding of the normal form of the prion protein (PrPC) into disease associated conformers (PrPD), the latter enriched in β-strand secondary structure.

    Over the past 10 years two protein amplification techniques, the protein misfolding cyclic amplification (PMCA) assay and real-time quaking induced conversion (RT-QuIC) assay have been developed and successfully deployed in prion biology across a range of scientific and clinical applications, including generation of de novo prions, quantitation of prion infectivity and ultra-sensitive detection of PrPD. While PMCA utilises sonication to facilitate protein amplification, RT-QuIC employs vigorous shaking to achieve this outcome, with both techniques sharing the ability to amplify miniscule quantities of PrPD seed present in various tissues and body fluids to levels detectable using routine biochemical methods.

    The enhanced specificity of the RT-QuIC for detection of PrPD in cerebrospinal fluid (CSF) has spawned international collaborations to rigorously assess and validate the assay for clinical diagnostic purposes. In parallel with collaborative CSF validation studies have been successful efforts to refine the RT-QuIC allowing its use for more accessible body fluids or tissues such as urine and nasal brushings, as well as promote higher sample throughput, shorten assay times and offer accurate quantification of PrPD even at levels below those detectable by animal bioassays. Animal studies support the generic capacity of the RT-QuIC for PrPD detection, underpinning the utility of this assay for studying prion disease and the high likelihood of inter-convertibility of technical refinements for human and animal use.

  • Anne Balkema-Buschmann, Grit Priemer, Markus Keller, Maria Mazza, Bob ...
    Type: Review
    2016 Volume 4 Issue 4 Pages 121-129
    Published: 2016
    Released: December 22, 2016
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    After the detection of the first cases of atypical bovine spongiform encephalopathy (BSE) more than ten years ago, the etiology, pathogenesis and agent distribution of these novel BSE forms in cattle were completely unknown. Many studies have been performed in the meantime to elucidate the pathogenic mechanisms of these diseases. A wealth of data has been accumulated regarding the distribution of the abnormal isoform of the prion protein, PrPSc, in tissues of affected cattle, confirming the general restriction of the PrPSc and agent distribution to the central and peripheral nervous system, albeit at slightly higher levels as compared to classical BSE. However, due to lack of data, the assumptions regarding the spontaneous etiology of both atypical BSE forms (H-BSE and L-BSE) and also the origin of the classical BSE epidemic are still mainly speculative. By performing subpassage experiments of both the atypical BSE forms in a variety of conventional and transgenic mice and Syrian Gold hamsters, we aimed to improve our understanding of the strain stability of these BSE forms. It turned out that under these experimental conditions, both the atypical BSE forms may alter their phenotypes and become indistinguishable from classical BSE. Information about the classical and atypical BSE strain characteristics help to improve our understanding of the correlation between all three BSE forms.

  • Elena Vallino Costassa, Barbara Iulini*, Maria Mazza, Pierluigi Acutis ...
    Type: Review
    2016 Volume 4 Issue 4 Pages 130-134
    Published: 2016
    Released: December 22, 2016
    [Advance publication] Released: December 07, 2016
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    Many mammalian species can be affected by prion diseases, also known as transmissible spongiform encephalopathies (TSEs). “Classical” bovine spongiform encephalopathy (C-BSE) was the first prion disease recognized in cattle and it is the only known zoonotic prion disease, having caused variant Creutzfeldt-Jakob disease (vCJD) in humans. Based on the biochemical signatures of disease-associated prion protein (PrPSc), two distinct forms of atypical bovine spongiform encephalopathies (H-BSE and L-BSE) have been distinguished from C-BSE since 2004. To date there is no comprehensive information about the origin of atypical BSEs (sporadic vs. acquired) and this has an influence on the interpretation of the knowledge gathered from experimental studies, regarding how well such models may represent the real distribution of the agent in the body of naturally affected animals. Moreover, there are only very limited data available concerning the pathogenesis of both atypical BSE forms, as compared to C-BSE. Thus, precautions that are presently taken to minimize the risk of prion contamination of the food supply might not be as effective at preventing the spread of these recently recognized strains. In the last few years a wide range of experimental transmission studies of atypical strains in different animal hosts have been performed. The most recent data on classical and atypical BSE studies concerning characteristics, pathogenesis and transmissions in cattle will be summarized in this review.

  • Jean C. Manson, Abigail B. Diack
    Type: Review
    2016 Volume 4 Issue 4 Pages 135-141
    Published: 2016
    Released: December 22, 2016
    [Advance publication] Released: December 07, 2016
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    A Transmissible Spongiform Encephalopathy (TSE) agent from one species generally transmits poorly to a new species, a phenomenon known as the species barrier. However once in the new species it generally but not always adapts and then more readily transmits within the new host. No single test is available to determine accurately the ability of a prion strain to transmit between species. Evaluating the species barrier for any prion strain has to take into consideration as much information as can be gathered for that strain from surveillance and research. The interactions of the agent with a particular host can be measured by in vivo and in vitro methods and assessing the species barrier needs to make full use of all the tools available. This review will identify the important considerations that need to be made when evaluating the species barrier.

Risk assessment report: Guidelines
Risk Assessment Report: Genetically Modified Foods and Feeds
  • Summary
    Food Safety Commission of Japan
    Type: RAR (Summary)
    2016 Volume 4 Issue 4 Pages 169-172
    Published: 2016
    Released: December 22, 2016
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    The Food Safety Commission of Japan (FSCJ) conducted a safety assessment of soybean lines generated through cross-breeding of MON87705, MON87708 and MON89788, based on the documents submitted by the applicant. The safety assessment of all the three parental lines and the MON87705 × MON89788 line had been completed as no safety concern. The safety assessment was judged unnecessary for the MON87708 × MON89788 line. The data and information submitted by the applicant were reviewed from the various points, including the safety of the inserted genes, the induction of allergenicity, the stability of the introduced genes in the progeny, and especially the possible influences of the expressed gene products on the metabolic pathway and the contents of nutritional and hazardous components. It was considered that either trait was independent of the other traits, regardless of the crossings. Consequently, FSCJ thus concluded that the MON87705 × MON87708 × MON89788 and MON87705 × MON87708 soybean lines showed no safety concern relevant to human health.

Risk assessment report: Veterinary Medicinal Products
  • Summary
    Food Safety Commission of Japan
    Type: RAR (Summary)
    2016 Volume 4 Issue 4 Pages 173-174
    Published: 2016
    Released: December 22, 2016
    JOURNALS FREE ACCESS FULL-TEXT HTML

    The Food Safety Commission of Japan (FSCJ) conducted a risk assessment of triptorelin acetate (CAS No. 140194-24-7), which is intended for use in a single fixed-time insemination by synchronizing estrus cycles of weaned sows, based on the documents for the import tolerance application. FSCJ recognize none of adverse effects of triptorelin acetate on human health through dietary exposure, because of the lack of genotoxicity relevant to human health and negligible oral bioavailability due to the degradation in the digestive tract. FSCJ thus judged it unnecessary to establish an acceptable daily intake (ADI) for triptorelin acetate.

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