共查询到9条相似文献,搜索用时 15 毫秒
1.
Jean Yves Douet Saima Zafar Armand Perret-Liaudet Caroline Lacroux Séverine Lugan Naima Aron Herve Cassard Claudia Ponto Fabien Corbière Juan Maria Torres Inga Zerr Olivier Andreoletti 《Emerging infectious diseases》2014,20(1):114-117
We report the presence of infectivity in erythrocytes, leukocytes, and plasma of 1 person with variant Creutzfeldt-Jakob disease and in the plasma of 2 in 4 persons whose tests were positive for sporadic Creutzfeldt-Jakob disease. The measured infectivity levels were comparable to those reported in various animals with transmissible spongiform encephalopathies. 相似文献
2.
Judith Montag Walter Schulz-Schaeffer Annette Schrod Gerhard Hunsmann Dirk Motzkus 《Emerging infectious diseases》2013,19(7):1125-1127
To estimate the effect of the variability of prion disease onset on primary bovine spongiform encephalopathy transmission to humans, we studied 6 cynomolgus macaques. The preclinical incubation period was significantly prolonged in 2 animals, implying that onset of variant Creutzfeldt-Jacob disease in humans could be more diverse than previously expected. 相似文献
3.
Jonathan D.F. Wadsworth Susan Joiner Jacqueline M. Linehan Anne Balkema-Buschmann John Spiropoulos Marion M. Simmons Peter C. Griffiths Martin H. Groschup James Hope Sebastian Brandner Emmanuel A. Asante John Collinge 《Emerging infectious diseases》2013,19(11):1731-1739
Public and animal health controls to limit human exposure to animal prions are focused on bovine spongiform encephalopathy (BSE), but other prion strains in ruminants may also have zoonotic potential. One example is atypical/Nor98 scrapie, which evaded statutory diagnostic methods worldwide until the early 2000s. To investigate whether sheep infected with scrapie prions could be another source of infection, we inoculated transgenic mice that overexpressed human prion protein with brain tissue from sheep with natural field cases of classical and atypical scrapie, sheep with experimental BSE, and cattle with BSE. We found that these mice were susceptible to BSE prions, but disease did not develop after prolonged postinoculation periods when mice were inoculated with classical or atypical scrapie prions. These data are consistent with the conclusion that prion disease is less likely to develop in humans after exposure to naturally occurring prions of sheep than after exposure to epizootic BSE prions of ruminants. 相似文献
4.
Abigail B. Diack Diane L. Ritchie Alexander H. Peden Deborah Brown Aileen Boyle Laura Morabito David Maclennan Paul Burgoyne Casper Jansen Richard S. Knight Pedro Piccardo James W. Ironside Jean C. Manson 《Emerging infectious diseases》2014,20(12):1969-1979
Variably protease-sensitive prionopathy (VPSPr) can occur in persons of all codon 129 genotypes in the human prion protein gene (PRNP) and is characterized by a unique biochemical profile when compared with other human prion diseases. We investigated transmission properties of VPSPr by inoculating transgenic mice expressing human PRNP with brain tissue from 2 persons with the valine-homozygous (VV) and 1 with the heterozygous methionine/valine codon 129 genotype. No clinical signs or vacuolar pathology were observed in any inoculated mice. Small deposits of prion protein accumulated in the brains of inoculated mice after challenge with brain material from VV VPSPr patients. Some of these deposits resembled microplaques that occur in the brains of VPSPr patients. Comparison of these transmission properties with those of sporadic Creutzfeldt-Jakob disease in the same lines of mice indicated that VPSPr has distinct biological properties. Moreover, we established that VPSPr has limited potential for human-to-human transmission. 相似文献
5.
Notari S Qing L Pocchiari M Dagdanova A Hatcher K Dogterom A Groisman JF Lumholtz IB Puopolo M Lasmezas C Chen SG Kong Q Gambetti P 《Emerging infectious diseases》2012,18(1):21-28
Prion diseases are neurodegenerative conditions associated with a misfolded and infectious protein, scrapie prion protein (PrP(Sc)). PrP(Sc) propagate prion diseases within and between species and thus pose risks to public health. Prion infectivity or PrP(Sc) presence has been demonstrated in urine of experimentally infected animals, but there are no recent studies of urine from patients with Creutzfeldt-Jakob disease (CJD). We performed bioassays in transgenic mice expressing human PrP to assess prion infectivity in urine from patients affected by a common subtype of sporadic CJD, sCJDMM1. We tested raw urine and 100-fold concentrated and dialyzed urine and assessed the sensitivity of the bioassay along with the effect of concentration and dialysis on prion infectivity. Intracerebral inoculation of transgenic mice with urine from 3 sCJDMM1 patients failed to demonstrate prion disease transmission, indicating that prion infectivity in urine from sCJDMM1 patients is either not present or is <0.38 infectious units/mL. 相似文献
6.
Chronic wasting disease (CWD) is a fatal, transmissible prion disease that affects captive and free-ranging deer, elk, and moose. Although the zoonotic potential of CWD is considered low, identification of multiple CWD strains and the potential for agent evolution upon serial passage hinders a definitive conclusion. Surveillance for CWD in free-ranging populations has documented a continual geographic spread of the disease throughout North America. CWD prions are shed from clinically and preclinically affected hosts, and CWD transmission is mediated at least in part by the environment, perhaps by soil. Much remains unknown, including the sites and mechanisms of prion uptake in the naive host. There are no therapeutics or effective eradication measures for CWD-endemic populations. Continued surveillance and research of CWD and its effects on cervid ecosystems is vital for controlling the long-term consequences of this emerging disease. 相似文献
7.
Susanne Krasemann Giulia Mearini Elisabeth Kr?mer Katja Wagenführ Walter Schulz-Schaeffer Melanie Neumann Walter Bodemer Franz-Josef Kaup Michael Beekes Lucie Carrier Adriano Aguzzi Markus Glatzel 《Emerging infectious diseases》2013,19(6):985-988
Prion amyloidosis occurred in the heart of 1 of 3 macaques intraperitoneally inoculated with bovine spongiform encephalopathy prions. This macaque had a remarkably long duration of disease and signs of cardiac distress. Variant Creutzfeldt-Jakob disease, caused by transmission of bovine spongiform encephalopathy to humans, may manifest with cardiac symptoms from prion-amyloid cardiomyopathy. 相似文献
8.
Marcelo A. Barria Aru Balachandran Masanori Morita Tetsuyuki Kitamoto Rona Barron Jean Manson Richard Knight James W. Ironside Mark W. Head 《Emerging infectious diseases》2014,20(1):88-97
The risks posed to human health by individual animal prion diseases cannot be determined a priori and are difficult to address empirically. The fundamental event in prion disease pathogenesis is thought to be the seeded conversion of normal prion protein to its pathologic isoform. We used a rapid molecular conversion assay (protein misfolding cyclic amplification) to test whether brain homogenates from specimens of classical bovine spongiform encephalopathy (BSE), atypical BSE (H-type BSE and L-type BSE), classical scrapie, atypical scrapie, and chronic wasting disease can convert normal human prion protein to the abnormal disease-associated form. None of the tested prion isolates from diseased animals were as efficient as classical BSE in converting human prion protein. However, in the case of chronic wasting disease, there was no absolute barrier to conversion of the human prion protein. 相似文献
9.
Juan-María Torres Joaquín Castilla Belén Pintado Alfonso Gutiérrez-Adan Olivier Andréoletti Patricia Aguilar-Calvo Ana-Isabel Arroba Beatriz Parra-Arrondo Isidro Ferrer Jorge Manzanares Juan-Carlos Espinosa 《Emerging infectious diseases》2013,19(12):1938-1947
We generated transgenic mice expressing bovine cellular prion protein (PrPC) with a leucine substitution at codon 113 (113L). This protein is homologous to human protein with mutation 102L, and its genetic link with Gerstmann–Sträussler–Scheinker syndrome has been established. This mutation in bovine PrPC causes a fully penetrant, lethal, spongiform encephalopathy. This genetic disease was transmitted by intracerebral inoculation of brain homogenate from ill mice expressing mutant bovine PrP to mice expressing wild-type bovine PrP, which indicated de novo generation of infectious prions. Our findings demonstrate that a single amino acid change in the PrPC sequence can induce spontaneous generation of an infectious prion disease that differs from all others identified in hosts expressing the same PrPC sequence. These observations support the view that a variety of infectious prion strains might spontaneously emerge in hosts displaying random genetic PrPC mutations. 相似文献