scholarly journals Experimental Infection of Cattle With a Novel Prion Derived From Atypical H-Type Bovine Spongiform Encephalopathy

2017 ◽  
Vol 54 (6) ◽  
pp. 892-900 ◽  
Author(s):  
Hiroyuki Okada ◽  
Kentaro Masujin ◽  
Kohtaro Miyazawa ◽  
Yoshifumi Iwamaru ◽  
Morikazu Imamura ◽  
...  
Keyword(s):  
Bovine Spongiform Encephalopathy ◽  
Cauda Equina ◽  
Brain Homogenate ◽  
Biochemical Properties ◽  
Spongiform Encephalopathy ◽  
Infected Cattle ◽  
Atypical Form ◽  
Pathologic Features ◽  
Topographical Distribution ◽  
The Brain

H-type bovine spongiform encephalopathy (H-BSE) is an atypical form of BSE in cattle. During passaging of H-BSE in transgenic bovinized (TgBoPrP) mice, a novel phenotype of BSE, termed BSE-SW emerged and was characterized by a short incubation time and host weight loss. To investigate the biological and biochemical properties of the BSE-SW prion, a transmission study was conducted in cattle, which were inoculated intracerebrally with brain homogenate from BSE-SW–infected TgBoPrP mice. The disease incubation period was approximately 15 months. The animals showed characteristic neurological signs of dullness, and severe spongiform changes and a widespread, uniform distribution of disease-associated prion protein (PrPSc) were observed throughout the brain of infected cattle. Immunohistochemical PrPSc staining of the brain revealed the presence of intraglial accumulations and plaque-like deposits. No remarkable differences were identified in vacuolar lesion scores, topographical distribution patterns, and staining types of PrPSc in the brains of BSE-SW– vs H-BSE–infected cattle. PrPSc deposition was detected in the ganglia, vagus nerve, spinal nerve, cauda equina, adrenal medulla, and ocular muscle. Western blot analysis revealed that the specific biochemical properties of the BSE-SW prion, with an additional 10- to 12-kDa fragment, were well maintained after transmission. These findings indicated that the BSE-SW prion has biochemical properties distinct from those of H-BSE in cattle, although clinical and pathologic features of BSW-SW in cattle are indistinguishable from those of H-BSE. The results suggest that the 2 infectious agents, BSE-SW and H-BSE, are closely related strains.

scholarly journals Properties of L-Type Bovine Spongiform Encephalopathy in Intraspecies Passages

2011 ◽  
Vol 49 (5) ◽  
pp. 819-823 ◽  
Author(s):  
H. Okada ◽  
Y. Iwamaru ◽  
M. Kakizaki ◽  
K. Masujin ◽  
M. Imamura ◽  
...  
Keyword(s):  
Western Blot ◽  
Bovine Spongiform Encephalopathy ◽  
Blot Analysis ◽  
Western Blot Analysis ◽  
Brain Homogenate ◽  
Spongiform Encephalopathy ◽  
Biochemical Characteristics ◽  
Atypical Bovine Spongiform Encephalopathy ◽  
Single Host ◽  
The Brain

The origin and transmission routes of atypical bovine spongiform encephalopathy (BSE) remain unclear. To assess whether the biological and biochemical characteristics of atypical L-type BSE detected in Japanese cattle (BSE/JP24) are conserved during serial passages within a single host, 3 calves were inoculated intracerebrally with a brain homogenate prepared from first-passaged BSE/JP24-affected cattle. Detailed immunohistochemical and neuropathologic analysis of the brains of second-passaged animals, which had developed the disease and survived for an average of 16 months after inoculation, revealed distribution of spongiform changes and disease-associated prion protein (PrPSc) throughout the brain. Although immunolabeled PrPSc obtained from brain tissue was characterized by the presence of PrP plaques and diffuse synaptic granular accumulations, no stellate-type deposits were detected. Western blot analysis suggested no obvious differences in PrPSc molecular mass or glycoform pattern in the brains of first- and second-passaged cattle. These findings suggest failures to identify differences in mean incubation period and biochemical and neuropathologic properties of the BSE/JP24 prion between the first and second passages in cattle.

scholarly journals Prion in Saliva of Bovine Spongiform Encephalopathy–Infected Cattle

2012 ◽  
Vol 18 (12) ◽  
pp. 2091-2092 ◽  
Author(s):  
Hiroyuki Okada ◽  
Yuichi Murayama ◽  
Noriko Shimozaki ◽  
Miyako Yoshioka ◽  
Kentaro Masujin ◽  
...  
Keyword(s):  
Bovine Spongiform Encephalopathy ◽  
Spongiform Encephalopathy ◽  
Infected Cattle

Are Bacterial Toxins Involved in the Aetiology of Transmissible Spongiform Encephalopathies?

1997 ◽  
Vol 11 (4) ◽  
pp. 301-307 ◽  
Author(s):  
T. Stockdale
Keyword(s):  
Bovine Spongiform Encephalopathy ◽  
Bacterial Toxins ◽  
Transmissible Spongiform Encephalopathies ◽  
Spongiform Encephalopathy ◽  
Meat And Bone Meal ◽  
Bone Meal ◽  
Spongiform Encephalopathies ◽  
Infected Meat ◽  
Disease Epidemics ◽  
The Brain

It is argued that the conditions for Bovine Spongiform Encephalopathy and Creutzfeld-Jacob disease epidemics necessitate, in addition to a diet that contains infected meat and bone meal, the presence of leaky membranes that enable bacterial toxins to circulate in the blood and enter the brain.

scholarly journals Significant differences in incubation times in sheep infected with bovine spongiform encephalopathy result from variation at codon 141 in the PRNP gene

2012 ◽  
Vol 93 (12) ◽  
pp. 2749-2756 ◽  
Author(s):  
Boon Chin Tan ◽  
Anthony R. Alejo Blanco ◽  
E. Fiona Houston ◽  
Paula Stewart ◽  
Wilfred Goldmann ◽  
...  
Keyword(s):  
Amino Acid ◽  
Bovine Spongiform Encephalopathy ◽  
Prion Protein ◽  
Protein Misfolding ◽  
Prnp Gene ◽  
Brain Homogenate ◽  
Spongiform Encephalopathy ◽  
Direct Effects ◽  
Prion Infection ◽  
Incubation Periods

The susceptibility of sheep to prion infection is linked to variation in the PRNP gene, which encodes the prion protein. Common polymorphisms occur at codons 136, 154 and 171. Sheep which are homozygous for the A136R154Q171 allele are the most susceptible to bovine spongiform encephalopathy (BSE). The effect of other polymorphisms on BSE susceptibility is unknown. We orally infected ARQ/ARQ Cheviot sheep with equal amounts of BSE brain homogenate and a range of incubation periods was observed. When we segregated sheep according to the amino acid (L or F) encoded at codon 141 of the PRNP gene, the shortest incubation period was observed in LL141 sheep, whilst incubation periods in FF141 and LF141 sheep were significantly longer. No statistically significant differences existed in the expression of total prion protein or the disease-associated isoform in BSE-infected sheep within each genotype subgroup. This suggested that the amino acid encoded at codon 141 probably affects incubation times through direct effects on protein misfolding rates.

Altered expression of CRMPs in the brain of bovine spongiform encephalopathy-infected mice during disease progression

2009 ◽  
Vol 1261 ◽  
pp. 1-6 ◽  
Author(s):  
Nathalie Auvergnon ◽  
Sophie Reibel ◽  
Monique Touret ◽  
Jérôme Honnorat ◽  
Thierry Baron ◽  
...  
Keyword(s):  
Disease Progression ◽  
Bovine Spongiform Encephalopathy ◽  
Spongiform Encephalopathy ◽  
Altered Expression ◽  
The Brain

scholarly journals Characterization of two distinct prion strains derived from bovine spongiform encephalopathy transmissions to inbred mice

2004 ◽  
Vol 85 (8) ◽  
pp. 2471-2478 ◽  
Author(s):  
Sarah E. Lloyd ◽  
Jacqueline M. Linehan ◽  
Melanie Desbruslais ◽  
Susan Joiner ◽  
Jennifer Buckell ◽  
...  
Keyword(s):  
Bovine Spongiform Encephalopathy ◽  
Prion Protein ◽  
Incubation Time ◽  
Inbred Mice ◽  
Biochemical Properties ◽  
Distinct Pattern ◽  
Spongiform Encephalopathy ◽  
Prion Strain ◽  
Disease Phenotypes ◽  
Prion Strains

Distinct prion strains can be distinguished by differences in incubation period, neuropathology and biochemical properties of disease-associated prion protein (PrPSc) in inoculated mice. Reliable comparisons of mouse prion strain properties can only be achieved after passage in genetically identical mice, as host prion protein sequence and genetic background are known to modulate prion disease phenotypes. While multiple prion strains have been identified in sheep scrapie and Creutzfeldt–Jakob disease, bovine spongiform encephalopathy (BSE) is thought to be caused by a single prion strain. Primary passage of BSE prions to different lines of inbred mice resulted in the propagation of two distinct PrPSc types, suggesting that two prion strains may have been isolated. To investigate this further, these isolates were subpassaged in a single line of inbred mice (SJL) and it was confirmed that two distinct prion strains had been identified. MRC1 was characterized by a short incubation time (110±3 days), a mono-glycosylated-dominant PrPSc type and a generalized diffuse pattern of PrP-immunoreactive deposits, while MRC2 displayed a much longer incubation time (155±1 days), a di-glycosylated-dominant PrPSc type and a distinct pattern of PrP-immunoreactive deposits and neuronal loss. These data indicate a crucial involvement of the host genome in modulating prion strain selection and propagation in mice. It is possible that multiple disease phenotypes may also be possible in BSE prion infection in humans and other animals.

scholarly journals Detection of PrPSc in peripheral tissues of clinically affected cattle after oral challenge with bovine spongiform encephalopathy

2012 ◽  
Vol 93 (12) ◽  
pp. 2740-2748 ◽  
Author(s):  
Martin Franz ◽  
Martin Eiden ◽  
Anne Balkema-Buschmann ◽  
Justin Greenlee ◽  
Hermann Schatzl ◽  
...  
Keyword(s):  
Bovine Spongiform Encephalopathy ◽  
Protein Misfolding ◽  
Brain Homogenate ◽  
Diagnostic Methods ◽  
Spongiform Encephalopathy ◽  
Variant Form ◽  
Mesenteric Lymph Nodes ◽  
Tissue Samples ◽  
Peripheral Tissues ◽  
Resistant Disease

Bovine spongiform encephalopathy (BSE) is a fatal neurodegenerative prion disease that mainly affects cattle. Transmission of BSE to humans caused a variant form of Creutzfeldt–Jakob disease. Following infection, the protease-resistant, disease-associated isoform of prion protein (PrPSc) accumulates in the central nervous system and in other tissues. Many countries have defined bovine tissues that may contain prions as specified risk materials, which must not enter the human or animal food chains and therefore must be discarded. Ultrasensitive techniques such as protein misfolding cyclic amplification (PMCA) have been developed to detect PrPSc when present in minuscule amounts that are not readily detected by other diagnostic methods such as immunohistochemistry or Western blotting. This study was conducted to determine when and where PrPSc can be found by PMCA in cattle orally challenged with BSE. A total of 48 different tissue samples from four cattle infected orally with BSE at various clinical stages of disease were examined using a standardized PMCA protocol. The protocol used brain homogenate from bovine PrP transgenic mice (Tgbov XV) as substrate and three consecutive rounds of PMCA. Using this protocol, PrPSc was found in the brain, spinal cord, nerve ganglia, optic nerve and Peyer’s patches. The presence of PrPSc was confirmed in adrenal glands, as well as in mesenteric lymph nodes – a finding that was reported recently by another group. Interestingly, additional positive results were obtained for the first time in the oesophagus, abomasum, rumen and rectum of clinically affected cattle.

scholarly journals Meningoencephalitis Tuberculosa in a Holstein Cow

2005 ◽  
Vol 42 (6) ◽  
pp. 856-858 ◽  
Author(s):  
E. Oruç
Keyword(s):  
Bovine Spongiform Encephalopathy ◽  
Plasma Cells ◽  
Clinical Signs ◽  
Giant Cells ◽  
Spongiform Encephalopathy ◽  
Multinucleated Giant Cells ◽  
Holstein Cow ◽  
Acid Fast Bacilli ◽  
The Brain

The gross and histopathologic lesions of meningoencephalitis tuberculosa in a 4-year-old Holstein cow showing clinical signs compatible with bovine spongiform encephalopathy are described in this report. Grossly, numerous gray to yellow, firm and caseous nodules were seen on the ventral surfaces of the brain and in the lateral and fourth ventricles. Histopathologically, foci of caseation and dystrophic mineralization were surrounded by multinucleated giant cells, epitheloid macrophages, plasma cells, lymphocytes and fibrous proliferation. Ziehl-Neelsen stains of the lesions revealed masses of slender acid-fast bacilli in the necrotic centers of lesions and within surrounding giant cells.

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