The N-terminal cleavage site of PrPSc from BSE differs from that of PrPSc from scrapie

Hayashi, Hiroko; Yokoyama, Takashi; Takata, Masuhiro; Iwamaru, Yoshifumi; Imamura, Morikazu; Ushiki, Yuko; Shinagawa, Morikazu

doi:10.1016/j.bbrc.2005.01.065

Cited by 56 publications

(66 citation statements)

References 18 publications

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“…PrP Sc was extracted from the cattle brain tissues by a method described previously. 24 Briefly, the brain tissues of cattle were homogenized at 20% concentration (wt/vol) in a buffer containing 100 mM NaCl and 50 mM Tris-HCl (pH 7.6). The brain homogenate (250 μl) were mixed with an equal volume of detergent buffer containing 4% (wt/vol) Zwittergent 3-14 (Calbiochem), 1% (wt/vol) Sarkosyl, 100 mM NaCl and 50 mM Tris-HCl (pH 7.6), and incubated with 6.25 μl of 40 mg/ ml collagenase.…”

Section: Methodsmentioning

confidence: 99%

Biological and biochemical characterization of L-type-like bovine spongiform encephalopathy (BSE) detected in Japanese black beef cattle

Masujin

Shu

Yamakawa

et al. 2008

Prion

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A case of L-type-like atypical bovine spongiform encephalopathy was detected in 14-year-old Japanese black beef cattle (BSE/ JP24). To clarify the biological and biochemical properties of the prion in BSE/JP24, we performed a transmission study with wildtype mice and bovinized transgenic mice (TgBoPrP). The BSE/ JP24 prion was transmitted to TgBoPrP mice with the incubation period of 199.7 ± 3.4 days, which was shorter than that of classical BSE (C-BSE) (223.5 ± 13.5 days). Further, C-BSE was transmitted to wild-type mice with the incubation period of about 409 days, whereas BSE/JP24 prion inoculated mice showed no clinical signs up to 649 days. Severe vacuolation and a widespread and uniform distribution of PrP Sc were pathologically observed in the brain of BSE/JP24 prion affected TgBoPrP mice. The molecular weight and glycoform ratio of PrP Sc in BSE/JP24 were different from those in C-BSE, and PrP Sc in BSE/JP24 exhibited weaker proteinase K resistance than that in C-BSE. These findings revealed that the BSE/JP24 prion has distinct biological and biochemical properties reported for that of C-BSE. Interestingly, a shorter incubation period was observed at the subsequent passage of the BSE/JP24 prion to TgBoPrP mice (152.2 ± 3.1 days). This result implies that BSE/JP24 prion has newly emerged and showed the possibility that L-type BSE prion might be classified into multiple strains.

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Section: Methodsmentioning

confidence: 99%

Biological and biochemical characterization of L-type-like bovine spongiform encephalopathy (BSE) detected in Japanese black beef cattle

Masujin

Shu

Yamakawa

et al. 2008

Prion

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“…Up to 1998, all the scrapie strains classically showed, after proteinase K treatment and Western blot, a typical triplet pattern comprising the typical di-, mono-, and unglycosylated band migrating between 18 and 30 kDa [19,20]. Recently, three published biological studies have given a more precise description of newly identified fragments.…”

Section: Identification Of New Prp Sc Fragmentsmentioning

confidence: 99%

Atypical/Nor98 scrapie: properties of the agent, genetics, and epidemiology

et al. 2008

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-Atypical/Nor98 scrapie cases in sheep were diagnosed for the first time in Norway in 1998. They are now identified in small ruminants in most European countries and represent an increasingly large proportion of the scrapie cases diagnosed in Europe. Atypical/Nor98 scrapie isolates have shown to be experimentally transmissible into transgenic mice and sheep but the properties of the TSE agent involved, like its biological and biochemical features, are so clearly distinct from the agent involved in classical scrapie that they have provided a challenging diagnostic for many years. No strain diversity has yet been identified among the atypical/Nor98 scrapie sample cases. The genetic predisposition of the sheep affected by atypical/Nor98 scrapie is almost inverted compared to classical scrapie, and the exact origin of this sporadic TSE strain is still speculative, but a spontaneous, non-contagious origin, like sporadic CreutzfeldtJakob disease in humans, can not be excluded. Further transmission and epidemiological studies are needed to better address this hypothesis. atypical scrapie / Nor98 / transmissible spongiform encephalopathies TSE / genetics / epidemiology

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“…Brain samples of BSE-affected cattle in Japan were used for the transmission study. Mouse-passaged BSE prions (Hayashi et al, 2005) were also used, along with the mouse-adapted scrapie Obihiro strain and hamster-adapted scrapie Sc237 strain (Yokoyama et al, 1995).…”

Section: Methodsmentioning

confidence: 99%

“…The blotted membrane was incubated with anti-PrP antibodies. Polyclonal antibody (pAb) B103 (Horiuchi et al, 1995) and monoclonal antibodies (mAbs) 44B1 (Kim et al, 2004), T2 (Hayashi et al, 2005) and 3F4 (Signet Laboratories) were used as primary antibodies. These antibodies recognized different epitopes: one located at the N terminus of PK-digested PrP Sc (pAb B103 and mAb 3F4) and the others located at the C terminus of the globular domain of PrP Sc (mAbs T2 and 44B1).…”

Section: Methodsmentioning

confidence: 99%

Alteration of the biological and biochemical characteristics of bovine spongiform encephalopathy prions during interspecies transmission in transgenic mice models

Yokoyama

Masujin

Iwamaru

et al. 2009

Journal of General Virology

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In the interspecies transmission of prions, the species barrier influences the susceptibility of the host. Bovine spongiform encephalopathy (BSE) prions affect a wide range of host species but do not affect hamsters. In order to study this species barrier, this study analysed the transmissibility of BSE prions to several lines of transgenic (Tg) mice, including those expressing mouse and hamster chimeric prion proteins (MH2M and MHM2 mice). BSE prions were transmitted to tga20, MHM2 and ICR mice, and the incubation period was approximately 400 days. Thus, these mice were classified as 'susceptible mice'. However, BSE prions were not transmitted to MH2M and TgHaNSE mice, and these mice were classified as 'resistant mice'. After the BSE prions were passaged once in wild-type mice, they could be transmitted to resistant mice. The characteristics of the accumulated abnormal isoform of PrP (PrP Sc ) in susceptible and resistant mice were determined using Western blotting. A BSE-like glycoform pattern of PrP Sc was detected in all of the susceptible mice using two different antibodies that recognized either the N-or the C-terminal end of the 27-30 kDa protease-resistant fragment of PrP (PrP 27-30 ) as the epitope. In contrast, proteinase digestion followed by deglycosylation analysis showed that, in addition to PrP 27-30 , truncated PrP Sc fragments existed in resistant mice. These mixed PrP Sc fragments may have resulted from the adaptation of resistant mice to BSE prions.

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The N-terminal cleavage site of PrPSc from BSE differs from that of PrPSc from scrapie

Cited by 56 publications

References 18 publications

Biological and biochemical characterization of L-type-like bovine spongiform encephalopathy (BSE) detected in Japanese black beef cattle

Biological and biochemical characterization of L-type-like bovine spongiform encephalopathy (BSE) detected in Japanese black beef cattle

Atypical/Nor98 scrapie: properties of the agent, genetics, and epidemiology

Alteration of the biological and biochemical characteristics of bovine spongiform encephalopathy prions during interspecies transmission in transgenic mice models

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