Literature DB >> 9292029

Immunodetection of PrPSc in spleens of some scrapie-infected sheep but not BSE-infected cows.

R A Somerville1, C R Birkett, C F Farquhar, N Hunter, W Goldmann, J Dornan, D Grover, R M Hennion, C Percy, J Foster, M Jeffrey.   

Abstract

The development of diagnostic tools for transmissible spongiform encephalopathies (TSEs) would greatly assist their study and may provide assistance in controlling the disease. The detection of an abnormal form of the host protein PrP in noncentral nervous system tissues may form the basis for diagnosis of TSEs. Using a new antibody reagent to PrP produced in chickens, PrP can be readily detected in crude tissue extracts. PrP from uninfected spleen had a lower molecular mass range than PrP from brain, suggesting a lower degree of glycosylation. A simple method for detecting the abnormal form of the protein, PrPSc, in ruminant brain and spleen has been developed. PrPSc was detected in sheep spleen extracts from a flock affected by natural scrapie and was also found in spleens from some, but not all, experimental TSE cases. In spleens from cattle with bovine spongiform encephalopathy (BSE) no PrPSc was detected. It is therefore suggested that there is differential targeting of PrPSc deposition between organs in these different types of TSE infection which, with other factors, depends on strain of infecting agent.

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Year:  1997        PMID: 9292029     DOI: 10.1099/0022-1317-78-9-2389

Source DB:  PubMed          Journal:  J Gen Virol        ISSN: 0022-1317            Impact factor:   3.891


  18 in total

1.  Autonomic nervous system innervation of lymphoid territories in spleen: a possible involvement of noradrenergic neurons for prion neuroinvasion in natural scrapie.

Authors:  A Bencsik; S Lezmi; T Baron
Journal:  J Neurovirol       Date:  2001-10       Impact factor: 2.643

2.  First case of feline spongiform encephalopathy in a captive cheetah born in France: PrP(sc) analysis in various tissues revealed unexpected targeting of kidney and adrenal gland.

Authors:  Stephane Lezmi; Anna Bencsik; Eoin Monks; Thierry Petit; Thierry Baron
Journal:  Histochem Cell Biol       Date:  2003-05-01       Impact factor: 4.304

3.  Susceptibility of sheep for scrapie as assessed by in vitro conversion of nine naturally occurring variants of PrP.

Authors:  A Bossers; R de Vries; M A Smits
Journal:  J Virol       Date:  2000-02       Impact factor: 5.103

4.  Extraneural prion neuroinvasion without lymphoreticular system infection.

Authors:  Jason C Bartz; Crista Dejoia; Tammy Tucker; Anthony E Kincaid; Richard A Bessen
Journal:  J Virol       Date:  2005-09       Impact factor: 5.103

5.  Comparison of cattle and sheep colonic permeabilities to horseradish peroxidase and hamster scrapie prion protein in vitro.

Authors:  A T McKie; P S Zammit; R J Naftalin
Journal:  Gut       Date:  1999-12       Impact factor: 23.059

6.  Characterization and polyanion-binding properties of purified recombinant prion protein.

Authors:  D B Brimacombe; A D Bennett; F S Wusteman; A C Gill; J C Dann; C J Bostock
Journal:  Biochem J       Date:  1999-09-15       Impact factor: 3.857

7.  Temporary blockade of the tumor necrosis factor receptor signaling pathway impedes the spread of scrapie to the brain.

Authors:  Neil A Mabbott; Gillian McGovern; Martin Jeffrey; Moira E Bruce
Journal:  J Virol       Date:  2002-05       Impact factor: 5.103

8.  Immunohistochemical characterization of cell types expressing the cellular prion protein in the small intestine of cattle and mice.

Authors:  Kohtaro Miyazawa; Takashi Kanaya; Sachi Tanaka; Ikuro Takakura; Kouichi Watanabe; Shyuichi Ohwada; Haruki Kitazawa; Michael T Rose; Suehiro Sakaguchi; Shigeru Katamine; Takahiro Yamaguchi; Hisashi Aso
Journal:  Histochem Cell Biol       Date:  2006-12-13       Impact factor: 4.304

9.  Prions of ruminants show distinct splenotropisms in an ovine transgenic mouse model.

Authors:  Thierry Baron; Anna Bencsik; Eric Morignat
Journal:  PLoS One       Date:  2010-04-26       Impact factor: 3.240

10.  Complement Regulatory Protein Factor H Is a Soluble Prion Receptor That Potentiates Peripheral Prion Pathogenesis.

Authors:  Sarah J Kane; Taylor K Farley; Elizabeth O Gordon; Joshua Estep; Heather R Bender; Julie A Moreno; Jason Bartz; Glenn C Telling; Matthew C Pickering; Mark D Zabel
Journal:  J Immunol       Date:  2017-10-25       Impact factor: 5.422

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