Four types of scrapie in goats differentiated from each other and bovine spongiform encephalopathy by biochemical methods

J.p.m Langeveld ,Wilfred Goldmann,Maria Mazza,Stéphanie Simon,Isabelle Lantier,Elena Esposito,J.g Jacobs ,Christine Fast,L.j.m Van Keulen ,Umberto Agrimi,Frédéric Lantier ,Olivier Andréoletti ,Loukia Ekateriniadou,Cristina Acín ,Penelope Papasavva-Stylianou,Pier Luigi Acutis ,John Spiropoulos,Theodoros Sklaviadis,Alex Bossers,Martin H Groschup ,Laura Pirisinu,Romolo Nonno

doi:10.1186/s13567-019-0718-z

Abstract

Scrapie in goats has been known since 1942, the archetype of prion diseases in which only prion protein (PrP) in misfolded state (PrPSc) acts as infectious agent with fatal consequence. Emergence of bovine spongiform encephalopathy (BSE) with its zoonotic behaviour and detection in goats enhanced fears that its source was located in small ruminants. However, in goats knowledge on prion strain typing is limited. A European-wide study is presented concerning the biochemical phenotypes of the protease resistant fraction of PrPSc (PrPres) in over thirty brain isolates from transmissible spongiform encephalopathy (TSE) affected goats collected in seven countries. Three different scrapie forms were found: classical scrapie (CS), Nor98/atypical scrapie and one case of CH1641 scrapie. In addition, CS was found in two variants—CS-1 and CS-2 (mainly Italy)—which differed in proteolytic resistance of the PrPresN-terminus. Suitable PrPres markers for discriminating CH1641 from BSE (C-type) appeared to be glycoprofile pattern, presence of two triplets instead of one, and structural (in)stability of its core amino acid region. None of the samples exhibited BSE like features. BSE and these four scrapie types, of which CS-2 is new, can be recognized in goats with combinations of a set of nine biochemical parameters.

Highlights

Prion diseases or transmissible spongiform encephalopathies (TSEs) are lethal neurological infections in mammals caused by prions from either sporadic, familial or transmissible origin [1, 2]
Analyses to discriminate between bovine spongiform encepha‐ lopathy (BSE), classical scrapie and Nor98/atypical scrapie Initial analyses were carried out by Commissariat à l’Énergie Atomique (CEA)-ELISA on goat samples from all countries except on those from UK and G11–G17 from Greece
The PrPres banding pattern of sample I15 was as in atypical/Nor98 scrapie (AS)-like samples with a major band at 8 kDa, when using antibody P4, while SAF84 did not show binding. This was further confirmed in IZSTOWB with monoclonal antibodies (mAbs) 12B2, 9A2, Sha31 and SAF84

Summary

Introduction

Prion diseases or transmissible spongiform encephalopathies (TSEs) are lethal neurological infections in mammals caused by prions from either sporadic, familial or transmissible origin [1, 2]. Since the 1980s, a zoonotic form of the disease emerged in cattle as bovine spongiform encephalopathy (BSE, C-type) through consumption of contaminated meat and bone meal (MBM) [3, 4]. In 1995, a human variant form of human Creutzfeldt-Jakob disease (vCJD) emerged with phenotypic similarities to BSE [5, 6]. Awareness and strict surveillance of prion infections remain necessary, because of the zoonotic and epizootic risks of BSE and other forms of TSE with different transmittabilities such as chronic wasting disease (CWD) in cervids in North America and South Korea, and newly discovered TSEs in cervids in Norway and camelids in Algeria [11–13]

Methods

Results

Conclusion