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Bovine spongiform encephalopathy Update

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EN
Bovine spongiform encephalopathy (BSE) is a zoonosis being the origin of variant Creutzfeldt-Jakob disease and an important cattle disease in its own right. Countries have been slow to learn the importance of protecting, not only their cattle populations, but also their human populations. Since 2000, several additional European countries have reported BSE in native-born stock and this has led to a concern about the BSE status of countries that have imported cattle and cattle products from infected countries. Extensive feed and offal bans and application of newly-developed, ?Rapid? tests for prion protein in central nervous tissue of targeted, high-risk animals and slaughter cattle over 30 months old now provides the tools whereby the public are fully protected and BSE can be eradicated.
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issue 3
35-51
EN
Prions are devoid of nucleic acids and they are composed mainly or exclusively of protein PrPSC, that is a conformational variant of the normal cellular prion protein PrPC, encoded by a chromosomal gene. Conversion of PrPC into PrPSC is a posttranslational process which is accompanied by the acquisition of high b-sheet content. Human prion diseases may be of sporadic, genetic or infectious origin. Human activity caused a 'mad cow disease' epidemic, iatrogenic Creutzfeldt-Jakob disease (CJD), and lately, a new variant of CJD, which is thought to be a result of transmission of bovine prions to humans. Prion diseases are always fatal, and there is a need to develop effective methods of prevention and therapy for these disorders.
EN
Variation of the PrP gene was examined in healthy and BSE-affected Slovak cattle. According to previous studies, the 23-bp indel polymorphism is supposed to be associated with higher susceptibility to BSE. We investigated 301 samples from healthy cattle of various Slovak breeds and 24 samples obtained from tissues of BSE-affected cattle in Slovakia. We examined the PrP gene for the 23-bp indel polymorphism in the putative promoter region, 12-bp indel polymorphism in the first intron of the PrP gene, variations in number of octapeptide repeat units, and presence of the silent AAC?AAT transition in codon 192 within the protein-coding region of the PrP gene. Altogether we found 23 different genotypes in the group of healthy cattle and only 6 genotypes in the group of BSE-affected cattle. Comparison of homozygotes for the 23-bp insertion and heterozygotes showed significant differences (P < 0.05) in genotype distribution between the examined groups. Thereby the homozygous insertion genotype at the 23-bp indel polymorphism site in the promoter region of the prion protein gene seems to have a protective effect against BSE.
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