Abstract
To assess risk for cattle-to-human transmission of prions that cause uncommon forms of bovine spongiform encephalopathy (BSE), we inoculated mice expressing human PrP Met129 with field isolates. Unlike classical BSE agent, L-type prions appeared to propagate in these mice with no obvious transmission barrier. H-type prions failed to infect the mice.
Highlights
Human Prion ProteinThe large-scale testing of livestock nervous tissues for the presence of protease-resistant prion protein (PrPres) has enabled assessment of bovine spongiform encephalopathy (BSE) prevalence and exclusion of BSE-infected animals from human food [2]
To assess risk for cattle-to-human transmission of prions that cause uncommon forms of bovine spongiform encephalopathy (BSE), we inoculated mice expressing human PrP methionine at codon 129 (Met129) with field isolates
We found that atypical L-type bovine prions can propagate in human PrP transgenic mice with no significant transmission barrier
Summary
The large-scale testing of livestock nervous tissues for the presence of protease-resistant prion protein (PrPres) has enabled assessment of BSE prevalence and exclusion of BSE-infected animals from human food [2] This active surveillance has led to the recognition of 2 variant PrPres molecular signatures, termed H-type and L-type BSE. They differ from that of classical BSE by having protease-resistant fragments of a higher (H) or a slightly lower (L) molecular mass, respectively, and different patterns of glycosylation [3,4,5] Both types have been detected worldwide as rare cases in older animals, at a low prevalence consistent with the possibility of sporadic forms of prion diseases in cattle [6]. Transmission of L-type isolates to tg650 mice produced markedly different results
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