Comparative analysis of normal prion protein expression on human, rodent, and ruminant blood cells by using a panel of prion antibodies

Barclay, G. R.; Houston, E. Fiona; Halliday, S.; Farquhar, Christine; Turner, Marc

doi:10.1046/j.1537-2995.2002.00095.x

Cited by 32 publications

(30 citation statements)

References 60 publications

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“…The presence of PrP C in blood has been documented [14], [15], and is confirmed by our own unpublished observations. To produce one liter of milk, about 400 to 500 liters of blood must pass through the udder of a cow.…”

Section: Discussionsupporting

confidence: 84%

Prion Protein in Milk

Franscini¹,

Gedaily²,

Matthey³

et al. 2006

PLoS ONE

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BackgroundPrions are known to cause transmissible spongiform encephalopathies (TSE) after accumulation in the central nervous system. There is increasing evidence that prions are also present in body fluids and that prion infection by blood transmission is possible. The low concentration of the proteinaceous agent in body fluids and its long incubation time complicate epidemiologic analysis and estimation of spreading and thus the risk of human infection. This situation is particularly unsatisfactory for food and pharmaceutical industries, given the lack of sensitive tools for monitoring the infectious agent.Methodology/Principal FindingsWe have developed an adsorption matrix, Alicon PrioTrap®, which binds with high affinity and specificity to prion proteins. Thus we were able to identify prion protein (PrPC)–the precursor of prions (PrPSc)–in milk from humans, cows, sheep, and goats. The absolute amount of PrPC differs between the species (from µg/l range in sheep to ng/l range in human milk). PrPC is also found in homogenised and pasteurised off-the-shelf milk, and even ultrahigh temperature treatment only partially diminishes endogenous PrPC concentration.Conclusions/SignificanceIn view of a recent study showing evidence of prion replication occurring in the mammary gland of scrapie infected sheep suffering from mastitis, the appearance of PrPC in milk implies the possibility that milk of TSE-infected animals serves as source for PrPSc.

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Section: Discussionsupporting

confidence: 84%

Prion Protein in Milk

Franscini¹,

Gedaily²,

Matthey³

et al. 2006

PLoS ONE

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“…The reaction to PrP C on bovine leukocytes was weaker with both mAbs (E12/2 and 6H4), probably due to the lower expression of PrP C on the surface of bovine leukocytes. Barclay et al [45] also reported that PrP C appeared to be less widely distributed on the blood cells of mice, cattle and sheep compared to PrP C expressed on human blood cells. Beside the level of PrP C expression, the conformation and/or glycosylation state may affect the results as well [45].…”

Section: Discussionmentioning

confidence: 99%

“…Barclay et al [45] also reported that PrP C appeared to be less widely distributed on the blood cells of mice, cattle and sheep compared to PrP C expressed on human blood cells. Beside the level of PrP C expression, the conformation and/or glycosylation state may affect the results as well [45]. It was previously observed that bovine lymphocytes only express a diglycosylated isoform of PrP C [46].…”

Section: Discussionmentioning

confidence: 99%

Identification of an epitope on the recombinant bovine PrP that is able to elicit a prominent immune response in wild-type mice

Černilec¹,

Vranac²,

Hafner-Bratkovič³

et al. 2007

Immunology Letters

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“…Some authors have attempted to infer the likely distribution of PrP Sc and infectivity in blood components by studying the distribution of PrP c [47]. However, this approach should be treated with caution on two main grounds: first, PrP c is widely distributed in many tissues throughout the body, but only some of these tissues are capable of supporting infectivity and/or PrP Sc [2]; second, there is remarkable interspecies variation in the distribution of PrP c in blood components [48], but these differences do not appear (admittedly on the basis of incomplete data) to reflect interspecies differences in infectivity and/or PrP Sc distribution in blood components, at least in experimental models of prion disease (Table 5).…”

Section: Evidence For Infectivity In Blood In Prion Diseasesmentioning

confidence: 99%

Variant Creutzfeldt–Jakob disease and its transmission by blood

Ironside

Head

2003

Journal of Thrombosis and Haemostasis

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Summary. Variant Creutzfeldt–Jakob disease (vCJD) is a novel acquired human prion disease resulting from human exposure to the agent causing bovine spongiform encephalopathy (BSE). vCJD differs from all other human prion diseases in that the disease‐associated form of the prion protein and infectivity are present in lymphoid tissues throughout the body. Lymphoid tissues and lymphocytes are implicated in the peripheral pathogenesis of prion diseases (where infectivity may be detected during the preclinical phase of the illness), giving rise to concerns that blood and blood products may also contain infectivity, thus representing a possible source of iatrogenic spread of vCJD. These concerns have been reinforced by the recent transmission of BSE in an experimental sheep model by blood transfusion from an infected animal in the preclinical phase of the illness. Studies in other animal models suggest that most infectivity in blood may be cell‐associated, with lower levels in the plasma, and there is evidence to indicate that any infectivity present may be reduced during the process of plasma fractionation. At present, the attempts to detect disease‐associated prion protein and infectivity in buffy coat from vCJD patients have been negative, but these studies have been limited in size and in the sensitivity of the detection systems employed. Further studies are required to develop more sensitive means of detection of disease‐associated prion protein in blood; such techniques could also be employed for screening purposes, both individually and to help ascertain more precisely the likely numbers of future cases of vCJD.

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Comparative analysis of normal prion protein expression on human, rodent, and ruminant blood cells by using a panel of prion antibodies

Cited by 32 publications

References 60 publications

Prion Protein in Milk

Prion Protein in Milk

Identification of an epitope on the recombinant bovine PrP that is able to elicit a prominent immune response in wild-type mice

Variant Creutzfeldt–Jakob disease and its transmission by blood

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