Ultra-high-pressure inactivation of prion infectivity in processed meat: A practical method to prevent human infection

Brown, Paul; Meyer, Richard D.; Cardone, Franco; Pocchiari, Maurizio

doi:10.1073/pnas.1031826100

Cited by 82 publications

(37 citation statements)

References 17 publications

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“…Recently, Torrent et al (41) described that high pressure (2,000 bar) dissociates the high temperature-induced aggregates of recombinant prion protein. However much higher pressures (12,000 bar) at high temperature conditions (Ͼ100°C) were recently demonstrated to be able to inactivate prion infectivity in processed meat (42). On the other hand, the yeast prion protein Ure2 undergoes only limited perturbation at a pressure of 6,000 bar (43).…”

Section: Discussionmentioning

confidence: 99%

Dissociation of amyloid fibrils of α-synuclein and transthyretin by pressure reveals their reversible nature and the formation of water-excluded cavities

Foguel

Suarez

Gonzales

et al. 2003

Proc. Natl. Acad. Sci. U.S.A.

175

159

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Protein misfolding and aggregation have been linked to several human diseases, including Alzheimer's disease, Parkinson's disease, and systemic amyloidosis, by mechanisms that are not yet completely understood. The hallmark of most of these diseases is the formation of highly ordered and ␤-sheet-rich aggregates referred to as amyloid fibrils. Fibril formation by WT transthyretin (TTR) or TTR variants has been linked to the etiology of systemic amyloidosis and familial amyloid polyneuropathy, respectively. Similarly, amyloid fibril formation by ␣-synuclein (␣-syn) has been linked to neurodegeneration in Parkinson's disease, a movement disorder characterized by selective degeneration of dopaminergic neurons in the substantia nigra. Here we show that consecutive cycles of compression-decompression under aggregating conditions lead to reversible dissociation of TTR and ␣-syn fibrils. The high sensitivity of amyloid fibrils toward high hydrostatic pressure (HHP) indicates the existence of packing defects in the fibril core. In addition, through the use of HHP we are able to detect differences in stability between fibrils formed from WT TTR and the familial amyloidotic polyneuropathy-associated variant V30M. The fibrils formed by WT ␣-syn were less susceptible to pressure denaturation than the Parkinson's disease-linked variants, A30P and A53T. This finding implies that fibrils of ␣-syn formed from the variants would be more easily dissolved into small oligomers by the cellular machinery. This result has physiological importance in light of the current view that the pathogenic species are the small aggregates rather the mature fibrils. Finally, the HHP-induced formation of fibrils from TTR is relatively fast (Ϸ60 min), a quality that allows screening of antiamyloidogenic drugs.

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Section: Discussionmentioning

confidence: 99%

Dissociation of amyloid fibrils of α-synuclein and transthyretin by pressure reveals their reversible nature and the formation of water-excluded cavities

Foguel

Suarez

Gonzales

et al. 2003

Proc. Natl. Acad. Sci. U.S.A.

175

159

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“…Brown et al (2003) reported a *Disease transmission to hamsters after intracerebral inoculation of 2 mg of scrapie-infected brain tissue after heating and/or exposure to high hydrostatic pressure for 120 min. The results show the number of hamsters that died after intracerebral inoculation/total number of hamsters infected at each treatment.…”

mentioning

confidence: 99%

Reduced proteinase K resistance and infectivity of prions after pressure treatment at 60 °C

García¹,

Heindl²,

Voigt

et al. 2004

Journal of General Virology

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High hydrostatic pressure is a mild technology compared with high temperatures and is commonly used for food pasteurization. Crude brain homogenates of terminally diseased hamsters infected with scrapie 263K strain were heated at 60 6C and/or pressurized up to 1000 MPa for 2 h. Prion proteins were analysed for their proteinase K sensitivity using a Western blot technique. PrP Sc pressurized with 500 MPa or above proved to be proteinase K sensitive. To test the remaining infectivity of the pressurized material, hamsters were infected intracerebrally. Results showed a greatly delayed onset of disease (from 80 up to 153 days) when samples had been pressurized at 500 MPa and above. An increase in the survival rate was also observed: 47 % survival over 180 days was seen following infection with homogenates pressurized at 700-1000 MPa.Prion diseases are associated with the accumulation of an isoform of the cellular prion protein, designated PrP Sc , after misfolding in a b-rich aggregated pathogenic multimer, which seems to be the main component of the transmissible form (Prusiner, 1991). The transmissible agent resists conventional autoclaving (Brown et al., 2000). Thus, the European Directive of 1996 recommends the use of at least 133 uC for 20 min to achieve effective inactivation during sterilization processes or rendering. Other suitable treatments, such as the combination of alkali and heat, or the use of hypochlorite solutions, although efficient, are aggressive, with a consequent loss of quality or texture in the treated tissues. Therefore, an interest in assessing the effects of unconventional milder technologies on prion stability and infectivity is growing. Milder processes would provide alternative sterilization procedures for at-risk materials and may reduce economic losses in the rendering industry. Here we report the effects of treatment with high hydrostatic pressure at 60 uC on the proteinase K (PK) sensitivity of hamster PrP Sc and the in vivo infectivity of the highpressure-treated samples.These experiments were performed with a single brain pool of the 263K strain of hamster-adapted scrapie agent. Brains containing PrP Sc were homogenized in a 1 : 10 dilution of PBS, pH 7?4, in a FastPrep cell disrupter (Qbiogene). Sets of duplicate samples were heated at 60 uC and/or pressurized up to 1000 MPa for 2 h independently. Total volumes of 250 ml of homogenate (10 %, w/v) were pressurized in a hydraulic press, U 101 (Polish Academy of Sciences, Warsaw). U 101 is a manually operated twin-piston hydraulic press (100 mm piston length, 80 mm piston movement). The vessel is a cylinder made of steel, with an inside diameter of 16 mm and 150 mm in height. The piston position is monitored with a linear transformer transducer and the pressure-measuring unit is an in-vessel manganin pressure gauge; both are digitally displayed. The pressure-transmitting medium was a 7 : 3 mixture of petroleum ether (boiling point 80-100 uC) and hydraulic oil (SAE 32). Samples were pressurized in polyethylene caps hermetically clos...

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“…In the food industry, HPP has been used to inactivate food-borne infectious agents (such as bacteria, viruses, fungi, protozoa, and prions) and proteins (such as enzymes, allergens, and toxins) (2,3,6,9). The primary advantage of HPP is that it has minimal effect on the organoleptic and nutritional properties of foods compared to other processing methods, since the treatment does not disrupt the covalent bonds stabilizing the structure of micronutrients as well as color and flavor compounds (3,5,23,39).…”

mentioning

confidence: 99%

Lack of Correlation between Virus Barosensitivity and the Presence of a Viral Envelope during Inactivation of Human Rotavirus, Vesicular Stomatitis Virus, and Avian Metapneumovirus by High-Pressure Processing

Lou¹,

Neetoo

Chen

et al. 2011

Appl Environ Microbiol

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High-pressure processing (HPP) is a nonthermal technology that has been shown to effectively inactivate a wide range of microorganisms. However, the effectiveness of HPP on inactivation of viruses is relatively less well understood. We systematically investigated the effects of intrinsic (pH) and processing (pressure, time, and temperature) parameters on the pressure inactivation of a nonenveloped virus (human rotavirus [HRV]) and two enveloped viruses (vesicular stomatitis virus [VSV] and avian metapneumovirus [aMPV]). We demonstrated that HPP can efficiently inactivate all tested viruses under optimal conditions, although the pressure susceptibilities and the roles of temperature and pH substantially varied among these viruses regardless of the presence of a viral envelope. We found that VSV was much more stable than most food-borne viruses, whereas aMPV was highly susceptible to HPP. When viruses were held for 2 min under 350 MPa at 4°C, 1.1-log, 3.9-log, and 5.0-log virus reductions were achieved for VSV, HRV, and aMPV, respectively. Both VSV and aMPV were more susceptible to HPP at higher temperature and lower pH. In contrast, HRV was more easily inactivated at higher pH, although temperature did not have a significant impact on inactivation. Furthermore, we demonstrated that the damage of virion structure by disruption of the viral envelope and/or capsid is the primary mechanism underlying HPP-induced viral inactivation. In addition, VSV glycoprotein remained antigenic although VSV was completely inactivated. Taken together, our findings suggest that HPP is a promising technology to eliminate viral contaminants in high-risk foods, water, and other fomites.High-pressure processing (HPP) is a nonthermal pasteurization technology that uses pressure instead of thermal energy to inactivate harmful pathogens. In the food industry, HPP has been used to inactivate food-borne infectious agents (such as bacteria, viruses, fungi, protozoa, and prions) and proteins (such as enzymes, allergens, and toxins) (2, 3, 6, 9). The primary advantage of HPP is that it has minimal effect on the organoleptic and nutritional properties of foods compared to other processing methods, since the treatment does not disrupt the covalent bonds stabilizing the structure of micronutrients as well as color and flavor compounds (3,5,23,39). In addition, since pressure acts instantaneously and uniformly throughout the pressure vessel, the structure and texture of many high-moisture foods are minimally affected. In today's modern society, consumers are increasingly demanding food products that are minimally processed and free of preservatives. Thus, HPP is becoming a widely used nonthermal processing technology that can ensure food safety, food quality, shelf-life extension, and nutritional value.Despite the extensive research on the inactivation of bacterial pathogens by HPP, the inactivation of viruses by HPP is less well understood. With regard to applications in the area of food safety, HPP studies have focused on food-and waterborne virus...

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Ultra-high-pressure inactivation of prion infectivity in processed meat: A practical method to prevent human infection

Cited by 82 publications

References 17 publications

Dissociation of amyloid fibrils of α-synuclein and transthyretin by pressure reveals their reversible nature and the formation of water-excluded cavities

Dissociation of amyloid fibrils of α-synuclein and transthyretin by pressure reveals their reversible nature and the formation of water-excluded cavities

Reduced proteinase K resistance and infectivity of prions after pressure treatment at 60 °C

Lack of Correlation between Virus Barosensitivity and the Presence of a Viral Envelope during Inactivation of Human Rotavirus, Vesicular Stomatitis Virus, and Avian Metapneumovirus by High-Pressure Processing

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