{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,11,11]],"date-time":"2025-11-11T13:55:39Z","timestamp":1762869339590,"version":"build-2065373602"},"reference-count":39,"publisher":"MDPI AG","issue":"5","license":[{"start":{"date-parts":[[2024,5,16]],"date-time":"2024-05-16T00:00:00Z","timestamp":1715817600000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"name":"European Union","award":["T1EDK\u201402678"],"award-info":[{"award-number":["T1EDK\u201402678"]}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Pathogens"],"abstract":"<jats:p>Prions are proteinaceous pathogens responsible for a variety of devastating diseases in mammals, including scrapie in sheep and goats, chronic wasting disease in cervids, and Creutzfeldt\u2013Jakob disease (CJD) in humans. They are characterized by their exceptional persistence to common inactivation procedures. This applies to all possible sources of prion contamination as prions may be present in the tissues and biological fluids of infected individuals. Hence, efficient prion inactivation procedures are still being sought to minimize the risk of intra- or inter-species transmission. In the past, photocatalytic treatment has been proven to be capable of efficiently oxidizing and inactivating prions. In the present study, the efficacy of homogeneous photo-Fenton-based photocatalysis as well as heterogeneous photocatalysis with TiO2 in reducing RML mouse scrapie infectivity was evaluated. Prion inactivation was assessed by means of a bioassay, and the results were confirmed by in vitro experiments. While the prion infectivity of the RML mouse scrapie was reduced after treatment with the photo-Fenton reagent, the heterogeneous photocatalytic treatment of the same prion strain completely eliminated prion infectivity.<\/jats:p>","DOI":"10.3390\/pathogens13050420","type":"journal-article","created":{"date-parts":[[2024,5,16]],"date-time":"2024-05-16T11:26:17Z","timestamp":1715858777000},"page":"420","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":1,"title":["A Comparison of RML Prion Inactivation Efficiency by Heterogeneous and Homogeneous Photocatalysis"],"prefix":"10.3390","volume":"13","author":[{"given":"Ioannis","family":"Paspaltsis","sequence":"first","affiliation":[{"name":"Laboratory of Pharmacology, Department of Pharmacy, School of Health Sciences, Aristotle University of Thessaloniki, 54124 Thessaloniki, Greece"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-7363-9380","authenticated-orcid":false,"given":"Eirini","family":"Kanata","sequence":"additional","affiliation":[{"name":"Laboratory of Pharmacology, Department of Pharmacy, School of Health Sciences, Aristotle University of Thessaloniki, 54124 Thessaloniki, Greece"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Sotirios","family":"Sotiriadis","sequence":"additional","affiliation":[{"name":"Laboratory of Pharmacology, Department of Pharmacy, School of Health Sciences, Aristotle University of Thessaloniki, 54124 Thessaloniki, Greece"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Susana Silva","family":"Correia","sequence":"additional","affiliation":[{"name":"Department of Neurology, University Medicine Goettingen, German Center for Neurodegenerative Diseases (DZNE), 37075 G\u00f6ttingen, Germany"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-5502-681X","authenticated-orcid":false,"given":"Matthias","family":"Schmitz","sequence":"additional","affiliation":[{"name":"Department of Neurology, University Medicine Goettingen, German Center for Neurodegenerative Diseases (DZNE), 37075 G\u00f6ttingen, Germany"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-6722-2463","authenticated-orcid":false,"given":"Inga","family":"Zerr","sequence":"additional","affiliation":[{"name":"Department of Neurology, University Medicine Goettingen, German Center for Neurodegenerative Diseases (DZNE), 37075 G\u00f6ttingen, Germany"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-4170-0612","authenticated-orcid":false,"given":"Dimitra","family":"Dafou","sequence":"additional","affiliation":[{"name":"Department of Genetics, Development and Molecular Biology, School of Biology, Aristotle University of Thessaloniki, 54124 Thessaloniki, Greece"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-8759-8962","authenticated-orcid":false,"given":"Konstantinos","family":"Xanthopoulos","sequence":"additional","affiliation":[{"name":"Laboratory of Pharmacology, Department of Pharmacy, School of Health Sciences, Aristotle University of Thessaloniki, 54124 Thessaloniki, Greece"},{"name":"Centre for Research and Technology Hellas, Institute of Applied Biosciences, 57001 Thermi, Greece"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Theodoros","family":"Sklaviadis","sequence":"additional","affiliation":[{"name":"Laboratory of Pharmacology, Department of Pharmacy, School of Health Sciences, Aristotle University of Thessaloniki, 54124 Thessaloniki, Greece"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"1968","published-online":{"date-parts":[[2024,5,16]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"388","DOI":"10.1126\/science.161.3839.388","article-title":"Creutzfeldt-Jakob Disease (Spongiform Encephalopathy): Transmission to the Chimpanzee","volume":"161","author":"Gibbs","year":"1968","journal-title":"Science"},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"248","DOI":"10.1111\/bpa.12696","article-title":"Animal Prion Diseases: The Risks to Human Health","volume":"29","author":"Houston","year":"2019","journal-title":"Brain Pathol."},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"e153","DOI":"10.1212\/WNL.0000000000008680","article-title":"Prion Disease Incidence in the United States: 2003\u20132015","volume":"94","author":"Maddox","year":"2020","journal-title":"Neurology"},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"2191164","DOI":"10.1080\/14756366.2023.2191164","article-title":"Synthesis and Anti-Prion Aggregation Activity of Acylthiosemicarbazide Analogues","volume":"38","author":"Kim","year":"2023","journal-title":"J. Enzyme Inhib. Med. Chem."},{"key":"ref_5","doi-asserted-by":"crossref","unstructured":"Salzano, G., Giachin, G., and Legname, G. (2019). Structural Consequences of Copper Binding to the Prion Protein. Cells, 8.","DOI":"10.3390\/cells8080770"},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"13363","DOI":"10.1073\/pnas.95.23.13363","article-title":"Prions","volume":"95","author":"Prusiner","year":"1998","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"23","DOI":"10.21775\/cimb.036.023","article-title":"Inactivation Methods for Prions","volume":"36","author":"Sakudo","year":"2020","journal-title":"Curr. Issues Mol. Biol."},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"E10","DOI":"10.3171\/2016.5.FOCUS15126","article-title":"Human Prion Diseases: Surgical Lessons Learned from Iatrogenic Prion Transmission","volume":"41","author":"Bonda","year":"2016","journal-title":"Neurosurg. Focus"},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"296","DOI":"10.1111\/j.1365-2990.2012.01265.x","article-title":"Review: Creutzfeldt-Jakob Disease: Prion Protein Type, Disease Phenotype and Agent Strain","volume":"38","author":"Head","year":"2012","journal-title":"Neuropathol. Appl. Neurobiol."},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"521","DOI":"10.1016\/S0140-6736(04)16810-4","article-title":"Novel Methods for Disinfection of Prion-Contaminated Medical Devices","volume":"364","author":"Fichet","year":"2004","journal-title":"Lancet"},{"key":"ref_11","doi-asserted-by":"crossref","unstructured":"Williams, K., Hughson, A.G., Chesebro, B., and Race, B. (2019). Inactivation of Chronic Wasting Disease Prions Using Sodium Hypochlorite. PLoS ONE, 14.","DOI":"10.1371\/journal.pone.0223659"},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"163","DOI":"10.1111\/j.1348-0421.1991.tb01544.x","article-title":"Practical Methods for Chemical Inactivation of Creutzfeldt-Jakob Disease Pathogen","volume":"35","author":"Tateishi","year":"1991","journal-title":"Microbiol. Immunol."},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"483","DOI":"10.3892\/ijmm.2011.605","article-title":"Fundamentals of Prions and Their Inactivation (Review)","volume":"27","author":"Sakudo","year":"2011","journal-title":"Int. J. Mol. Med."},{"key":"ref_14","unstructured":"World Health Organization (2006). WHO Guidelines on Tissue Infectivity Distribution in Transmissible Spongiform Encephalopathies, World Health Organization Press."},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"107","DOI":"10.1086\/650197","article-title":"Guideline for Disinfection and Sterilization of Prion-Contaminated Medical Instruments","volume":"31","author":"Rutala","year":"2010","journal-title":"Infect. Control Hosp. Epidemiol."},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"397","DOI":"10.1016\/S0255-2701(97)00011-1","article-title":"Industrial Waste Water Treatment: Large Scale Development of a Light-Enhanced Fenton Reaction","volume":"36","author":"Oliveros","year":"1997","journal-title":"Chem. Eng. Process. Process Intensif."},{"key":"ref_17","unstructured":"Boule, P., Bahnemann, D.W., and Robertson, P.K.J. (2005). Introduction to Photochemical Advanced Oxidation Processes for Water Treatment BT\u2014Environmental Photochemistry Part II, Springer."},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"2003216","DOI":"10.1002\/aenm.202003216","article-title":"Strategies and Challenges on Selectivity of Photocatalytic Oxidation of Organic Substances","volume":"11","author":"Xiong","year":"2021","journal-title":"Adv. Energy Mater."},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"144163","DOI":"10.1016\/j.scitotenv.2020.144163","article-title":"An Overview of Homogeneous and Heterogeneous Photocatalysis Applications for the Removal of Pharmaceutical Compounds from Real or Synthetic Hospital Wastewaters under Lab or Pilot Scale","volume":"765","author":"Antonopoulou","year":"2021","journal-title":"Sci. Total Environ."},{"key":"ref_20","doi-asserted-by":"crossref","unstructured":"Antonopoulou, M. (2022). Homogeneous and Heterogeneous Photocatalysis for the Treatment of Pharmaceutical Industry Wastewaters: A Review. Toxics, 10.","DOI":"10.3390\/toxics10090539"},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"3125","DOI":"10.1099\/vir.0.81746-0","article-title":"Titanium Dioxide Photocatalytic Inactivation of Prions","volume":"87","author":"Paspaltsis","year":"2006","journal-title":"J. Gen. Virol."},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"488","DOI":"10.4161\/pri.27180","article-title":"Homogenous Photocatalytic Decontamination of Prion Infected Stainless Steel and Titanium Surfaces","volume":"7","author":"Berberidou","year":"2013","journal-title":"Prion"},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"149","DOI":"10.1016\/j.jhin.2008.09.015","article-title":"Photocatalytic Degradation of Prions Using the Photo-Fenton Reagent","volume":"71","author":"Paspaltsis","year":"2009","journal-title":"J. Hosp. Infect."},{"key":"ref_24","doi-asserted-by":"crossref","unstructured":"O\u2019Farrell, P.H. (1975). High Resolution Two-Dimensional Electrophoresis of Proteins. J. Biol. Chem., 4007\u20134021.","DOI":"10.1016\/S0021-9258(19)41496-8"},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"671","DOI":"10.1038\/nmeth.2089","article-title":"NIH Image to ImageJ: 25 Years of Image Analysis","volume":"9","author":"Schneider","year":"2012","journal-title":"Nat. Methods"},{"key":"ref_26","doi-asserted-by":"crossref","unstructured":"Wilham, J.M., Orr\u00fa, C.D., Bessen, R.A., Atarashi, R., Sano, K., Race, B., Meade-White, K.D., Taubner, L.M., Timmes, A., and Caughey, B. (2010). Rapid End-Point Quantitation of Prion Seeding Activity with Sensitivity Comparable to Bioassays. PLoS Pathog., 6.","DOI":"10.1371\/journal.ppat.1001217"},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"2233","DOI":"10.1038\/nprot.2016.120","article-title":"The Real-Time Quaking-Induced Conversion Assay for Detection of Human Prion Disease and Study of Other Protein Misfolding Diseases","volume":"11","author":"Schmitz","year":"2016","journal-title":"Nat. Protoc."},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"1092","DOI":"10.1046\/j.1471-4159.2002.00909.x","article-title":"Heterogeneity of Normal Prion Protein in Two-Dimensional Immunoblot: Presence of Various Glycosylated and Truncated Forms","volume":"81","author":"Pan","year":"2002","journal-title":"J. Neurochem."},{"key":"ref_29","first-page":"370ra183","article-title":"Detection of Prions in Blood from Patients with Variant Creutzfeldt-Jakob Disease","volume":"8","author":"Pritzkow","year":"2016","journal-title":"Sci. Transl. Med."},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"269","DOI":"10.1016\/0140-6736(91)90873-N","article-title":"Survival of Scrapie Virus after 3 Years\u2019 Interment","volume":"337","author":"Brown","year":"1991","journal-title":"Lancet"},{"key":"ref_31","doi-asserted-by":"crossref","unstructured":"Mahal, S.P., Jablonski, J., Suponitsky-Kroyter, I., Oelschlegel, A.M., Herva, M.E., Oldstone, M., and Weissmann, C. (2012). Propagation of RML Prions in Mice Expressing PrP Devoid of GPI Anchor Leads to Formation of a Novel, Stable Prion Strain. PLoS Pathog., 8.","DOI":"10.1371\/journal.ppat.1002746"},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"435","DOI":"10.1016\/j.wasman.2018.08.012","article-title":"Generation and Composition of Waste from Medical Histopathology Laboratories","volume":"79","author":"Kalogiannidou","year":"2018","journal-title":"Waste Manag."},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"121","DOI":"10.1016\/bs.pmbts.2020.08.006","article-title":"Strain Variation in Treatment and Prevention of Human Prion Diseases","volume":"175","author":"Ellett","year":"2020","journal-title":"Prog. Mol. Biol. Transl. Sci."},{"key":"ref_34","doi-asserted-by":"crossref","unstructured":"Moudjou, M., Castille, J., Passet, B., Herzog, L., Reine, F., Vilotte, J.L., Rezaei, H., B\u00e9ringue, V., and Igel-Egalon, A. (2020). Improving the Predictive Value of Prion Inactivation Validation Methods to Minimize the Risks of Iatrogenic Transmission with Medical Instruments. Front. Bioeng. Biotechnol., 8.","DOI":"10.3389\/fbioe.2020.591024"},{"key":"ref_35","doi-asserted-by":"crossref","unstructured":"Tixador, P., Herzog, L., Reine, F., Jaumain, E., Chapuis, J., le Dur, A., Laude, H., and B\u00e9ringue, V. (2010). The Physical Relationship between Infectivity and Prion Protein Aggregates Is Strain-Dependent. PLoS Pathog., 6.","DOI":"10.1371\/journal.ppat.1000859"},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"27972","DOI":"10.1074\/jbc.M113.477547","article-title":"Analyses of Protease Resistance and Aggregation State of Abnormal Prion Protein across the Spectrum of Human Prions","volume":"288","author":"Saverioni","year":"2013","journal-title":"J. Biol. Chem."},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"18","DOI":"10.1111\/j.1574-6968.2006.00190.x","article-title":"The Bactericidal Effect of TiO2 Photocatalysis Involves Adsorption onto Catalyst and the Loss of Membrane Integrity","volume":"258","author":"Gogniat","year":"2006","journal-title":"FEMS Microbiol. Lett."},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"1339","DOI":"10.1016\/S0896-6273(00)80653-4","article-title":"Neurological Illness in Transgenic Mice Expressing a Prion Protein with an Insertional Mutation","volume":"21","author":"Chiesa","year":"1998","journal-title":"Neuron"},{"key":"ref_39","doi-asserted-by":"crossref","first-page":"36","DOI":"10.1177\/0192623310385255","article-title":"Functional Assays for Neurotoxicity Testing","volume":"39","author":"Moser","year":"2011","journal-title":"Toxicol. Pathol."}],"container-title":["Pathogens"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/2076-0817\/13\/5\/420\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,10]],"date-time":"2025-10-10T14:43:33Z","timestamp":1760107413000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/2076-0817\/13\/5\/420"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2024,5,16]]},"references-count":39,"journal-issue":{"issue":"5","published-online":{"date-parts":[[2024,5]]}},"alternative-id":["pathogens13050420"],"URL":"https:\/\/doi.org\/10.3390\/pathogens13050420","relation":{},"ISSN":["2076-0817"],"issn-type":[{"type":"electronic","value":"2076-0817"}],"subject":[],"published":{"date-parts":[[2024,5,16]]}}}