Study protocol of D1Ce Screen: A pilot project of the Italian national screening program for type 1 diabetes and coeliac disease in the paediatric population.

Background: The D1Ce Screen pilot study stems from the Italian Republic Law 130/2023 introducing the screening based on autoantibody measurement on capillary blood for the identification of people in pre-symptomatic, early phase of type 1 diabetes (T1D) and/or having silent celiac disease (CD) in the general paediatric population to reduce the impact of the two more frequent and severe chronic diseases of childhood.

Aim: Primary aim is to assess, on a smaller scale, the organizational feasibility, acceptability and sustainability by the National Health Service of the screening program to be conducted nationwide in Italy according to the law.

Methods And Analysis: This is an observational multicenter study, planning to screen 5,363 children from four Italian regions (Lombardy, Marche, Campania, Sardinia), proportionally distributed according to population of the single Regions, representative of the North, Centre, South and Islands of Italy.

The Development of a Food Frequency Questionnaire for the Assessment of Ultra-Processed Food Consumption in the Italian Adult Population: Protocol for a Validity and Reproducibility Study.

Background: Over the last decade, while studies on the detrimental effects of ultra-processed food (UPF) consumption have increased, methodological limitations on the quality of available evidence have emerged. Starting from a critical reassessment of the NOVA classification, this project will aim to develop and validate a food frequency questionnaire (FFQ), which is based on the processing of consumed foods and specifically designed to estimate the UPF consumption and total dietary intake of macro- and micronutrients in the Italian adult population.

Methods: This study will take place in selected workplaces and include healthy males and females aged ≥18 years, residing in Italy and with Italian citizenship.

Follow-up and monitoring programme in children identified in early-stage type 1 diabetes during screening in the general population of Italy.

Aim: To provide guidance for follow-up and monitoring of children and adolescents identified as positive to islet autoantibodies (IA) in the general population screening for type 1 diabetes (T1D) in Italy.

Methods: Detection of IA helps to diagnose pre-symptomatic T1D, prevent diabetic ketoacidosis (DKA) and identify persons for new therapies to delay symptomatic diabetes. Italy recently became the first country to approve by law a general autoantibody screening program for T1D and celiac disease in all children and adolescents (age 1-17yr).

Characterization of the First Case of Classical Scrapie in a Sheep in Tunisia.

Classical scrapie is a contagious prion disease of sheep and goats. It is endemic in many countries in Europe, North America, and Asia. In Africa, imported scrapie cases have been described in South Africa and Kenia in the past.

Strain-Dependent Morphology of Reactive Astrocytes in Human- and Animal-Vole-Adapted Prions.

Reactive astrogliosis is one of the pathological hallmarks of prion diseases. Recent studies highlighted the influence of several factors on the astrocyte phenotype in prion diseases, including the brain region involved, the genotype backgrounds of the host, and the prion strain. Elucidating the influence of prion strains on the astrocyte phenotype may provide crucial insights for developing therapeutic strategies.

An optimized Western blot assay provides a comprehensive assessment of the physiological endoproteolytic processing of the prion protein.

The prion protein (PrP) is subjected to several conserved endoproteolytic events producing bioactive fragments that are of increasing interest for their physiological functions and their implication in the pathogenesis of prion diseases and other neurodegenerative diseases. However, systematic and comprehensive investigations on the full spectrum of PrP proteoforms have been hampered by the lack of methods able to identify all PrP-derived proteoforms. Building on previous knowledge of PrP endoproteolytic processing, we thus developed an optimized Western blot assay able to obtain the maximum information about PrP constitutive processing and the relative abundance of PrP proteoforms in a complex biological sample.

Gerstmann-Sträussler-Scheinker Disease with F198S Mutation Induces Independent Tau and Prion Protein Pathologies in Bank Voles.

Gerstmann-Sträussler-Scheinker disease (GSS) is a rare genetic prion disease. A large GSS kindred linked to the serine-for-phenylalanine substitution at codon 198 of the prion protein gene (GSS-F198S) is characterized by conspicuous accumulation of prion protein (PrP)-amyloid deposits and neurofibrillary tangles. Recently, we demonstrated the transmissibility of GSS-F198S prions to bank vole carrying isoleucine at 109 PrP codon (BvI).

A single amino acid residue in bank vole prion protein drives permissiveness to Nor98/atypical scrapie and the emergence of multiple strain variants.

Prions are infectious agents that replicate through the autocatalytic misfolding of the cellular prion protein (PrPC) into infectious aggregates (PrPSc) causing fatal neurodegenerative diseases in humans and animals. Prions exist as strains, which are encoded by conformational variants of PrPSc. The transmissibility of prions depends on the PrPC sequence of the recipient host and on the incoming prion strain, so that some animal prion strains are more contagious than others or are transmissible to new species, including humans.

Pelodera strongyloides in the critically endangered Apennine brown bear (Ursus arctos marsicanus).

Skin biopsies from 20 Apennine brown bears (Ursus arctos marsicanus), 17 of which displaying skin lesions, were investigated by histopathology. Different degrees of dermatitis characterized by folliculitis and furunculosis accompanied by epidermal hyperplasia and epidermal and follicular hyperkeratosis were detected. In the most severe lesions, the superimposition of traumatic wounds, probably self-induced by scratching, was observed.

Possible Human-to-Dog Transmission of SARS-CoV-2, Italy, 2020.

We detected severe acute respiratory syndrome coronavirus 2 in an otherwise healthy poodle living with 4 family members who had coronavirus disease. We observed antibodies in serum samples taken from the dog, indicating seroconversion. Full-length genome sequencing showed that the canine and human viruses were identical, suggesting human-to-animal transmission.

Stability of BSE infectivity towards heat treatment even after proteolytic removal of prion protein.

The unconventional infectious agents of transmissible spongiform encephalopathies (TSEs) are prions. Their infectivity co-appears with PrP, aberrant depositions of the host's cellular prion protein (PrP). Successive heat treatment in the presence of detergent and proteolysis by a keratinase from Bacillus licheniformis PWD-1 was shown before to destroy PrP from bovine TSE (BSE) and sheep scrapie diseased brain, however data regarding expected reduction of infectivity were still lacking.

Isolation of infectious, non-fibrillar and oligomeric prions from a genetic prion disease.

Prions are transmissible agents causing lethal neurodegenerative diseases that are composed of aggregates of misfolded cellular prion protein (PrPSc). Despite non-fibrillar oligomers having been proposed as the most infectious prion particles, prions purified from diseased brains usually consist of large and fibrillar PrPSc aggregates, whose protease-resistant core (PrPres) encompasses the whole C-terminus of PrP. In contrast, PrPSc from Gerstmann-Sträussler-Scheinker disease associated with alanine to valine substitution at position 117 (GSS-A117V) is characterized by a small protease-resistant core, which is devoid of the C-terminus.

Cofactor and glycosylation preferences for in vitro prion conversion are predominantly determined by strain conformation.

Prion diseases are caused by the misfolding of a host-encoded glycoprotein, PrPC, into a pathogenic conformer, PrPSc. Infectious prions can exist as different strains, composed of unique conformations of PrPSc that generate strain-specific biological traits, including distinctive patterns of PrPSc accumulation throughout the brain. Prion strains from different animal species display different cofactor and PrPC glycoform preferences to propagate efficiently in vitro, but it is unknown whether these molecular preferences are specified by the amino acid sequence of PrPC substrate or by the conformation of PrPSc seed.

Health and Climate Change: science calls for global action.

Climate changes affect social and environmental health determinants such as clean air, ecosystems health, safe drinking water and safe sufficient food. Globally, people at greatest risk of adverse health effects associated with climate change include children, the elderly and other vulnerable groups. Temperature-related death and illness, extreme events, polluted or stressed ecosystems represent relevant issues raising concern for both health and economic consequences.

Four types of scrapie in goats differentiated from each other and bovine spongiform encephalopathy by biochemical methods.

Scrapie in goats has been known since 1942, the archetype of prion diseases in which only prion protein (PrP) in misfolded state (PrP) acts as infectious agent with fatal consequence. Emergence of bovine spongiform encephalopathy (BSE) with its zoonotic behaviour and detection in goats enhanced fears that its source was located in small ruminants. However, in goats knowledge on prion strain typing is limited.

Full restoration of specific infectivity and strain properties from pure mammalian prion protein.

The protein-only hypothesis predicts that infectious mammalian prions are composed solely of PrPSc, a misfolded conformer of the normal prion protein, PrPC. However, protein-only PrPSc preparations lack significant levels of prion infectivity, leading to the alternative hypothesis that cofactor molecules are required to form infectious prions. Here, we show that prions with parental strain properties and full specific infectivity can be restored from protein-only PrPSc in vitro.

Novel Type of Chronic Wasting Disease Detected in Moose (Alces alces), Norway.

Chronic wasting disease (CWD) persists in cervid populations of North America and in 2016 was detected for the first time in Europe in a wild reindeer in Norway. We report the detection of CWD in 3 moose (Alces alces) in Norway, identified through a large scale surveillance program. The cases occurred in 13-14-year-old female moose, and we detected an abnormal form of prion protein (PrP) in the brain but not in lymphoid tissues.

Biodiversity and selection for scrapie resistance in sheep: genetic polymorphism in eight breeds of Algeria.

Scrapie is a prion disease that affects the sheep and goats. It belongs to the group of transmissible spongiform encephalopathies (TSE). TSEs are characterized by the accumulation of the pathological form (PrP) of the cellular prion protein (PrP).

Prion Disease in Dromedary Camels, Algeria.

Prions cause fatal and transmissible neurodegenerative diseases, including Creutzfeldt-Jakob disease in humans, scrapie in small ruminants, and bovine spongiform encephalopathy (BSE). After the BSE epidemic, and the associated human infections, began in 1996 in the United Kingdom, general concerns have been raised about animal prions. We detected a prion disease in dromedary camels (Camelus dromedarius) in Algeria.