​Our research efforts are focused on deciphering molecular pathobiology and providing early diagnostics for  multiple neurodegenerative protein misfolding diseases including sporadic, genetic and acquired Prion and Prion-like diseases such as Creutzfeldt-Jakob (CJD), Parkinson’s (PD), and Alzheimer’s (AD) diseases. 

Vision & research questions

Molecular pathobiology

Prion diseases are transmissible and invariably fatal neurodegenerative protein misfolding diseases with heterogenous neuroinflammatory changes in the brain. The most common prion disease, the sporadic Creutzfeldt-Jakob disease, is a rapidly progressing disease with an average duration of 6 months. The quick disease course and a lack of effective treatment options make the research of new biomarkers and therapeutically targetable molecules of utmost importance. 

Thus, we are interested in biological processes taking place in distinct brain regions of patients who suffered from various subtypes of CJD. We aim to define pathologic brain microenvironment- and disease-specific cell subtypes and their functions to improve the understanding of disease complexity, its heterogeneous manifestations and contribute to advancement of its treatment strategies. In parallel with CJD, we also investigate AD to determine whether our findings are disease-specific or could be applied to pathogenesis of neurodegenerative protein misfolding diseases in general. 

Early diagnostics

All neurodegenerative protein misfolding diseases have a disease-associated protein, misfolding of which is considered to cause the disease. In diagnostics of sporadic Creutzfeldt-Jakob disease, an ultrasensitive method called Real-Time Quaking-Induced Conversion (RT-QuIC) was designed to exploit the misfolded prion protein’s (PrPSc) ability to induce templated misfolding of cellular prion proteins (PrPC) normally present in the brain. 

Modified version of RT-QuIC could also be adopted for early diagnostics of other neurodegenerative protein misfolding diseases such as Parkinson’s, Alzheimer’s, frontotemporal dementia, amyotrophic lateral sclerosis and other that are caused by misfolding and accumulation of different proteins including alpha-synuclein, Tau, beta-amyloid, TDP-43, and SOD-1. Thus, our goal is to create a diagnostic platform which would require only one cerebrospinal fluid sample and one blood sample to provide a diagnosis of any neurodegenerative protein misfolding disease.

Main findings

Established improved Real-Time Quaking-Induced Convertion (RT-QuIC) for cerebrospinal fluid sample analysis to provide early sporadic Creutzfeldt-Jakob disease diagnosis at the Danish Reference Center for Prion Diseases (Manuscript in preparation). 

Identified regional and sub-regional differences in neuroinflammation-associated gene expression indicating variable strength of inflammation even within the same brain regions of different sporadic Creutzfeldt-Jakob disease patients and suggesting the existence of pathologic microenvironment-specific neural cell subtypes or other molecular co-factors (Areskeviciute et al. 2020). 

Detected and characterized multiple unique genetic and sporadic prion disease variants including the first in Denmark fatal insomnia, Variably Protease Sensitive Prionopathy, sporadic Creutzfeldt-Jakob disease subtype VV1 with 1-octapeptide repeat deletion, and a case of genetic Creutzfeldt-Jakob disease with 5-octapeptide repeats insertion mutation in the prion protein gene (Mkhitarjan et al. 2022; Areskeviciute et al., 2021, 2019a, Mok et al. 2018).

Detected a novel pathogenic 8-octapeptide repeats insertion mutation in the prion protein gene and characterized its neuro- and clinicopathologic features (Areskeviciute et al. 2019b).

Proposed and investigated a novel theory for prion disease transmission from mutation carrying-fetus to a mutation-free mother via microchimerism (Areskeviciute et al. 2018).

Main projects

Danish Reference Center for Prion Diseases welcomes unsolicited applications from knowledgeable and motivated medicine, molecular biology, biochemistry, bioinformatics and similar graduate students for MSc and PhD degree assignments within the scope of the two main projects described below. 

Molecular biology of Neurodegenerative Protein Misfolding Diseases. Main aims: 

  • Molecular characterization of pathologic brain microenvironments: spatial biology. 
  • Existence, prevalence and distribution of pathologic brain microenvironment-specific cell subtypes and their role in pathogenesis. 
  • Identification and investigation of novel disease-specific biomarkers and their potential use for improved diagnostics and disease treatment.

Early Diagnostics of Neurodegenerative Protein Misfolding Diseases. Main aim:

  • Establishment of a uniform diagnostic platform based on templated protein misfolding technology for early and precise diagnostics of multiple neurodegenerative protein misfolding diseases using patient samples that require less invasive clinical procedures than a brain biopsy or even a lumbar puncture.
In our investigations we use human samples donated for research purposes. Danish Reference Center for Prion Diseases, being a national service unit providing diagnostics for patients and their families in the whole country and collaborating with several Neurology Departments and Memory Clinics, has a large archive of well-characterized brain tissues and cerebrospinal fluid samples. ​

Head of Danish Reference Center for Prion Diseases 

Eva Løbner Lund, MD, PhD
Consultant neuropathologist, Associate professor 

Prion laboratory manager

Aušrinė Areškevičiūtė, PhD
Molecular biologist

Team Members

Remarh Bsoul, MSc

Michelle Rasmusen 
Biomedical Laboratory Scientist

Ema Ramusovic Savelieva
Biomedical Laboratory Scientist

Vladyslav Vadymovych Tkach, MD, 
PhD student

Oskar McWiliam, MD
PhD student


Danish Reference Center for Prion Diseases (DRCPD) has a specialized biosafety level 3* and GMO class 1 Prion laboratory dedicated for diagnostic and research work involving infectious biological materials. Technology and methodology applied in Prion laboratory allows safe handling of fresh frozen tissues and their analyses at nucleic acid and protein levels. 

For multiplex gene and protein expression profiling in the brain microenvironment studies we employ the-state-of-art spatial biology research tools including light microscopy, digital pathology, NanoString nCounter and Digital Spatial Profiler platforms. 

To study misfolding proteins of various neurodegenerative protein misfolding diseases to adapt and create disease-specific protein amplification protocols, we apply various protein production and analysis methods including Fast Protein Liquid Chromtography (FPLC) and Real-Time Quaking-Induced Conversion (RT-QuIC).

DRCPD is a part of Department of Pathology, Copenhagen University Hospital and thus has access to multiple core facilities and specialized equipment such as Genetic Analyzers (sequencing), autostainer platforms (immunohistochemistry and tissue morphology) and others.


Danish Dementia Research Center, Copenhagen University Hospital, Denmark
Prof. dr. med. Gunhild Waldemar
Dr. Kristian Steen Frederiksen, MD 
Dr. Anja Hviid Simonsen
Prof. dr. med. Steen Gregers Hasselbalch

Department of Neurology, Bispebjerg and Frederiksberg Hospital, Denmark
Dr. Sara Brynhild Winther Bech, MD

Institute for Clinical Medicine and Biotech Research and Innovation Center (BRIC), University of Copenhagen, Denmark 
Prof. Bjarne Winther Kristensen, MD

National Creutzfeldt-Jakob Disease Research and Surveillance Center, University of Edinburgh, UK
Dr. Alison Green

Department of Experimental Diagnostic and Specialty Medicine (DIMES), University of Bologna, Italy
Prof. Piero Parchi, MD

National Prion Clinic, MRC Prion Unit, University College London, UK
Prof. Simon Mead, MD

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