Workshop 1 Lecture Hall 103 |
Workshop on Animal prion diseases: Emerging Prion Diseases Surveillance, Detection, Pathogenesis
The focus of this workshop will be ongoing studies and findings that enhance our understanding about the emergence and transmission of animal prion diseases. Special emphasis will be placed on short oral talks from early career, students and technicians.
09:00h |
Welcome |
09:10h |
S. Benestad: Norwegian Veterinary Institute, Emerging CWD strains in Europe, overall view of current/emerging situation |
09:35h |
G. Telling: A diverse spectrum of novel strains among Nordic cervids with chronic wasting disease |
09:55h |
D. Walter: Strain Types of Chronic Wasting Disease and Efforts Towards a Virtual Tissue Repository |
10:15h |
A. Huor: ARR/ARR genotype sheep show no resistance to ovine adapted c-BSE infection by the oral route |
10:35h
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Coffee Break |
11:00h |
C. Mathiason: Colorado State University, Seeking biological relevance of CWD maternal infections and transmission from dam to offspring |
11:25h |
F. Houston: Subclinical infection in sheep exposed to low doses of prions by blood transfusion
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11:45h |
E. Vidal: Bona fide spontaneous and atypical scrapie faitfully reproduced through the expression of a polymorphic variant of ovine prion protein |
12:25h |
Concluding remarks |
Workshop 2 Lecture Hall 104 |
Structural biology of protein misfolding diseases
Recent advances in cryo electron microscopy and other techniques have given us detailed insights into the structures of amyloid fibrils that were either isolated from diseased brains or generated in vitro. The question, which of theses structures represent the biologically active form, can be difficult to answer.
In this workshop, we will discuss the latest technical approaches to analyze the structures of amyloid fibrils and other misfolded proteins. We welcome contributions describing structural analyses at low and high resolutions, as well as studies that investigate the question of biological activity.
Special emphasis will be given to short oral presentations by trainees (all levels) to encourage young structural biologists in their quest to analyze the structures of amyloid fibrils and other protein aggregates.
09:00h |
Welcome Requena/Wille |
09:05h |
A. Kraus: TBD Prion structure |
09:35h |
M. Zweckstetter: Tau – a key target to treat Alzheimer’s disease |
10:05h |
M. Rigoli: Computational Paradigms to Study Prion Folding & Misfolding |
10:20h |
H. Eraña: Understanding the key features of the spontaneous formation of bona fide recombinant prions through a new method allowing their consistent generation within hours |
10:35h |
Coffee break |
10:55h |
V. Rathod: In vitro refolding of the 7kDa A117V GSS peptide |
11:10h |
F. Wang: Faithful propagation of prion strain-specific conformation to recombinant protein |
11:25h |
H. Rezai: Strain determinant minimal substructure revealed by dissociation of PrPSc assemblies |
11:40h |
M. Rayner: Prion propagation is dependent upon key N-terminal amino acids within the prion protein |
11:55h |
H. Wille: Infectious prions – are they all PIRIBS structures now? |
12:25h |
Concluding remarks (Requena / Wille) |
Workshop 3 Different venue only for workshop 3: Universitätsmedizin Göttingen (UMG), Robert Koch Str.40, 37075 Göttingen, Room 01.E1.257 – DIPS3 |
Neuropathology and clinicopathological correlation of human prion diseases and related dementias.
Several dementias are characterized by aggregation of abnormally folded conformers of host encoded proteins. In prion diseases and related dementias, seeded aggregation can lead to the spread of protein aggregates throughout the brain.
In this workshop, we will focus on neuropathology, selective cellular and regional vulnerability, and clinicopathological correlation not only in Creutzfeldt-Jakob disease but also in Parkinson’s and Alzheimer’s disease. Besides lectures by prominent experts in the field such as Ellen Gelpi, Piero Parchi and Markus Glatzel there will be room for case discussions and hands-on neuropathology training in this exciting field of science.
14:00h |
M. Glatzel: Intruduccion into the concept of this workshop |
14:05h |
P. Parchi: Histopathological and molecular variability in Creutzfeldt-Jakob disease: the effect of prion strain, host genotype, and disease etiology |
14:30h |
E. Gelpi: alpha-synuclein neuroanatomical distribution in Parkinson’s disease |
14:55h |
M. Glatzel: beta-amyloid and prion protein interactions and what this means for Creutzfeldt-Jakob and Alzheimers disease |
15:15h
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Coffee Break |
15:30h |
Case discussion and hands-on neuropathology training. Cases will be presented by Ellen Gelpi, markus Glatzel and Piero Parchi and these cases will cover the topics of COVID-19 and sCJD. You have the chance to present your own interesting or puzzeling cases (in case you plan to do this, could you please inform us in advance by E-Mail) |
16:45h |
M. Glatzel: Summary and feedback |
Workshop 4 Lecture Hall 104 |
Bio-marker/Human diseases
The focus of this workshop will be ongoing studies on developments of seeding aggregation assays in neurodegenerative diseases. Special attention will be paid to clinical studies and improvement for early detection in various biological fluids and tissues in humans.
14:00h |
A. Green: SAA for alpha-synuclein
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14:20h |
G. Zanusso: Human Prion diseases diagnosis by RT-QuIC |
14:40h |
I. Zerr/M. Schmitz: Seeding conversion variability of misfolded tau conformers in classical and rapidly progressive Alzheimer’s disease |
15:00h |
R. Sánchez-Valle: Quantitative 14-3-3 protein and prion RT-QuIC concordance analysis of patients with suspected prion diseases in Spain |
15:15h |
N. Omer: Cerebrospinal fluid (CSF) and Plasma Biomarkers in patients with genetic Creutzfeldt-Jakob disease (gCJD) and healthy relatives, carriers of the E200K mutation: Results from an ongoing longitudinal study. |
15:30h |
N. Younas: Early preclinical proteomic signatures of prion infection |
15:45h |
Coffee break |
16:15h |
C. N. Kraft: Nasal swab detection of prion shedding in CWD-infected white-tailed |
16:30h |
C. M. Thomas: Comparison of in vitro tests (PMCA and RT-QuIC) and bioassay for longitudinal prion detection in preclinical blood samples from BSE infected sheep
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16:45h |
D. F. Browne: Hypochlorous acid solutions reduce disease-associated tau seeding activity |
17:00h |
S. Galušková: Evaluation of the seeding activity of alpha-synuclein in brain and cerebrospinal fluid tissue samples |
17:15h |
L. Concha: Semi-quantitative αS-SAA detects no difference in αSyn seeds in CSF from prodromal to phenocon- version in longitudinal samples |
17:30h |
M. Rossi: Towards an improved ‘quantitative’ α-synuclein Real-Time Quaking-Induced Conversion assay to assess Lewy body pathology in vivo |
17:45h |
O. Bannach: Combination of seeded aggregation and sFIDA for diagnostics of neurodegenerative diseases |
Session 1 Hall 011 |
Protein Structure– Function, Conversion, Dysfunction |
Chairs: D. Riesner/N. Lopez-Lorenzo |
09:00h |
B. Caughey: Prion structures |
Keynote |
09:45h |
E. Artikis: Understanding the Conformational Dynamics of Infectious Prion Fibrils |
1.1 |
10:00h |
S. Manka: A pipeline for atomic structure determination of infectious ex vivo prion fibrils by cryo-EM |
1.2 |
10:15h |
Y. Chernoff: Yeast models for studying aggregation of proteins, involved in Alzheimer’s disease |
1.3 |
10:30h |
Coffee break |
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Session 2 Hall 011 |
Pathogenic mechanisms in tauopathies |
Chairs: M. Jucker/S. Krasemann |
11.00h |
K. Duff: Mechanisms for the spread of tauopathies in AD and FTD |
Keynote |
11:45h |
R. Chiesa: Inoculation of human traumatic brain injury tissue homogenates induces cognitive deficits and widespread tau pathology in wild-type mice |
2.1 |
12:00h |
A. Kraus: Tau seeds precede earliest Alzheimer’s changes and are prevalent in synucleinopathies andother neurodegenerative diseases |
2.2 |
12:15h |
Lunch |
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Session 3 Hall 011 |
Pathogenic mechanisms in synucleinopathies |
Chairs: T. Outeiro/G. Zanusso |
14:00h |
A. L. Woerman: Alpha-synuclein prions in multiple system atrophy |
Keynote |
14:45h |
J. Ayers: Different Alpha-Synuclein Prion Strains Cause Dementia with Lewy Bodies and Multiple System Atrophy |
3.1 |
15:00h |
Ch. Orru: Performance of alpha-synuclein RT-QUIC in relation to neuropathological staging of Lewy body disease |
3.2 |
15:15h |
L. Blömeke: Quantitative Detection of α-Synuclein and Tau Oligomers and other Aggregates by Digital Single Particle Counting |
3.3 |
15.30h |
Coffee break |
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Session 4 Hall 011 |
Novel models for studying prion |
Chairs: M. Glatzel/I. Zerr |
16:00h |
O. Andréoletti: E200K CJD: a „model“ for studying sCJD? |
Keynote |
16.45h |
E. Comoy: Non-human primates: a renewed gold standard for prion(-like) diseases? |
4.1 |
17:00h |
A. Nihat: A dividing cell model for stable propagation and curing of bona fide human sporadic Creutzfeldt-Jakob Disease prions |
4.2 |
17:15h |
D. Bougard: Correlation between bioassay and PMCA for human prion decontamination studies |
4.3 |
Talk Hall 011 |
Special Lecture |
17:30h |
P. Liberski: Kuru – where all the prion research began |
Session 5 Hall 011 |
Structural biology of prions |
Chairs: H. Wille/H. Altmeppen |
09:00h |
J. Requena/R. Riek: Structure-Activity Relationship of Amyloids |
Keynote |
09.45h |
G. Jackson: Synthetic prions with high specific infectivity generated from recombinant PrP |
5.1 |
10:00h |
V. Beringue: Efficient propagation and strain diversity of prions from pure synthetic origin |
5.2 |
10:15h |
J. Bieschke: Direct Observation of Prion Protein Fibril Elongation Kinetics Reveals Competing Fibril Populations with Distinct Strain-like Structural and Dynamic Properties
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5.3 |
10:30h |
Coffee break |
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Session 6 Hall 011 |
Novel molecular mechanisms in prion diseases |
Chairs: R. Chiesa/ I.Vorberg |
11:00h |
A. Aguzzi: Genome-wide perturbations in prion science |
Keynote |
11:45h |
S. Mead: Genome wide association study of clinical duration and age at onset of sporadic CJD |
6.1 |
12:00h |
J. Tatzelt: Liquid-liquid phase separation of the prion protein promotes the formation of neurotoxic aggregates; a critical role of the N-terminal domain |
6.2 |
12:15h |
JM. Ribes: Prion protein converts at two distinct cellular sites and precedes fibril formation |
6.3 |
12:30h |
Lunch |
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Session 7 Hall 011 |
Pathogenic mechanisms in ß Amyloidosis |
Chairs: C. Lasmezas/T. Sklaviadis |
14:00h |
L. Walker: The prion paradigm, Abeta, and Alzheimer’s disease |
Keynote |
14:45h |
R. Gomez-Gutierrez: Structure-defined Aβ polymorphs promote different pathological changes in susceptible mice. |
7.1 |
15:00h |
C. Korth: Title: Abeta dimers are antiprions that interfere with seeded nucleation in vitro and in vivo |
7.2 |
15:15h |
M. Shafiq: Extracellular vesicles in the pathophysiology of Alzheimer’s disease: understanding the role of the prion protein |
7.3 |
15:30h |
Coffee break |
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Session 8 Hall 011 |
Function, dysfunction and conversion: from strains to transmission |
Chairs: J. Torres/A. Ruiz-Riquelme |
16:00h |
J. Collinge: Understanding prion structure, strains and neurotoxicity |
Keynote |
16:45h |
M. Arifin: Heterozygosity at cervid Prnp codon 138 progressively blocks prion conversion in vitro and partly confines prion propagation to the periphery in knock-in mice |
8.1 |
17:00h |
E. Cassmann: The chronic wasting disease agent from white-tailed deer is infectious to humanized mice after passage through raccoons |
8.2 |
17:15h |
H. Schaetzl: Transmission of prion infectivity from CWD-infected macaque tissues to rodent models demonstrates the zoonotic potential of chronic wasting disease. |
8.3 |
Talk Hall 011 |
Special Lecture by Industry |
17:30h |
P. Perin (Quanterix): Simoa Technology for Ultrasensitive Biomarker Detection |
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Poster Party |
Session 9 Hall 011 |
The interplay between Abeta and prion |
Chairs: J. Requena/D. Bougard |
09.00h |
SM. Strittmacher: Amyloid-ß Interaction with Cellular Prion Protein in Alzheimer’s Disease |
Keynote |
09:45h |
G. Merz: Cryo-EM reveals small-molecule binding to the paired helical fillament conformation of tau prions from Alzheimer’s disease |
9.1 |
10:00h |
S. Liu: De-repression of endogenous retroviruses promotes prion-like spreading of proteopathic seeds |
9.2 |
10:15h |
Coffee break |
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Session 10A Hall 011 |
CJD International Support Alliance |
Chairs: B. Appleby/P. Hermann |
11:00h |
S. Solvyns (CJDISA) |
Keynote |
11:30h |
J. & R. Backer: CJK-Initiative, Germany |
10A.1 |
11:45h |
J. Castilla: Spanish Foundation for prion diseases |
10A.2 |
Session 10B Hall 011 |
Genetic Prion Diseases |
Chairs: B. Appleby/P. Hermann |
12:00h |
N. Majbour: Defining the onset of prion infection and neurodegeneration in healthy individuals at risk of prion disease |
10B.3 |
12:15h |
A. Anane: Biobank of genetic CJD at Israel |
10B.4 |
12:30h |
Lunch |
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Session 11A Hall 011 |
Therapeutic perspectives in prion diseases |
Chairs: P. Cras/J. Castilla |
13:45h |
H. Zhao: ASO-mediated PrP suppression as disease modifying therapy for prion disease |
11A.1 |
14:00h |
V. Bonaldo: Folding intermediates of the cellular PrP across disease and therapy |
11A.2 |
14:15h |
S. Krasemann: mGluR5 inhibition delays cognitive decline and incubation time in a mouse model of prion disease |
11A.3 |
14:30h |
B. Zeitler: Engineered zinc finger protein transcription factors potently reduce brain PrP expression and extend survival in prion-infected mice |
11A.4 |
14:45h |
K. Xanthopoulos: Evaluation of the therapeutic action of poly(propylen Imine) glycodendrimers in prion disease mouse model |
11A.5 |
15:00h |
R. Mercer: Two pronged pharmacological interventions for prion disease targeting propagation and toxicity |
11A.6 |
15:15h |
M. Fleming: Optimizing prion vaccination in a transgenic mouse model of Gerstmann-Sträussler-Scheinker disease |
11A.7 |
15:30h |
Coffee break |
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Session 11B Hall 010 |
Animal Diseases |
Chairs: H. Schaetzl/C. Mathiason |
13:45 |
S. Canoyra:Conformational shift at the evolutionary mechanism for classical BSE emergence from atypical scrapie |
11B.1 |
14:00h |
G. Telling: Divergent strain profiles of European and North American CWD |
11B.2 |
14:15h |
R. Morales: Nasal bot: an emerging vector for natural chronic wasting disease transmission |
11B.3 |
14:30h |
N. Denkers: Shedding of Chronic Wasting Disease Prions in Multiple Excreta Throughout Disease Course in White-tailed Deer |
11B.4 |
14:45h |
R. Bujdoso: A new bioassay for the sensitive detection of blood-borne CWD prions |
11B.5 |
15:00h |
J. Greenlee: Cattle with the EK211 PRNP polymorphism are susceptible to the H-type bovine spongiform encephalopathy agent from either E211K or wild type donors after oronasal inoculation |
11B.6 |
15:30h |
Coffee break |
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Session 12 Hall 011 |
hot topics/breaking news/controversies |
Chairs: Chr. Orru/E. Gelpi |
16:00h |
S. Hannaoul: Transmission of Cervid Prions to Humanized Mice Demonstrates the Zoonotic Potencial of CWD |
12.1 |
16:15h |
W. Q. Zou: Generation of human chronic wasting diseases in transgenic mice |
12.2 |
16:30h |
A. Castle: Beta-endoproteolysis of the cellular prion protein by dipeptidyl peptidase-4 and fibroblast activation protein |
12.3 |
16:45h |
G. Jansen: Neuropathology of 8 patients of the New Brunswick cluster of Neurological Syndrome of Unknown Cause; human Chronic Wasting Disease or blue-green algae? |
12.4 |
17:00h |
C. Lasmezas: A novel neuroprotective approach for protein misfolding neurodegenerative diseases |
12.5 |
17:15h |
Poster Award
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17:30h |
Prion 2023/End of the meeting |
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