Prion pathogenesis in the absence of Toll-like receptor signalling
Open accessAbstract
To reach the brain from peripheral sites, prions must colonize various cell types within the lymphoreticular compartment. However, no prion entry receptors are yet known. Toll-like receptors (TLRs) are pattern-recognition receptors that bind a multitude of pathogens and are therefore candidates as effectors of prion entry. Moreover, injection of unmethylated CpG oligodinucleotides, which stimulate TLR9, has been reported to delay peripherally initiated scrapie. We therefore studied prion infection in MyD88(-/-) mice, which are defective in TLR signalling. Despite subtle defects in splenic microarchitecture, MyD88(-/-) mice challenged intraperitoneally or intracerebrally were fully susceptible to disease and died of scrapie after similar incubation times to those of wild-type mice. Splenic infectivity titres rose to similar levels with the same kinetics, and brains showed similar histopathological changes. TLR signalling therefore does not have any major role in prion pathogenesis, and the protective effect of TLR stimulation is unlikely to result from direct interactions with prions.
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Pathogenic changes in prion disease appear independent of MyD88, as ablation of this molecule did not lead to changes in incubation periods and neuropathological profiles of scrapie-infected mice.
“Pathogenic changes in prion disease appear to be independent of MyD88, a signaling intermediate for several TLR family members, as ablation of this molecule did not lead to changes in the incubation periods, and neuropathological profiles of scrapie-infected mice [12].”
From MicroRNA 146a (miR-146a) Is Over-Expressed during Prion Disease and Modulates the Innate Immune Response and the Microglial Activation State (2012) · cites this paper as [12]
In the RML infection mouse model of prion diseases, the incubation time to terminal disease is about 150 days ± 5 days.
“In the RML infection mouse model of prion diseases, the incubation time to terminal disease is about 150 days ± 5 days (Figure 2) [36].”
From Loss of Homeostatic Microglia Signature in Prion Diseases (2022) · cites this paper as [36]
MyD88 knock-out mice were readily infectable with scrapie and did not show any significant alteration in the time-course or pathology of the disease.
“Nevertheless, the study determined by Prinz et al. (2003) showed that MyD88 knock-out mice were readily infectable with scrapie and did not show any significant alteration in the time-course or pathology of the disease [12].”
From MicroRNA 146a (miR-146a) Is Over-Expressed during Prion Disease and Modulates the Innate Immune Response and the Microglial Activation State (2012) · cites this paper as [12]
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“In the RML infection mouse model of prion diseases, the incubation time to terminal disease is about 150 days ± 5 days (Figure 2) [36].”
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Kayesh, M. E. H., Kohara, M., & Tsukiyama–Kohara, K. (2025) · Vaccines · doi:10.3390/vaccines13080856 · Cited by 9 · see citing works
Tsou, A., Chen, P.-J., Tsai, K., Hu, W., & Lu, K. (2022) · Viruses · doi:10.3390/v14020408 · Cited by 9 · see citing works
Meling, S., Skovgaard, K., Bårdsen, K., Heegaard, P. M. H., & Ulvund, M. J. (2018) · BMC Veterinary Research · doi:10.1186/s12917-018-1607-9 · Cited by 6 · see citing works
Treatment by CpG or Flt3-ligand does not affect mouse susceptibility to BSE prions
Doré, G. R. G., Leclerc, C., & Lazarini, F. (2008) · Journal of Neuroimmunology · doi:10.1016/j.jneuroim.2008.03.016 · Cited by 4 · see citing works
Jorge, F. M. (2014) · UPT. Syiah Kuala University Library (Syiah Kuala University) · Cited by 4 · see citing works
Toll-like receptor response to Zika virus infection: progress toward infection control
Kayesh, M. E. H., Kohara, M., & Tsukiyama–Kohara, K. (2025) · npj Viruses · doi:10.1038/s44298-025-00102-3 · Cited by 3 · see citing works
Hailemariam, D., Goldansaz, S. A., Daude, N., Wishart, D. S., & Ametaj, B. N. (2021) · Veterinary Sciences · doi:10.3390/vetsci8090200 · Cited by 3 · see citing works
Aguzzi, A. (2010) · Wiley eBooks · doi:10.1002/9780470688618.taw0267 · Cited by 3 · see citing works
Self-citationOligoadenylate synthetase 1a suppresses prion infection through binding to cellular prion protein
Homma, T., Nakagaki, T., Nishinakagawa, T., Morita, Y., Atarashi, R., Kakuta, S., Iwakura, Y., Nishida, N., & Ishibashi, D. (2025) · Brain · doi:10.1093/brain/awaf193 · Cited by 2 · see citing works
Toll-like Receptors (TLRs) And Prion Disease: Relevance To Pathology And Novel Therapy
Ofodile, O. (2011) · Cited by 2 · see citing works
Protective Role of the Host Innate Immune System in Prion Pathogenesis
Ishibashi, D. (2019) · YAKUGAKU ZASSHI · doi:10.1248/yakushi.18-00165-2 · Cited by 2 · see citing works
Introduction to Prion Disorders
Aguzzi, A., & Kana, V. (2011) · doi:10.1002/9781444341256.ch31 · Cited by 1 · see citing works
Self-citationThe in vitro characterisation of prion diseases of sheep
Taema, M. M. (2012) · Nottingham ePrints (University of Nottingham)
Aguzzi, A. (2007) · Blue books of neurology · doi:10.1016/s1877-184x(09)70061-9
Self-citationChapter 7 A Neuropathologist's Diary
Aguzzi, A. (2007) · Comprehensive biochemistry · doi:10.1016/s0069-8032(07)45007-0
Self-citationImmunogenicity and immune function of the cellular prion protein.
Isaacs, J. D. (2007) · UCL Discovery (University College London)
The immune component of brain disease
Aguzzi, A. (2004) · Current Opinion in Immunology · doi:10.1016/j.coi.2004.07.019
Self-citationWilliams, R. O. (2006) · Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature · doi:10.3410/f.1031825.367942
Prion diseases of mammals: epidemiology, genetics, and pathogenesis
Aguzzi, A. (2006) · RENDICONTI LINCEI · doi:10.1007/bf02904771
Self-citationMaladies à prions : vers le développement d'une thérapie génique et cellulaire
Souder, C. L. (2017) · theses.fr (ABES) · doi:10.70675/2b878862z67daz4e3azab26z026e8344ce30
Interferon-Stimulated Gene-Mediated Defense Against Prion Infection: Noncanonical Function of Oas1a
Homma, T., & Ishibashi, D. (2026) · Viruses · doi:10.3390/v18090955
Sakurada, N., Watanabe, A., Yoshimura, M., Sakae, N., Arahata, H., Yamamoto, A., Kanemaru, T., Noguchi, H., Mori, S., Shijo, M., et al. (2026) · Journal of Neuropathology & Experimental Neurology · doi:10.1093/jnen/nlag099
- Authors
- Prinz, M., Heikenwalder, M., Schwarz, P., Takeda, K., Akira, S., & Aguzzi, A.
- Affiliations
- University Hospital Zurich (CH)
- Research Institute for Microbial Diseases, The University of Osaka (JP)
- Corresponding author
- Aguzzi, Adriano
- Venue
- The EMBO Reports
- Published
- 2003-02-01
- Volume
- 4
- Issue
- 2
- Pages
- 195-199
- ISSN
- 1469-221X (ISSN-L)
- 1469-3178
- PMC
- PMC1315829
- OpenAlex
- W2055789745
- Cited by
- 85
- References
- 30
- Citations by year
- 2026: 2 · 2025: 3 · 2024: 1 · 2023: 1 · 2022: 4 · 2021: 2 · 2020: 2 · 2019: 3 · 2018: 2 · 2017: 3 · 2016: 2 · 2015: 2 · 2014: 5 · 2013: 3 · 2012: 10
- FWCI
- 2.87
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- EMBO Reports (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Zurich Open Repository and Archive (University of Zurich) (acceptedVersion, other-oa)
- Zurich Open Repository and Archive (University of Zurich) (submittedVersion, other-oa)
- Zurich Open Repository and Archive (University of Zurich)
- Funders
- Deutsche Forschungsgemeinschaft
- Universität Zürich
- Office Fédéral de l'Education et de la Science
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Prion Diseases and Protein Misfolding
- Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
- Life Sciences › Immunology and Microbiology › Immunology › Immune Response and Inflammation
- Keywords
- prion pathogenesis, Toll-like receptors, MyD88-deficient mice, scrapie, TLR9, CpG oligodeoxynucleotides, prion susceptibility
- MeSH terms
- Animals, Antigens, Differentiation, Brain, Membrane Glycoproteins, Prions, Receptors, Cell Surface, Receptors, Immunologic, Scrapie, Spleen, Signal Transduction, PrPSc Proteins, Dendritic Cells, Follicular, Adaptor Proteins, Signal Transducing, Toll-Like Receptors, Mice, Myeloid Differentiation Factor 88
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