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Antigenic mimicry-mediated anti-prion effects induced by bacterial enzyme succinylarginine dihydrolase in mice
Daisuke Ishibashi1, Hitoki Yamanaka, Tsuyoshi Mori
1Department of Molecular Microbiology and Immunology, Nagasaki University Graduate School of Biomedical Sciences, 1-12-4 Sakamoto, Nagasaki 852-8523, Japan.
Abstract:
Prions, the causative agents of prion diseases, are immunologically tolerated because their major component, prion protein (PrP), is a host-encoded molecule. Therefore, no effective prion vaccines have been developed. We previously showed that heterologous bovine and sheep PrP immunizations of mice overcame tolerance by an antigenic mimicry mechanism to efficiently induce anti-PrP auto-antibodies (Abs), significantly prolonging incubation times in mice subsequently infected with the mouse-adapted Fukuoka-1 prion. These results prompted us to investigate if non-mammal derived molecules able to antigenically mimic anti-prion epitopes, could act as prion vaccines. We show here that immunization of mice with recombinant succinylarginine dihydrolase, a bacterial enzyme with a peptide sequence similar to an anti-prion epitope, induced anti-PrP auto-Abs with anti-prion activity and significantly retarded survival times of the mice subsequently infected with Fukuoka-1 prions. These results might open a way for development of a new type of antigenic mimicry-based prion vaccine.
Insights
Developing a novel prion vaccine using antigenic mimicry. Researchers induced anti-prion auto-antibodies in mice with a bacterial enzyme, showing potential for a new class of prion disease vaccines.
Area of Science:
- Immunology
- Neuroscience
- Biochemistry
Background:
- Prion diseases are fatal neurodegenerative disorders caused by prions.
- Prions are poorly immunogenic due to host prion protein (PrP) tolerance, hindering vaccine development.
- Previous studies demonstrated successful prion vaccination via heterologous PrP immunization using antigenic mimicry.
Purpose of the Study:
- To investigate the potential of non-mammal derived molecules as prion vaccines.
- To explore if antigenic mimicry using bacterial enzymes can induce anti-prion activity.
- To assess the efficacy of a bacterial enzyme-based approach in a mouse model of prion disease.
Main Methods:
- Immunization of mice with recombinant succinylarginine dihydrolase, a bacterial enzyme.
- Induction of auto-antibodies against prion protein (PrP).
- Infection of immunized mice with mouse-adapted Fukuoka-1 prions to evaluate survival rates.
Main Results:
- Recombinant succinylarginine dihydrolase successfully induced anti-PrP auto-antibodies with prion-neutralizing activity.
- Immunization significantly retarded survival times in mice infected with Fukuoka-1 prions.
- The bacterial enzyme demonstrated antigenic mimicry of anti-prion epitopes.
Conclusions:
- Non-mammal derived molecules can be utilized for prion vaccine development through antigenic mimicry.
- Succinylarginine dihydrolase shows promise as a component of a novel, broadly applicable prion vaccine.
- This approach may overcome immunological tolerance and lead to effective prion disease prevention strategies.
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