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Induction of antibodies against murine full-length prion protein in wild-type mice
Michael F Koller1, Thomas Grau, Philipp Christen
1Biochemisches Institut, Universität Zürich, Winterthurerstrasse 190, CH-8057 Zürich, Switzerland.
Abstract:
The causative and infectious agent of the transmissible spongiform encephalopathies, e.g. bovine spongiform encephalopathy in cattle or variant Creutzfeldt-Jakob disease in humans, is a pathogenic form of the scrapie prion protein (PrP(Sc)) generated by a conformational rearrangement in the normal cellular prion protein (PrP(C)). Anti-PrP antibodies have been shown to exert a protective effect against infection with PrP(Sc). However, the generation of anti-PrP antibodies has proven quite difficult in wild-type animals, PrP being a notoriously poor immunogen. We developed a vaccine against PrP by mixing recombinant murine PrP 23-231 with DnaK, an Hsp70 homolog in Escherichia coli, and cross-linking the two proteins by means of glutaraldehyde. After three injections of the vaccine into BALB/c mice at 6, 8 and 9 weeks of age, a low-titer immune response was detected with ELISA in all animals. The specificity of the antibodies for PrP was confirmed with Western blotting. The straightforward procedure might render active immunization against prion infection feasible.
Insights
Developing a novel vaccine using recombinant prion protein (PrP) and DnaK successfully elicited an immune response in mice. This breakthrough offers a potential strategy for active immunization against prion diseases.
Area of Science:
- Neuroscience
- Immunology
- Biochemistry
Background:
- Transmissible spongiform encephalopathies (TSEs) are caused by pathogenic prion protein (PrPSc).
- Normal cellular prion protein (PrPC) misfolds into PrPSc.
- Anti-PrP antibodies show protective effects, but generating them is challenging due to PrP's poor immunogenicity.
Purpose of the Study:
- To develop a feasible vaccine for active immunization against prion infections.
Main Methods:
- Recombinant murine PrP (23-231) was mixed with E. coli's DnaK (an Hsp70 homolog).
- The mixture was cross-linked using glutaraldehyde to create the vaccine.
- BALB/c mice were vaccinated at 6, 8, and 9 weeks of age.
Main Results:
- ELISA detected a low-titer immune response in all vaccinated animals.
- Western blotting confirmed the specificity of the generated antibodies for PrP.
- The procedure was straightforward and potentially applicable for active immunization.
Conclusions:
- A novel vaccine combining recombinant PrP and DnaK successfully induced an anti-PrP immune response in mice.
- This method presents a promising approach for active immunization against prion diseases.
- Further research may lead to effective strategies for preventing and treating TSEs.
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