Investigations into the immunogenicity of the prion protein are ongoing. To combat its pathological isoform without affecting the cellular prion protein is a challenge in prion research. We here summarize the studies in which prion protein peptides have been used for immunization, to thus determine the most immunogenic parts of the prion protein.
COBISS.SI-ID: 25501145
The article describes the production of anti-idiotypic antibodies (Ab2) against mAb V5B2, which selectively recognizes pathological isoform of PrP, PrPSc, in xenogeneic (hen) and syngeneic (BALB/c mice) experimental system. With adequate immunisation procedure following well-planned selection with mAbs, prepared in our laboratory in previous years, we were able not only to show that it was possible to produce Ab2, but also to use this approach in prion research.
COBISS.SI-ID: 2440072
Cross-contamination of the cell lines, which are used in research and in biotechnological processes, represents a huge problem and for this reason, the cell lines must be well defined. The methods, which must be used in the research work as well as in industry to assure a quality measures as well as the accurate and reproducible results, are proposed and described in our paper. Industrial partners have expressed their intent to implement our technology for the characterisation of the cell lines, which are used in their production.
COBISS.SI-ID: 27431385
We humanized a single-chain V5B2 antibody, using variable domain resurfacing approach guided by computer modelling. Design based on sequence alignments and computer modelling resulted in a humanized version bearing 13 mutations compared to initial murine scFv. The humanized scFv was expressed in bacterial system and purified by metal-affinity chromatography. Unaltered binding affinity to the original antigen was demonstrated by ELISA and maintained binding specificity was proven by Western blotting and immunohistochemistry. Described humanized scFv might become a potential therapeutic reagent.
COBISS.SI-ID: 34754053
The article describes epitope mapping of a PrPSc-specific monoclonal antibody, which does not discriminate a conformational change between cellular (PrPC) and pathological (PrPSc) prion protein isoform, as described previously. By using phage display technology and molecular biology methods, a new C-terminally truncated fragment, PrP226, was determined in TSE infected samples.
COBISS.SI-ID: 27952345