Identification of an epitope on the recombinant bovine PrP that is able to elicit a prominent immune response in wild-type mice

Černilec, Maja; Vranac, Tanja; Hafner-Bratkovič, Iva; Koren, Simon; Venturini, Anja Colja; Popović, Mara; Juntes, Polona; Šerbec, Vladka Čurin

doi:10.1016/j.imlet.2007.07.012

Cited by 8 publications

(4 citation statements)

References 48 publications

(68 reference statements)

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“…In the positive selection step, only hybridoma lines that reacted with Fab V5B2 in ELISA were selected for further characterization, whereas in the following negative selection step, only cell lines that did not bind to any of the negative selection proteins (the monoclonal antibodies and Fab fragments listed in Table 1 ) were chosen. In particular, the first protein used for negative selection was the Fab fragment from the E12/2 anti-recombinant bovine prion protein monoclonal antibody [ 26 ], which has a different epitope specificity but is of the same isotype as V5B2. This served to eliminate hypothetical isotype-specific antibodies that recognize the CH 1 domain, the first constant domain, in addition to the variable domain that was also present in the Fab fragment.…”

Section: Resultsmentioning

confidence: 99%

Anti-idiotypic antibodies: a new approach in prion research

et al. 2009

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Background: In certain cases, anti-idiotypic antibodies that recognize an antigen-combining site of an antibody can mimic the structure and/or function of certain nominal antigens. This feature makes them particularly useful if conventional experimental approaches fail to fulfil expectations, especially when the molecule of interest is infectious, toxic or difficult to isolate and purify. We suggest the application of an anti-idiotype concept to the field of prion biology, with the aim of evoking a humoral immune response against the pathological isoform of the prion protein (PrP Sc ). Different ways to induce anti-idiotypic responses were studied in mice and chickens using various forms of V5B2, a PrP Sc -specific monoclonal antibody we have described previously.

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Section: Resultsmentioning

confidence: 99%

Anti-idiotypic antibodies: a new approach in prion research

et al. 2009

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“…Its epitope was located at C-terminal end of helix 1 of human PrP with His155 being crucial for binding. 23 Microtiter plate was coated with mAb V5B2 (5 μg ml −1 ). Prepared samples were loaded and incubated for 90 min.…”

Section: Methodsmentioning

confidence: 99%

Regional distribution of anchorless prion protein, PrP226*, in the human brain

Lukan

Černilec

Vranac

et al. 2014

Prion

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It was shown previously that truncated molecules of prion protein can be found in brains of patients with some types of transmissible spongiform encephalopathy. One such molecule, PrP226*, is a fragment of prion protein, truncated at Tyr226. It was found to be present in aggregates, from which it can be released using chaotropic salts. In this study we investigated the distribution of PrP226* in Creutzfeldt–Jakob disease affected human brain, employing the mAb V5B2, specifically recognizing this fragment. The results show that PrP226* is not evenly distributed among different regions of human brain. Among brain regions analyzed, the fragment was found most likely to be accumulated in the cerebellum. Its distribution correlates with the distribution of PrPSc.

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“…Prion strains differ in many aspects: by their biochemical profiles and characteristics, like differences in band pattern in electrophoresis, resistance to proteinase-K digestion and altered amino-terminal proteinase-K cleavage sites, also resulting in different antibody binding patterns. Additionally, they differ regarding their efficiency of transmission, differences in species barrier, the length of incubation time, pattern and intensity of brain lesions and clinical symptoms, different immune response, and stability (Solforosi et al, 2013;Šnajder et al, 2012;Hamir et al, 2011;Černilec et al, 2007;Telling, 2004). In sheep, for instance, we recognise at least ten ovine scrapie strains (Moore et al, 2016;Benestad et al, 2008;Morales et al, 2007;Bossers et al, 2000).…”

Section: Prion Strains and Transmissibilitymentioning

confidence: 99%

Prions and animal transmissible spongiform encephalopathies

2017

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Background. Transmissible spongiform encephalopathies (TSEs) or prion diseases are a unique group of neurodegenerative diseases of animals and humans, which always have a fatal outcome and are transmissible among animals of the same or different species. Scope and Approach. The aim of this work is to review some recent data about animal TSEs, with the emphasis on their causative agents and zoonotic potential, and to discuss why the surveillance and control measures over animal TSEs should remain in force. Key Findings and Conclusions. We still have incomplete knowledge of prions and prion diseases. Scrapie has been present for a very long time and controlled with varied success. Bovine spongiform encephalopathy (BSE) emerged unnoticed, and spread within a few years to epidemic proportions, entailing enormous economic consequences and public concerns. Currently, the classical BSE epidemic is under control, but atypical cases do, and probably will, persist in bovine populations. The Chronic Wasting Disease (CWD) of the cervids has been spreading in North America and has recently been detected in Europe. Preventive measures for the control of classical BSE remain in force, including the feed ban and removal of specified risk materials. However, active BSE surveillance has considerably decreased. In the absence of such preventive and control measures, atypical BSE cases in healthy slaughtered bovines might persist in the human food chain, and BSE prions might resurface. Moreover, other prion strains might emerge and spread undetected if the appropriate preventive and surveillance measures were to cease, leaving behind inestimable consequences.

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Identification of an epitope on the recombinant bovine PrP that is able to elicit a prominent immune response in wild-type mice

Cited by 8 publications

References 48 publications

Anti-idiotypic antibodies: a new approach in prion research

Anti-idiotypic antibodies: a new approach in prion research

Regional distribution of anchorless prion protein, PrP226*, in the human brain

Prions and animal transmissible spongiform encephalopathies

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