Epitope-specific anti-PrP antibody toxicity: a comparative in-silico study of human and mouse prion proteins.

ABSTRACT: Despite having therapeutic potential, anti-PrP antibodies caused a major controversy due to their neurotoxic effects. For instance, treating mice with ICSM antibodies delayed prion disease onset, but both were found to be either toxic or innocuous to neurons by researchers following cross-linking PrP^C. In order to elucidate and understand the reasons that led to these contradictory outcomes, we conducted a comprehensive in silico study to assess the antibody-specific toxicity. Since most therapeutic anti-PrP antibodies were generated against human truncated recombinant PrP^91-231 or full-length mouse PrP^23-231, we reasoned that host specificity (human vs murine) of PrP^C might influence the nature of the specific epitopes recognized by these

SUBMITTER: Adhikari UK 

PROVIDER: S-EPMC8900626 | biostudies-literature | 2021 Dec

REPOSITORIES: biostudies-literature