Transmissible spongiform encephalopathies (TSEs) are a group of fatal neurodegenerative diseases that include bovine spongiform encephalopathy (BSE), scrapie in sheep, and Creutzfeldt–Jakob disease (CJD) in humans. In TSEs the normal cellular prion protein (PrPC) is transformed into an infectious disease-associated isoform, PrPSc — a potential target for immunotherapy. In the March 6 Nature, Anthony R. White and colleagues at Imperial College, London, UK, show that specific anti-PrP monoclonal antibodies can inhibit prion replication and delay the development of prion disease in vivo (Nature 422, 80-83, March 6, 2003).

White et al. injected anti-PrP monoclonal antibodies with high affinity for both murine PrPC and PrPSc into individual mice from a scrapie model strain. They observed that peripheral PrPSc levels and prion infectivity were markedly reduced, even when the antibodies were first administered at the point of near maximal accumulation of PrPSc...

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