4.5 Article

PrP interactions with nucleic acids and glycosaminoglycans in function and disease

Journal

FRONTIERS IN BIOSCIENCE-LANDMARK
Volume 15, Issue -, Pages 132-150

Publisher

FRONTIERS IN BIOSCIENCE INC
DOI: 10.2741/3611

Keywords

Prion protein; Aggregation; Encephalopathy; DNA; RNA; Glycosaminoglycan; Review

Funding

  1. Conselho Nacional de Desenvolvimento Cientifico e Tecnologico (CNPq)
  2. Millenium Institute for Structural Biology in Biomedicine and Biotechnology
  3. Instituto Nacional de Ciencia e Tecnologia de Biologia Estrutural e Bioimagem

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Since the first description of prion diseases, great effort has been made toward comprehending this new paradigm in biology. Despite large advances in the field, many questions remain unanswered, especially concerning the conversion of PrPC into PrPSc. How this conformational transition evolves is a crucial problem that must be solved in order to attain further progress in therapeutics and prevention. Recent developments have indicated the requirement for partners of the prion protein in triggering the conversion. In the present review, we will explore the interaction of PrP with some of its most intriguing partners, such as sulfated glycans and nucleic acids. These molecules seem to play a dual role in prion biology and could be fundamental to explaining how prion diseases arise, as well as in the development of effective therapeutic approaches.

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