Expression and functions of cellular prion proteins in immunocytes

Abstract

Prion diseases are fatal neurodegenerative processes caused by the accumulation of the pathological prion protein, PrPSc. While pathological lesions are limited to the central nervous system (CNS), disease‐specific proteins accumulate and replicate in secondary lymphoid organs prior to neuroinvasion, and their replication there depends on the abundance of cellular prion protein (PrPC). PrPC is expressed in both central and peripheral lymphoid tissues, and up‐ or downregulates innate and adaptive immune responses. In addition to prion diseases, PrPC is also immunologically involved in other neurological disorders and infectious diseases, including Alzheimer's disease and human immunodeficiency virus infection. Herein, we summarize the expression and functions of PrPC in various immunocytes, as well as its immunological and pathological roles in neurodegeneration and infection.

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

“…All the linear epitopes with protrusion index (PI) scores are shown in Table 2. Four epitopes, L2 (89-111), L7 (24-49), L9 (56-66) and L10 (76)(77)(78)(79)(80)(81)(82)(83)(84)(85)(86) are located in the FT region of which L9 (56-66) and L10 (76)(77)(78)(79)(80)(81)(82)(83)(84)(85)(86) are within the OR region. The GD region revealed three epitopes, L3 (167-174), L4 (137-153) and L6 (189-204).…”

“…It is believed that cellular prion protein PrP C is widely expressed in the immune system and is naturally immune tolerated and no antibodies are released against this protein [86][87][88]. In addition, PrP C has important effects on the B-cell repertoire and antibody production [86].…”

“…It is believed that cellular prion protein PrP C is widely expressed in the immune system and is naturally immune tolerated and no antibodies are released against this protein [86][87][88]. In addition, PrP C has important effects on the B-cell repertoire and antibody production [86]. A recent report by Senatore and colleagues described the characterization of novel ant-PrP antibodies identified with a synthetic human Fab phage display library [89].…”

Prion Protein in Stem Cells: A Lipid Raft Component Involved in the Cellular Differentiation Process

“…In humans, PrP C is encoded by the PRNP gene, and the protein consists of approximately 250 amino acid residues and a highly conserved membrane-bound glycoprotein anchored by glycosylphosphatidylinositol (GPI) [11].…”

“…Researchers focused on understanding the physiological role of the PrP C [11]. In fact, since its discovery, many functions have been attributed to PrP C , such as the copper-binding ability in brain membrane fractions, which controls the activity of other membrane-associated copper-binding proteins and enhances copper incorporation into superoxide dismutase (SOD) [28,29].…”