Major prion protein (PrP) (PrP)

The Major prion protein (PrP), encoded by the PRNP gene, is a glycosylphosphatidylinositol (GPI)-anchored glycoprotein primarily expressed on the surface of neurons in the central nervous system [1]. While its exact physiological function is still being elucidated, it is known to play roles in copper homeostasis, neuroprotection, and synaptic signaling [1, 2]. PrP is the central component in the pathogenesis of transmissible spongiform encephalopathies (TSEs), such as Creutzfeldt-Jakob disease, where the normal cellular form (PrPC) undergoes a conformational change into a misfolded, protease-resistant isoform (PrPSc) [2, 3]. This misfolded protein acts as a template for further conversion, leading to toxic aggregation and severe neurodegeneration [3]. Therapeutic strategies, including the use of monoclonal antibodies like cHJ7, aim to stabilize PrPC or block the interaction between PrPC and PrPSc to halt disease progression [4]. Research into cHJ7 specifically focuses on its ability to bind the 117–125 region of the protein to inhibit prion replication without inducing the neurotoxicity seen with some other anti-PrP antibodies [4, 5].

Other names

PrPCPrPScCD230PRNPPrion-related protein

Binding to the cellular prion protein (PrPC) to stabilize its structure and prevent its conversion into the pathogenic, misfolded scrapie isoform (PrPSc), or by blocking the binding sites required for PrPSc-mediated recruitment and aggregation.