Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
4336445 | Journal of Neuroscience Methods | 2007 | 8 Pages |
Abstract
These and other observations have led to the commonly accepted notion that the 3F4 epitope consists of the tetra-peptide Met-Lys-His-Met. In this study, we have identified the minimal epitope for 3F4 by studying its binding to synthetic peptides and by analysis of mutated ovine PrP::GFP constructs expressed in cell culture. We have found that the 3F4 epitope consists of a hepta-peptide (Lys-Thr-Asn-Met-Lys-His-Met), which in sheep encompass residues 109-115. We found that Lys 109 is critically important for 3F4 binding, as omission, or substitution of this residue to Ala resulted in no binding. We also demonstrate that the hepta-peptide constituting the minimal 3F4 epitope, can be used as a discrete, moveable high-affinity molecular tag. Thus, the 3F4 antibody can find its use beyond prion research.
Related Topics
Life Sciences
Neuroscience
Neuroscience (General)
Authors
Christoffer Lund, Christel Moræus Olsen, Heidi Tveit, Michael A. Tranulis,