Identification and characterization of a B-cell determinant within the amphipathic domain (residues 178-238) of the myelin proteolipid protein

摘要: Pooled polyclonal rabbit anti-rat myelin and mouse anti-human proteolipid protein (PLP) antisera were screened against a panel of PLP synthetic peptides spanning residues 178–238 the protein. Cross-reactivity one determinant defined by PLP200–219 was particularly prominent in both anti-myelin anti-PLP chosen for further study. Competitive inhibition studies, utilizing overlapping peptides, demonstrated that C-terminal portion PLP200–219, specifically comprising PLP209–217, important antibody recognition this region. Immunohistochemical analyses with an affinity-purified anti-PLP200–219 antiserum cross-reactivity paraffin- gelatin-embedded brain sections immunocytochemical staining oligodendrocyte-enriched cultures binding native situ. Staining living non-permeabilized cells localized to extracellular face membrane. Collectively, these data argue presence immunodominant B-cell 200–219. Furthermore, structural conformation can be mimicked peptide, resulting generation reagent has considerable utility immunohistochemical investigations expression localization within central nervous system © 1996 Wiley-Liss, Inc.