Characterization of conformation-dependent prion protein epitopes

Hae Eun Kang, Chu Chun Weng, Eri Saijo, Vicki Saylor, Jifeng Bian, Sehun Kim, Laylaa Ramos, Rachel Angers, Katie Langenfeld, Vadim Khaychuk, Carla Calvi, Jason Bartz, Nora Hunter, Glenn C. Telling

Research output: Contribution to journalArticle

23 Scopus citations


Background: Despite structural reorganization during disease, conformational prion protein epitopes remain undefined. Results: We identify specific amino acids constituting novel conformational monoclonal antibody epitopes. Conclusion: Immunoreactivities of globular domain epitopes depend on maintenance of regional tertiary structure. Significance: Our studies address how denatured conformational epitopes remain functional, provide insights into normal and disease-related prion protein, and expand epitope tagging options.

Original languageEnglish (US)
Pages (from-to)37219-37232
Number of pages14
JournalJournal of Biological Chemistry
Issue number44
StatePublished - Oct 26 2012


All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Cite this

Kang, H. E., Weng, C. C., Saijo, E., Saylor, V., Bian, J., Kim, S., Ramos, L., Angers, R., Langenfeld, K., Khaychuk, V., Calvi, C., Bartz, J., Hunter, N., & Telling, G. C. (2012). Characterization of conformation-dependent prion protein epitopes. Journal of Biological Chemistry, 287(44), 37219-37232.