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 C. Bartz, Nora Hunter, Glenn C. Telling

Research output: Contribution to journal › Article

23 Citations (Scopus)

Abstract

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
Pages (from-to)37219-37232
Number of pages14
JournalJournal of Biological Chemistry
Volume287
Issue number44
DOIs
StatePublished - Oct 26 2012

Fingerprint

Conformations
Epitopes
Prion Diseases
Monoclonal Antibodies
Maintenance
Prions
Prion Proteins
Amino Acids

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Cell Biology
  • Molecular Biology

Cite this

Kang, H. E., Weng, C. C., Saijo, E., Saylor, V., Bian, J., Kim, S., ... Telling, G. C. (2012). Characterization of conformation-dependent prion protein epitopes. Journal of Biological Chemistry, 287(44), 37219-37232. https://doi.org/10.1074/jbc.M112.395921

Characterization of conformation-dependent prion protein epitopes. / Kang, Hae Eun; Weng, Chu Chun; Saijo, Eri; Saylor, Vicki; Bian, Jifeng; Kim, Sehun; Ramos, Laylaa; Angers, Rachel; Langenfeld, Katie; Khaychuk, Vadim; Calvi, Carla; Bartz, Jason C.; Hunter, Nora; Telling, Glenn C.

In: Journal of Biological Chemistry, Vol. 287, No. 44, 26.10.2012, p. 37219-37232.

Research output: Contribution to journal › Article

Kang, HE, Weng, CC, Saijo, E, Saylor, V, Bian, J, Kim, S, Ramos, L, Angers, R, Langenfeld, K, Khaychuk, V, Calvi, C, Bartz, JC, Hunter, N & Telling, GC 2012, 'Characterization of conformation-dependent prion protein epitopes', Journal of Biological Chemistry, vol. 287, no. 44, pp. 37219-37232. https://doi.org/10.1074/jbc.M112.395921
Kang HE, Weng CC, Saijo E, Saylor V, Bian J, Kim S et al. Characterization of conformation-dependent prion protein epitopes. Journal of Biological Chemistry. 2012 Oct 26;287(44):37219-37232. https://doi.org/10.1074/jbc.M112.395921
Kang, Hae Eun ; Weng, Chu Chun ; Saijo, Eri ; Saylor, Vicki ; Bian, Jifeng ; Kim, Sehun ; Ramos, Laylaa ; Angers, Rachel ; Langenfeld, Katie ; Khaychuk, Vadim ; Calvi, Carla ; Bartz, Jason C. ; Hunter, Nora ; Telling, Glenn C. / Characterization of conformation-dependent prion protein epitopes. In: Journal of Biological Chemistry. 2012 ; Vol. 287, No. 44. pp. 37219-37232.
@article{9ea8bfc156924c6a90ea7a510b1ac17b,
title = "Characterization of conformation-dependent prion protein epitopes",
abstract = "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.",
author = "Kang, {Hae Eun} and Weng, {Chu Chun} and Eri Saijo and Vicki Saylor and Jifeng Bian and Sehun Kim and Laylaa Ramos and Rachel Angers and Katie Langenfeld and Vadim Khaychuk and Carla Calvi and Bartz, {Jason C.} and Nora Hunter and Telling, {Glenn C.}",
year = "2012",
month = "10",
day = "26",
doi = "10.1074/jbc.M112.395921",
language = "English",
volume = "287",
pages = "37219--37232",
journal = "Journal of Biological Chemistry",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology Inc.",
number = "44",

}

TY - JOUR

T1 - Characterization of conformation-dependent prion protein epitopes

AU - Kang, Hae Eun

AU - Weng, Chu Chun

AU - Saijo, Eri

AU - Saylor, Vicki

AU - Bian, Jifeng

AU - Kim, Sehun

AU - Ramos, Laylaa

AU - Angers, Rachel

AU - Langenfeld, Katie

AU - Khaychuk, Vadim

AU - Calvi, Carla

AU - Bartz, Jason C.

AU - Hunter, Nora

AU - Telling, Glenn C.

PY - 2012/10/26

Y1 - 2012/10/26

N2 - 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.

AB - 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.

UR - http://www.scopus.com/inward/record.url?scp=84868253461&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=84868253461&partnerID=8YFLogxK

U2 - 10.1074/jbc.M112.395921

DO - 10.1074/jbc.M112.395921

M3 - Article

VL - 287

SP - 37219

EP - 37232

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 0021-9258

IS - 44

ER -

Access to Document