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

doi:10.1074/jbc.M112.395921

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

Department of Medical Microbiology and Immunology

Research output: Contribution to journal › Article › peer-review

26 Scopus citations

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 language	English (US)
Pages (from-to)	37219-37232
Number of pages	14
Journal	Journal of Biological Chemistry
Volume	287
Issue number	44
DOIs	https://doi.org/10.1074/jbc.M112.395921
State	Published - Oct 26 2012

All Science Journal Classification (ASJC) codes

Biochemistry
Molecular Biology
Cell Biology

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10.1074/jbc.M112.395921

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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 Jason Bartz and Nora Hunter and Telling, {Glenn C.}",

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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

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.

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JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 0021-9258

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ER -

Characterization of conformation-dependent prion protein epitopes

Abstract

All Science Journal Classification (ASJC) codes

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