Titelangaben
Ottosson, Lars ; Salomonsson, S. ; Hennig, Janosch ; Sonesson, S.-E. ; Dörner, T. ; Raats, J. ; Kuchroo, V. K. ; Sunnerhagen, Maria ; Wahren-Herlenius, Marie:
Structurally Derived Mutations Define Congenital Heart Block-Related Epitopes Within the 200-239 Amino Acid Stretch of the Ro52 Protein.
In: Scandinavian Journal of Immunology.
Bd. 61
(2005)
Heft 2
.
- S. 109-118.
ISSN 1365-3083
DOI: https://doi.org/10.1111/j.0300-9475.2005.01542.x
Abstract
Congenital heart block is a passively transferred autoimmune condition, which affects the children of mothers with Ro/SSA autoantibodies. During pregnancy, the antibodies are transported across the placenta and affect the fetus. We have previously demonstrated that antibodies directed to the 200–239 amino acid (aa) stretch of the Ro52 component of the Ro/SSA antigen correlate with the development of congenital heart block. In this report, we investigated the antibody–antigen interaction of this target epitope in detail at a molecular and structural level. Peptides representing aa 200–239 (p200) with structurally derived mutations were synthesized to define the epitopes recognized by two Ro52 human monoclonal antibodies, S3A8 and M4H1, isolated from patient-derived phage display libraries. Analyses by ELISA, circular dichroism and MALDI-TOF-MS demonstrate that the antibody recognition is dependent on a partly α-helical fold within the putative leucine zipper of the 200–239 aa stretch and that the two human anti-p200 monoclonal antibodies, M4H1 and S3A8, recognize different epitopic structures within the p200 peptide. In addition, we investigated the representation of each fine specificity within the sera of mothers with children born with congenital heart block, and in such sera, antibodies of the S3A8 idiotype were more commonly detected and at higher levels than M4H1-like antibodies.
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Publikationsform: | Artikel in einer Zeitschrift |
---|---|
Begutachteter Beitrag: | Ja |
Institutionen der Universität: | Fakultäten > Fakultät für Biologie, Chemie und Geowissenschaften > Fachgruppe Chemie > Lehrstuhl Biochemie mit Schwerpunkt Biophysikalische Chemie > Lehrstuhl Biochemie mit Schwerpunkt Biophysikalische Chemie - Univ.-Prof. Dr. Janosch Hennig Fakultäten Fakultäten > Fakultät für Biologie, Chemie und Geowissenschaften Fakultäten > Fakultät für Biologie, Chemie und Geowissenschaften > Fachgruppe Chemie Fakultäten > Fakultät für Biologie, Chemie und Geowissenschaften > Fachgruppe Chemie > Lehrstuhl Biochemie mit Schwerpunkt Biophysikalische Chemie |
Titel an der UBT entstanden: | Nein |
Themengebiete aus DDC: | 500 Naturwissenschaften und Mathematik > 540 Chemie 500 Naturwissenschaften und Mathematik > 570 Biowissenschaften; Biologie |
Eingestellt am: | 08 Okt 2021 09:42 |
Letzte Änderung: | 10 Aug 2022 13:09 |
URI: | https://eref.uni-bayreuth.de/id/eprint/67260 |