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Structurally Derived Mutations Define Congenital Heart Block-Related Epitopes Within the 200-239 Amino Acid Stretch of the Ro52 Protein

Title data

Ottosson, Lars ; Salomonsson, S. ; Hennig, Janosch ; Sonesson, S.-E. ; Dörner, T. ; Raats, J. ; Kuchroo, V. K. ; Sunnerhagen, M. ; Wahren-Herlenius, M.:
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. Vol. 61 (2005) Issue 2 . - pp. 109-118.
ISSN 1365-3083
DOI: https://doi.org/10.1111/j.0300-9475.2005.01542.x

Abstract in another language

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.

Further data

Item Type: Article in a journal
Refereed: Yes
Institutions of the University: Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry > Chair Biochemistry with an Emphasis on Biophysical Chemistry > Chair Biochemistry with an Emphasis on Biophysical Chemistry - Univ.-Prof. Dr. Janosch Hennig
Faculties
Faculties > Faculty of Biology, Chemistry and Earth Sciences
Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry
Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry > Chair Biochemistry with an Emphasis on Biophysical Chemistry
Result of work at the UBT: No
DDC Subjects: 500 Science > 540 Chemistry
500 Science > 570 Life sciences, biology
Date Deposited: 08 Oct 2021 09:42
Last Modified: 04 Apr 2022 09:38
URI: https://eref.uni-bayreuth.de/id/eprint/67260