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Identification of a Tetanus Toxin Specific Epitope in Single Amino Acid Resolution
Author(s) -
Palermo Andrea,
Weber Laura K.,
Rentschler Simone,
Isse Awale,
Sedlmayr Martyna,
Herbster Karin,
List Volker,
Hubbuch Jürgen,
Löffler Felix F.,
NesterovMüller Alexander,
Breitling Frank
Publication year - 2017
Publication title -
biotechnology journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.144
H-Index - 84
eISSN - 1860-7314
pISSN - 1860-6768
DOI - 10.1002/biot.201700197
Subject(s) - epitope , antibody , antigen , immune system , biology , epitope mapping , immunogenicity , toxin , peptide , linear epitope , virology , computational biology , immunology , microbiology and biotechnology , biochemistry
Vaccinations are among the most potent tools to fight infectious diseases. However, cross‐reactions are an ongoing problem and there is an urgent need to fully understand the mechanisms of the immune response. For the development of a methodological workflow, the linear epitopes in the immune response to the tetanus toxin is investigated in sera of 19 vaccinated Europeans applying epitope mapping with peptide arrays. The most prominent epitope, appearing in nine different sera ( 923 IHLVNNESSEVIVHK 937 ), is investigated in a substitution analysis to identify the amino acids that are crucial for the binding of the corresponding antibody species − the antibody fingerprint. The antibody fingerprints of different individuals are compared and found to be strongly conserved ( 929 ExxEVIVxK 937 ), which is astonishing considering the randomness of their development. Additionally, the corresponding antibody species is isolated from one serum with batch chromatography using the amino acid sequence of the identified epitope and the tetanus specificity of the isolated antibody is verified by ELISA. Studying antibody fingerprints with peptide arrays should be transferable to any kind of humoral immune response toward protein antigens. Furthermore, antibody fingerprints have shown to be highly disease‐specific and, therefore, can be employed as reliable biomarkers enabling the study of cross‐reacting antigens.