Epitope mapping of monoclonal antibodies to calreticulin reveals that charged amino acids are essential for antibody binding

Ann Christina Bergmann, Cecilie Kyllesbech, Rimantas Slibinskas, Evaldas Ciplys, Peter Højrup, Nicole Hartwig Trier*, Gunnar Houen

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Abstrakt

Calreticulin is a chaperone protein, which is associated with myeloproliferative diseases. In this study, we used resin-bound peptides to characterize two monoclonal antibodies (mAbs) directed to calreticulin, mAb FMC 75 and mAb 16, which both have significantly contributed to understanding the biological function of calreticulin. The antigenicity of the resin-bound peptides was determined by modified enzyme-linked immunosorbent assay. Specific binding was determined to an 8-mer epitope located in the N-terminal (amino acids 34–41) and to a 12-mer peptide located in the C-terminal (amino acids 362–373). Using truncated peptides, the epitopes were identified as TSRWIESK and DEEQRLKEEED for mAb FMC 75 and mAb 16, respectively, where, especially the charged amino acids, were found to have a central role for a stable binding. Further studies indicated that the epitope of mAb FMC 75 is assessable in the oligomeric structure of calreticulin, making this epitope a potential therapeutic target.

OriginalsprogEngelsk
Artikelnummer31
TidsskriftAntibodies
Vol/bind10
Udgave nummer3
Antal sider13
ISSN2073-4468
DOI
StatusUdgivet - 2021

Bibliografisk note

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© 2021 by the authors. Licensee MDPI, Basel, Switzerland.

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