ArticleAntibodies (Basel, Switzerland)2021
Epitope Mapping of Monoclonal Antibodies to Calreticulin Reveals That Charged Amino Acids Are Essential for Antibody Binding.
Article in Antibodies (Basel, Switzerland), 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed.
- Bioinformatics-based B-cell epitope identification from Leptospira interrogans outer membrane proteins LIC11574 and LIC13411 for the rational development of a multi-epitope anti-Leptospira vaccine.Archives of microbiology · 2026Article
- Article
- Regulated cell death and DAMPs as biomarkers and therapeutic targets in normothermic perfusion of transplant organs. Part 2: implementation strategies.Frontiers in transplantation · 2025Review
- Sequential Double Immunoblotting with Peptide Antibodies.Methods in molecular biology (Clifton, N.J.) · 2024Article
- Peptide Antibodies: Current Status.Methods in molecular biology (Clifton, N.J.) · 2024Article
- Determination of crucial epitopes in the sperm protein calsperin employing synthetic peptides and monoclonal antibodies.Journal of peptide science : an official publication of the European Peptide Society · 2023Article
- Design, Production, Characterization, and Use of Peptide Antibodies.Antibodies (Basel, Switzerland) · 2023Article
- Production and Characterization of Peptide Antibodies to the C-Terminal of Frameshifted Calreticulin Associated with Myeloproliferative Diseases.International journal of molecular sciences · 2022Article
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Authors and funding
7 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
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.
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Registered trials
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